PAG_BACAN
ID PAG_BACAN Reviewed; 764 AA.
AC P13423; Q937W2; Q937W3; Q9F5R7; Q9KH69; Q9RQU2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Protective antigen {ECO:0000303|PubMed:3148491};
DE Short=PA {ECO:0000303|PubMed:3148491};
DE AltName: Full=Anthrax toxins translocating protein {ECO:0000305};
DE AltName: Full=PA-83 {ECO:0000303|PubMed:8051159};
DE Short=PA83 {ECO:0000303|PubMed:8051159};
DE Contains:
DE RecName: Full=Protective antigen PA-20 {ECO:0000305};
DE Short=PA-20 {ECO:0000303|PubMed:11207581, ECO:0000303|PubMed:8051159};
DE Short=PA20 {ECO:0000303|PubMed:11207581, ECO:0000303|PubMed:8051159};
DE Contains:
DE RecName: Full=Protective antigen PA-63 {ECO:0000305};
DE Short=PA-63 {ECO:0000303|PubMed:11207581, ECO:0000303|PubMed:8051159};
DE Short=PA63 {ECO:0000303|PubMed:11207581, ECO:0000303|PubMed:8051159};
DE Flags: Precursor;
GN Name=pagA; Synonyms=pag;
GN OrderedLocusNames=pXO1-110, BXA0164, GBAA_pXO1_0164;
OS Bacillus anthracis.
OG Plasmid pXO1.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3148491; DOI=10.1016/0378-1119(88)90439-8;
RA Welkos S.L., Lowe J.R., Eden-Mccutchan F., Vodkin M., Leppla S.H.,
RA Schmidt J.J.;
RT "Sequence and analysis of the DNA encoding protective antigen of Bacillus
RT anthracis.";
RL Gene 69:287-300(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=28, 33, BA1024, and BA1035;
RX PubMed=10197996; DOI=10.1128/jb.181.8.2358-2362.1999;
RA Price L.B., Hugh-Jones M., Jackson P.J., Keim P.;
RT "Genetic diversity in the protective antigen gene of Bacillus anthracis.";
RL J. Bacteriol. 181:2358-2362(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=V770-NP1-R / ATCC 14185;
RX PubMed=10899854; DOI=10.1128/iai.68.8.4549-4558.2000;
RA Cohen S., Mendelson I., Altboum Z., Kobiler D., Elhanany E., Bino T.,
RA Leitner M., Inbar I., Rosenberg H., Gozes Y., Barak R., Fisher M.,
RA Kronman C., Velan B., Shafferman A.;
RT "Attenuated nontoxinogenic and nonencapsulated recombinant Bacillus
RT anthracis spore vaccines protect against anthrax.";
RL Infect. Immun. 68:4549-4558(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RX PubMed=10515943; DOI=10.1128/jb.181.20.6509-6515.1999;
RA Okinaka R.T., Cloud K., Hampton O., Hoffmaster A.R., Hill K.K., Keim P.,
RA Koehler T.M., Lamke G., Kumano S., Mahillon J., Manter D., Martinez Y.,
RA Ricke D., Svensson R., Jackson P.J.;
RT "Sequence and organization of pXO1, the large Bacillus anthracis plasmid
RT harboring the anthrax toxin genes.";
RL J. Bacteriol. 181:6509-6515(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ames / isolate Florida / A2012;
RX PubMed=12004073; DOI=10.1126/science.1071837;
RA Read T.D., Salzberg S.L., Pop M., Shumway M.F., Umayam L., Jiang L.,
RA Holtzapple E., Busch J.D., Smith K.L., Schupp J.M., Solomon D., Keim P.,
RA Fraser C.M.;
RT "Comparative genome sequencing for discovery of novel polymorphisms in
RT Bacillus anthracis.";
RL Science 296:2028-2033(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-751.
RC STRAIN=Carbosap, and Ferrara;
RX PubMed=12067380; DOI=10.1046/j.1365-2672.2002.01660.x;
RA Adone R., Pasquali P., La Rosa G., Marianelli C., Muscillo M.,
RA Fasanella A., Francia M., Ciuchini F.;
RT "Sequence analysis of the genes encoding for the major virulence factors of
RT Bacillus anthracis vaccine strain 'Carbosap'.";
RL J. Appl. Microbiol. 93:117-121(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-434.
RC STRAIN=PAI;
RX PubMed=14985634;
RA Inoue S., Noguchi A., Tanabayashi K., Yamada A.;
RT "Preparation of a positive control DNA for molecular diagnosis of Bacillus
RT anthracis.";
RL Jpn. J. Infect. Dis. 57:29-32(2004).
RN [9]
RP FUNCTION, AND DOMAINS.
RX PubMed=1651334; DOI=10.1016/s0021-9258(18)98643-6;
RA Singh Y., Klimpel K.R., Quinn C.P., Chaudhary V.K., Leppla S.H.;
RT "The carboxyl-terminal end of protective antigen is required for receptor
RT binding and anthrax toxin activity.";
RL J. Biol. Chem. 266:15493-15497(1991).
RN [10]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=1644824; DOI=10.1016/s0021-9258(18)42016-9;
RA Molloy S.S., Bresnahan P.A., Leppla S.H., Klimpel K.R., Thomas G.;
RT "Human furin is a calcium-dependent serine endoprotease that recognizes the
RT sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective
RT antigen.";
RL J. Biol. Chem. 267:16396-16402(1992).
RN [11]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=1512256; DOI=10.1016/s0021-9258(18)41911-4;
RA Novak J.M., Stein M.P., Little S.F., Leppla S.H., Friedlander A.M.;
RT "Functional characterization of protease-treated Bacillus anthracis
RT protective antigen.";
RL J. Biol. Chem. 267:17186-17193(1992).
RN [12]
RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF 193-ARG--ARG-196; ARG-193;
RP 194-LYS--ARG-196 AND 194-LYS-LYS-195.
RX PubMed=1438214; DOI=10.1073/pnas.89.21.10277;
RA Klimpel K.R., Molloy S.S., Thomas G., Leppla S.H.;
RT "Anthrax toxin protective antigen is activated by a cell surface protease
RT with the sequence specificity and catalytic properties of furin.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10277-10281(1992).
RN [13]
RP FUNCTION.
RC STRAIN=Weybridge;
RX PubMed=8300513; DOI=10.1128/jb.176.3.586-595.1994;
RA Koehler T.M., Dai Z., Kaufman-Yarbray M.;
RT "Regulation of the Bacillus anthracis protective antigen gene: CO2 and a
RT trans-acting element activate transcription from one of two promoters.";
RL J. Bacteriol. 176:586-595(1994).
RN [14]
RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF PHE-342; 342-PHE-PHE-343; ASP-344
RP AND SER-719.
RC STRAIN=Sterne;
RX PubMed=7961869; DOI=10.1016/s0021-9258(19)62010-7;
RA Singh Y., Klimpel K.R., Arora N., Sharma M., Leppla S.H.;
RT "The chymotrypsin-sensitive site, FFD315, in anthrax toxin protective
RT antigen is required for translocation of lethal factor.";
RL J. Biol. Chem. 269:29039-29046(1994).
RN [15]
RP PROTEOLYTIC CLEAVAGE, AND SUBUNIT.
RC STRAIN=Sterne;
RX PubMed=8051159; DOI=10.1016/s0021-9258(17)32036-7;
RA Milne J.C., Furlong D., Hanna P.C., Wall J.S., Collier R.J.;
RT "Anthrax protective antigen forms oligomers during intoxication of
RT mammalian cells.";
RL J. Biol. Chem. 269:20607-20612(1994).
RN [16]
RP FUNCTION (PROTECTIVE ANTIGEN PA-63), INTERACTION WITH LF (PROTECTIVE
RP ANTIGEN PA-63), SUBUNIT (PROTECTIVE ANTIGEN PA-63), AND SUBCELLULAR
RP LOCATION (PROTECTIVE ANTIGEN PA-63).
RX PubMed=10085027; DOI=10.1128/iai.67.4.1853-1859.1999;
RA Singh Y., Klimpel K.R., Goel S., Swain P.K., Leppla S.H.;
RT "Oligomerization of anthrax toxin protective antigen and binding of lethal
RT factor during endocytic uptake into mammalian cells.";
RL Infect. Immun. 67:1853-1859(1999).
RN [17]
RP DOMAIN.
RC STRAIN=Sterne;
RX PubMed=10085028; DOI=10.1128/iai.67.4.1860-1865.1999;
RA Varughese M., Teixeira A.V., Liu S., Leppla S.H.;
RT "Identification of a receptor-binding region within domain 4 of the
RT protective antigen component of anthrax toxin.";
RL Infect. Immun. 67:1860-1865(1999).
RN [18]
RP PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
RX PubMed=11207581; DOI=10.1046/j.1462-5822.2000.00052.x;
RA Beauregard K.E., Collier R.J., Swanson J.A.;
RT "Proteolytic activation of receptor-bound anthrax protective antigen on
RT macrophages promotes its internalization.";
RL Cell. Microbiol. 2:251-258(2000).
RN [19]
RP MUTAGENESIS OF TRP-375; MET-379 AND LEU-381.
RC STRAIN=Sterne;
RX PubMed=11178978; DOI=10.1006/bbrc.2001.4320;
RA Batra S., Gupta P., Chauhan V., Singh A., Bhatnagar R.;
RT "Trp 346 and Leu 352 residues in protective antigen are required for the
RT expression of anthrax lethal toxin activity.";
RL Biochem. Biophys. Res. Commun. 281:186-192(2001).
RN [20]
RP MUTAGENESIS OF PHE-581; PHE-583; ILE-591; LEU-595 AND ILE-603.
RC STRAIN=Sterne;
RX PubMed=11554763; DOI=10.1006/bbrc.2001.5613;
RA Ahuja N., Kumar P., Bhatnagar R.;
RT "Hydrophobic residues Phe552, Phe554, Ile562, Leu566, and Ile574 are
RT required for oligomerization of anthrax protective antigen.";
RL Biochem. Biophys. Res. Commun. 287:542-549(2001).
RN [21]
RP MUTAGENESIS OF PRO-289.
RC STRAIN=Sterne;
RX PubMed=11356563; DOI=10.1111/j.1574-6968.2001.tb10646.x;
RA Khanna H., Chopra A.P., Arora N., Chaudhry A., Singh Y.;
RT "Role of residues constituting the 2beta1 strand of domain II in the
RT biological activity of anthrax protective antigen.";
RL FEMS Microbiol. Lett. 199:27-31(2001).
RN [22]
RP MUTAGENESIS OF GLN-512; ASP-541; LEU-543 AND ARG-621.
RX PubMed=11222612; DOI=10.1128/jb.183.6.2111-2116.2001;
RA Mogridge J., Mourez M., Collier R.J.;
RT "Involvement of domain 3 in oligomerization by the protective antigen
RT moiety of anthrax toxin.";
RL J. Bacteriol. 183:2111-2116(2001).
RN [23]
RP MUTAGENESIS OF LYS-426; ASP-454 AND PHE-456.
RX PubMed=11113126; DOI=10.1074/jbc.m008309200;
RA Sellman B.R., Nassi S., Collier R.J.;
RT "Point mutations in anthrax protective antigen that block translocation.";
RL J. Biol. Chem. 276:8371-8376(2001).
RN [24]
RP FUNCTION, INTERACTION WITH HOST ANTXR1, AND SUBCELLULAR LOCATION
RP (PROTECTIVE ANTIGEN).
RX PubMed=11700562; DOI=10.1038/n35101999;
RA Bradley K.A., Mogridge J., Mourez M., Collier R.J., Young J.A.T.;
RT "Identification of the cellular receptor for anthrax toxin.";
RL Nature 414:225-229(2001).
RN [25]
RP REVIEW.
RX PubMed=11544370; DOI=10.1146/annurev.micro.55.1.647;
RA Mock M., Fouet A.;
RT "Anthrax.";
RL Annu. Rev. Microbiol. 55:647-671(2001).
RN [26]
RP FUNCTION (PROTECTIVE ANTIGEN PA-63), INTERACTION WITH LF (PROTECTIVE
RP ANTIGEN PA-63), AND MUTAGENESIS OF PRO-213; LEU-216; PHE-231; LEU-232;
RP PRO-234; ILE-236; ILE-239; TRP-255 AND PHE-265.
RC STRAIN=Sterne;
RX PubMed=12117959; DOI=10.1128/iai.70.8.4477-4484.2002;
RA Chauhan V., Bhatnagar R.;
RT "Identification of amino acid residues of anthrax protective antigen
RT involved in binding with lethal factor.";
RL Infect. Immun. 70:4477-4484(2002).
RN [27]
RP SUBCELLULAR LOCATION.
RX PubMed=12606539; DOI=10.1074/jbc.m301244200;
RA Williams R.C., Rees M.L., Jacobs M.F., Pragai Z., Thwaite J.E.,
RA Baillie L.W., Emmerson P.T., Harwood C.R.;
RT "Production of Bacillus anthracis protective antigen is dependent on the
RT extracellular chaperone, PrsA.";
RL J. Biol. Chem. 278:18056-18062(2003).
RN [28]
RP MUTAGENESIS OF ASN-686; LYS-708; LYS-709; TYR-710; ASN-711; ASP-712;
RP LYS-713; LEU-714; PRO-715; LEU-716; TYR-717; ILE-718; ASN-720; PRO-721 AND
RP ASN-722.
RX PubMed=12771151; DOI=10.1074/jbc.m301154200;
RA Rosovitz M.J., Schuck P., Varughese M., Chopra A.P., Mehra V., Singh Y.,
RA McGinnis L.M., Leppla S.H.;
RT "Alanine-scanning mutations in domain 4 of anthrax toxin protective antigen
RT reveal residues important for binding to the cellular receptor and to a
RT neutralizing monoclonal antibody.";
RL J. Biol. Chem. 278:30936-30944(2003).
RN [29]
RP FUNCTION, INTERACTION WITH HOST ANTXR1, AND SUBCELLULAR LOCATION
RP (PROTECTIVE ANTIGEN).
RX PubMed=14507921; DOI=10.1074/jbc.m307900200;
RA Bradley K.A., Mogridge J., Jonah G., Rainey G.J.A., Batty S., Young J.A.T.;
RT "Binding of anthrax toxin to its receptor is similar to alpha integrin-
RT ligand interactions.";
RL J. Biol. Chem. 278:49342-49347(2003).
RN [30]
RP FUNCTION (PROTECTIVE ANTIGEN PA-63).
RX PubMed=12551953; DOI=10.1083/jcb.200211018;
RA Abrami L., Liu S., Cosson P., Leppla S.H., van der Goot F.G.;
RT "Anthrax toxin triggers endocytosis of its receptor via a lipid raft-
RT mediated clathrin-dependent process.";
RL J. Cell Biol. 160:321-328(2003).
RN [31]
RP MUTAGENESIS OF ILE-393; THR-409; SER-411; THR-422; LYS-426; ASN-428;
RP TYR-440; ASN-451; ASP-454 AND PHE-456.
RX PubMed=14623961; DOI=10.1073/pnas.2436299100;
RA Mourez M., Yan M., Lacy D.B., Dillon L., Bentsen L., Marpoe A., Maurin C.,
RA Hotze E., Wigelsworth D., Pimental R.-A., Ballard J.D., Collier R.J.,
RA Tweten R.K.;
RT "Mapping dominant-negative mutations of anthrax protective antigen by
RT scanning mutagenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13803-13808(2003).
RN [32]
RP FUNCTION (PROTECTIVE ANTIGEN PA-63), INTERACTION WITH LF AND EF (PROTECTIVE
RP ANTIGEN PA-63), AND SUBCELLULAR LOCATION.
RX PubMed=15313199; DOI=10.1016/j.bbrc.2004.07.105;
RA Pimental R.A., Christensen K.A., Krantz B.A., Collier R.J.;
RT "Anthrax toxin complexes: heptameric protective antigen can bind lethal
RT factor and edema factor simultaneously.";
RL Biochem. Biophys. Res. Commun. 322:258-262(2004).
RN [33]
RP FUNCTION (PROTECTIVE ANTIGEN PA-63), SUBUNIT (PROTECTIVE ANTIGEN PA-63),
RP DOMAIN (PROTECTIVE ANTIGEN PA-63), SUBCELLULAR LOCATION (PROTECTIVE ANTIGEN
RP PA-63), AND MUTAGENESIS OF PHE-456.
RX PubMed=16051798; DOI=10.1126/science.1113380;
RA Krantz B.A., Melnyk R.A., Zhang S., Juris S.J., Lacy D.B., Wu Z.,
RA Finkelstein A., Collier R.J.;
RT "A phenylalanine clamp catalyzes protein translocation through the anthrax
RT toxin pore.";
RL Science 309:777-781(2005).
RN [34]
RP SUBUNIT (PROTECTIVE ANTIGEN PA-63).
RX PubMed=19627991; DOI=10.1016/j.jmb.2009.07.037;
RA Kintzer A.F., Thoren K.L., Sterling H.J., Dong K.C., Feld G.K., Tang I.I.,
RA Zhang T.T., Williams E.R., Berger J.M., Krantz B.A.;
RT "The protective antigen component of anthrax toxin forms functional
RT octameric complexes.";
RL J. Mol. Biol. 392:614-629(2009).
RN [35]
RP SUBUNIT (PROTECTIVE ANTIGEN PA-63).
RX PubMed=20433851; DOI=10.1016/j.jmb.2010.04.041;
RA Kintzer A.F., Sterling H.J., Tang I.I., Abdul-Gader A., Miles A.J.,
RA Wallace B.A., Williams E.R., Krantz B.A.;
RT "Role of the protective antigen octamer in the molecular mechanism of
RT anthrax lethal toxin stabilization in plasma.";
RL J. Mol. Biol. 399:741-758(2010).
RN [36]
RP SUBCELLULAR LOCATION (PROTECTIVE ANTIGEN PA-63).
RX PubMed=20221438; DOI=10.1371/journal.ppat.1000792;
RA Abrami L., Bischofberger M., Kunz B., Groux R., van der Goot F.G.;
RT "Endocytosis of the anthrax toxin is mediated by clathrin, actin and
RT unconventional adaptors.";
RL PLoS Pathog. 6:e1000792-e1000792(2010).
RN [37] {ECO:0007744|PDB:1ACC}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CALCIUM, AND DOMAIN.
RX PubMed=9039918; DOI=10.1038/385833a0;
RA Petosa C., Collier R.J., Klimpel K.R., Leppla S.H., Liddington R.C.;
RT "Crystal structure of the anthrax toxin protective antigen.";
RL Nature 385:833-838(1997).
RN [38] {ECO:0007744|PDB:1T6B}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 30-764 IN COMPLEX WITH HOST ANTXR2
RP AND CALCIUM, AND FUNCTION.
RX PubMed=15243628; DOI=10.1038/nature02763;
RA Santelli E., Bankston L.A., Leppla S.H., Liddington R.C.;
RT "Crystal structure of a complex between anthrax toxin and its host cell
RT receptor.";
RL Nature 430:905-908(2004).
RN [39] {ECO:0007744|PDB:1TZN, ECO:0007744|PDB:1TZO}
RP X-RAY CRYSTALLOGRAPHY (4.3 ANGSTROMS) OF 203-764 IN COMPLEX WITH HOST
RP ANTXR2 AND CALCIUM, AND FUNCTION.
RX PubMed=15326297; DOI=10.1073/pnas.0405405101;
RA Lacy D.B., Wigelsworth D.J., Melnyk R.A., Harrison S.C., Collier R.J.;
RT "Structure of heptameric protective antigen bound to an anthrax toxin
RT receptor: a role for receptor in pH-dependent pore formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13147-13151(2004).
RN [40] {ECO:0007744|PDB:3KWV}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 197-764 IN COMPLEX WITH EF AND
RP CALCIUM, FUNCTION (PROTECTIVE ANTIGEN PA-63), DOMAIN (PROTECTIVE ANTIGEN
RP PA-63), INTERACTION WITH LF (PROTECTIVE ANTIGEN PA-63), AND MUTAGENESIS OF
RP ARG-207; ARG-229; PHE-231; PRO-234; ILE-236; HIS-240 AND PHE-265.
RX PubMed=21037566; DOI=10.1038/nsmb.1923;
RA Feld G.K., Thoren K.L., Kintzer A.F., Sterling H.J., Tang I.I.,
RA Greenberg S.G., Williams E.R., Krantz B.A.;
RT "Structural basis for the unfolding of anthrax lethal factor by protective
RT antigen oligomers.";
RL Nat. Struct. Mol. Biol. 17:1383-1390(2010).
RN [41] {ECO:0007744|PDB:3J9C}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 203-764 IN COMPLEX
RP WITH CALCIUM, DOMAIN (PROTECTIVE ANTIGEN PA-63), SUBCELLULAR LOCATION
RP (PROTECTIVE ANTIGEN PA-63), AND SUBUNIT (PROTECTIVE ANTIGEN PA-63).
RX PubMed=25778700; DOI=10.1038/nature14247;
RA Jiang J., Pentelute B.L., Collier R.J., Zhou Z.H.;
RT "Atomic structure of anthrax protective antigen pore elucidates toxin
RT translocation.";
RL Nature 521:545-549(2015).
RN [42] {ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 203-764 IN COMPLEX
RP WITH CALCIUM; LF AND EF, INTERACTION WITH LF AND EF (PROTECTIVE ANTIGEN
RP PA-63), FUNCTION (PROTECTIVE ANTIGEN PA-63), AND DOMAIN (PROTECTIVE ANTIGEN
RP PA-63).
RX PubMed=32047164; DOI=10.1038/s41467-020-14658-6;
RA Hardenbrook N.J., Liu S., Zhou K., Ghosal K., Hong Zhou Z., Krantz B.A.;
RT "Atomic structures of anthrax toxin protective antigen channels bound to
RT partially unfolded lethal and edema factors.";
RL Nat. Commun. 11:840-840(2020).
RN [43] {ECO:0007744|PDB:6ZXJ, ECO:0007744|PDB:6ZXK, ECO:0007744|PDB:6ZXL}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 202-764 IN COMPLEX
RP WITH LF, INTERACTION WITH LF (PROTECTIVE ANTIGEN PA-63), SUBUNIT
RP (PROTECTIVE ANTIGEN PA-63), AND FUNCTION (PROTECTIVE ANTIGEN PA-63).
RX PubMed=32810181; DOI=10.1371/journal.ppat.1008530;
RA Antoni C., Quentin D., Lang A.E., Aktories K., Gatsogiannis C., Raunser S.;
RT "Cryo-EM structure of the fully-loaded asymmetric anthrax lethal toxin in
RT its heptameric pre-pore state.";
RL PLoS Pathog. 16:e1008530-e1008530(2020).
RN [44] {ECO:0007744|PDB:6VRA, ECO:0007744|PDB:6WJJ}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 203-764 IN COMPLEX
RP WITH CALCIUM; LF AND EF, INTERACTION WITH LF AND EF (PROTECTIVE ANTIGEN
RP PA-63), FUNCTION (PROTECTIVE ANTIGEN PA-63), AND DOMAIN (PROTECTIVE ANTIGEN
RP PA-63).
RX PubMed=32521227; DOI=10.1016/j.str.2020.05.009;
RA Zhou K., Liu S., Hardenbrook N.J., Cui Y., Krantz B.A., Zhou Z.H.;
RT "Atomic structures of anthrax prechannel bound with full-length Lethal and
RT Edema factors.";
RL Structure 28:879-887(2020).
CC -!- FUNCTION: Protective antigen constitutes one of the three proteins
CC composing the anthrax toxin; it mediates attachment to host cells and
CC translocation of edema factor (EF) and lethal factor (LF) into the host
CC cytoplasm (PubMed:11700562, PubMed:14507921, PubMed:15243628,
CC PubMed:15326297). PA associated with LF forms the lethal toxin (LeTx)
CC and causes death when injected; PA associated with EF forms the edema
CC toxin (EdTx) and produces edema (PubMed:1651334). PA induces immunity
CC to infection with anthrax (PubMed:11544370).
CC {ECO:0000269|PubMed:11700562, ECO:0000269|PubMed:14507921,
CC ECO:0000269|PubMed:15243628, ECO:0000269|PubMed:15326297,
CC ECO:0000269|PubMed:1651334, ECO:0000303|PubMed:11544370}.
CC -!- FUNCTION: [Protective antigen]: Mediates the attachment to host cells
CC by binding host cell receptors ANTXR1 and ANTXR2 (PubMed:11700562,
CC PubMed:14507921, PubMed:15243628, PubMed:15326297). Following host cell
CC surface attachment, PA is cleaved by FURIN to generate the PA-63
CC (Protective antigen PA-63) form, which constitutes the mature form of
CC the protein that oligomerizes and forms a pore to translocate the
CC enzymatic toxin components edema factor (EF) and lethal factor (LF)
CC into the host cytosol (PubMed:11700562, PubMed:15243628,
CC PubMed:15326297). {ECO:0000269|PubMed:11700562,
CC ECO:0000269|PubMed:14507921, ECO:0000269|PubMed:15243628,
CC ECO:0000269|PubMed:15326297}.
CC -!- FUNCTION: [Protective antigen PA-63]: Mature form that oligomerizes and
CC forms a pore to translocate the enzymatic toxin components edema factor
CC (EF) and lethal factor (LF) into the host cytosol (PubMed:15243628,
CC PubMed:15326297). Following attachment to host cell receptors and
CC cleavage by FURIN, homooligomerizes to form ring-shaped oligomers that
CC are in a pre-pore conformation, and associates with EF and LF
CC (PubMed:10085027, PubMed:12117959, PubMed:15313199). Toxin-leaded
CC complexes are then endocytosed in a clathrin-dependent process,
CC followed by a conformational change of oligomerized PA-63 from the pre-
CC pore to pore state, which is triggered by the low pH in the endosome
CC (PubMed:10085027, PubMed:12551953, PubMed:20221438, PubMed:15326297).
CC Once active, the pore mediates unfolding of EF and LF, which pass
CC through the pore and translocate into the host cytosol
CC (PubMed:16051798, PubMed:21037566, PubMed:32047164, PubMed:32810181,
CC PubMed:32521227). {ECO:0000269|PubMed:10085027,
CC ECO:0000269|PubMed:12117959, ECO:0000269|PubMed:12551953,
CC ECO:0000269|PubMed:15243628, ECO:0000269|PubMed:15313199,
CC ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:16051798,
CC ECO:0000269|PubMed:20221438, ECO:0000269|PubMed:21037566,
CC ECO:0000269|PubMed:32047164, ECO:0000269|PubMed:32521227,
CC ECO:0000269|PubMed:32810181}.
CC -!- SUBUNIT: [Protective antigen]: Interacts with host ANTXR1 and ANTXR2.
CC {ECO:0000269|PubMed:11700562, ECO:0000269|PubMed:14507921,
CC ECO:0000269|PubMed:15243628, ECO:0000269|PubMed:15326297}.
CC -!- SUBUNIT: [Protective antigen PA-63]: Homooligomer; homooligomerizes to
CC form homoheptamers (PA-63(7)) or homooctamers (PA-63(8))
CC (PubMed:10085027, PubMed:16051798, PubMed:19627991, PubMed:20433851,
CC PubMed:25778700, PubMed:32810181). PA-63(7) or PA-63(8) form ring-
CC shaped oligomers that are in a pre-pore conformation, which do not
CC penetrate the host membrane (PubMed:19627991, PubMed:20433851,
CC PubMed:32810181). PA-63(8) displays an enhanced stability, suggesting
CC that this form circulates in the blood to reach and exert toxicity even
CC in distant tissues (PubMed:20433851). Interacts with lethal factor (LF)
CC and edema factor (EF); can bind LF and EF simultaneously and
CC interaction takes place following homooligomerization on the host cell
CC membrane (PubMed:10085027, PubMed:12117959, PubMed:15313199,
CC PubMed:21037566, PubMed:32047164, PubMed:32810181, PubMed:32521227).
CC PA-63(7) homoheptamer interacts with three molecules of LF to form the
CC PA(7)LF(3) complex, in which the relative position of the N-terminal
CC alpha-helices in the three LFs determines which factor is translocated
CC first (PubMed:32810181). {ECO:0000269|PubMed:10085027,
CC ECO:0000269|PubMed:12117959, ECO:0000269|PubMed:15313199,
CC ECO:0000269|PubMed:16051798, ECO:0000269|PubMed:19627991,
CC ECO:0000269|PubMed:20433851, ECO:0000269|PubMed:21037566,
CC ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164,
CC ECO:0000269|PubMed:32521227, ECO:0000269|PubMed:32810181}.
CC -!- INTERACTION:
CC P13423; P15917: lef; NbExp=28; IntAct=EBI-456868, EBI-456923;
CC P13423; P13423: pagA; NbExp=16; IntAct=EBI-456868, EBI-456868;
CC P13423; Q9H6X2-2: ANTXR1; Xeno; NbExp=3; IntAct=EBI-456868, EBI-905659;
CC P13423; P58335: ANTXR2; Xeno; NbExp=7; IntAct=EBI-456868, EBI-456840;
CC P13423; P0A6F5: groEL; Xeno; NbExp=2; IntAct=EBI-456868, EBI-543750;
CC -!- SUBCELLULAR LOCATION: [Protective antigen]: Secreted
CC {ECO:0000269|PubMed:11207581, ECO:0000269|PubMed:12606539}. Host cell
CC membrane {ECO:0000269|PubMed:11700562, ECO:0000269|PubMed:14507921}.
CC Note=Secreted through the Sec-dependent secretion pathway
CC (PubMed:12606539). Therefore, PA is translocated across the membrane in
CC an unfolded state and then it is folded into its native configuration
CC on the trans side of the membrane, prior to its release to the
CC environment (PubMed:12606539). PA requires the extracellular chaperone
CC PrsA for efficient folding (PubMed:12606539). It circulates in the host
CC blood and binds host cell receptors at the cell surface
CC (PubMed:11700562, PubMed:14507921). {ECO:0000269|PubMed:11700562,
CC ECO:0000269|PubMed:12606539, ECO:0000269|PubMed:14507921}.
CC -!- SUBCELLULAR LOCATION: [Protective antigen PA-63]: Host cell membrane
CC {ECO:0000305|PubMed:16051798, ECO:0000305|PubMed:25778700}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:25778700,
CC ECO:0000269|PubMed:32047164}. Host endosome membrane
CC {ECO:0000305|PubMed:10085027}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164}.
CC Note=Following attachment to host cell receptors at the cell surface
CC and cleavage by FURIN, homooligomerizes to form ring-shaped oligomers
CC that are in a pre-pore conformation, and associates with EF and LF
CC (PubMed:15313199). Loaded complexes are then endocytosed in a clathrin-
CC dependent process, followed by a conformational change of oligomerized
CC PA-63 from the pre-pore to pore state, which is triggered by the low pH
CC in the endosome (PubMed:10085027, PubMed:15326297).
CC {ECO:0000269|PubMed:10085027, ECO:0000269|PubMed:15313199,
CC ECO:0000269|PubMed:15326297}.
CC -!- DOMAIN: The molecule is folded into four functional domains
CC (PubMed:1651334, PubMed:9039918). Each domain is required for a
CC particular step in the toxicity process (PubMed:1651334). Domain 1
CC contains two calcium ions and the proteolytic activation site
CC (PubMed:1651334). Cleavage of the PA monomer releases the subdomain 1a,
CC which is the N-terminal fragment of 20-kDa (PA-20) (PubMed:8051159,
CC PubMed:11207581, PubMed:9039918). The subdomain 1b is part of the
CC remaining 63-kDa fragment (PA-63) and contains the binding sites for LP
CC and EF (PubMed:8051159, PubMed:11207581, PubMed:9039918). Domain 2 is a
CC beta-barrel core containing a large flexible loop that has been
CC implicated in membrane insertion and pore formation (PubMed:1651334,
CC PubMed:11356563, PubMed:9039918). There is a chymotrypsin cleavage site
CC in this loop that is required for toxicity (PubMed:1512256,
CC PubMed:7961869, PubMed:9039918). Domain 3 has a hydrophobic patch
CC thought to be involved in protein-protein interactions (PubMed:1651334,
CC PubMed:11222612, PubMed:9039918). Domain 4 appears to be a separate
CC domain and shows limited contact with the other three domains: it would
CC swing out of the way during membrane insertion (PubMed:1651334,
CC PubMed:10085028, PubMed:12771151, PubMed:9039918). It is required for
CC binding to the receptor; the small loop is involved in receptor
CC recognition (PubMed:1651334, PubMed:10085028, PubMed:12771151,
CC PubMed:9039918). {ECO:0000269|PubMed:10085028,
CC ECO:0000269|PubMed:11207581, ECO:0000269|PubMed:11222612,
CC ECO:0000269|PubMed:11356563, ECO:0000269|PubMed:12771151,
CC ECO:0000269|PubMed:1512256, ECO:0000269|PubMed:1651334,
CC ECO:0000269|PubMed:7961869, ECO:0000269|PubMed:8051159,
CC ECO:0000269|PubMed:9039918}.
CC -!- DOMAIN: [Protective antigen PA-63]: Phe-456 residue forms the phi-clamp
CC in the pore and catalyzes protein translocation via a charge-state-
CC dependent Brownian ratchet (PubMed:16051798, PubMed:25778700). During
CC conversion of the heptameric pre-pore precursor to the pore, the seven
CC Phe-427 residues converge within the lumen to generate the narrowest
CC point in the channel lumen (6 Angstroms in width) (PubMed:16051798,
CC PubMed:25778700). To pass through this hydrophobic restriction,
CC substrate proteins LF and EF need to be unfolded prior to translocation
CC (PubMed:25778700). {ECO:0000269|PubMed:16051798,
CC ECO:0000269|PubMed:25778700}.
CC -!- DOMAIN: [Protective antigen PA-63]: The alpha-clamp consists in an
CC amphipathic cleft between two adjacent PA protomers, which assists the
CC unfolding of substrate proteins LF and EF (PubMed:21037566,
CC PubMed:32047164, PubMed:32521227). The alpha-clamp binds non-
CC specifically to alpha-helices of substrate proteins LF and EF
CC (PubMed:21037566, PubMed:32047164, PubMed:32521227).
CC {ECO:0000269|PubMed:21037566, ECO:0000269|PubMed:32047164,
CC ECO:0000269|PubMed:32521227}.
CC -!- PTM: Proteolytic activation by FURIN cleaves the protein in two parts,
CC PA-20 and PA-63; the latter is the mature protein (PubMed:1644824,
CC PubMed:1438214, PubMed:8051159, PubMed:11207581). The cleavage occurs
CC at the cell surface and probably in the serum of infected animals as
CC well; both native and cleaved PA are able to bind to the cell receptor
CC (PubMed:8051159, PubMed:11207581). The release of PA-20 from the
CC remaining receptor-bound PA-63 exposes the binding site for EF and LF,
CC and promotes oligomerization and internalization of the protein
CC (PubMed:8051159, PubMed:11207581). {ECO:0000269|PubMed:11207581,
CC ECO:0000269|PubMed:1438214, ECO:0000269|PubMed:1644824,
CC ECO:0000269|PubMed:8051159}.
CC -!- SIMILARITY: Belongs to the bacterial binary toxin family.
CC {ECO:0000305}.
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DR EMBL; M22589; AAA22637.1; -; Genomic_DNA.
DR EMBL; AF306778; AAG24446.1; -; Genomic_DNA.
DR EMBL; AF306779; AAG24447.1; -; Genomic_DNA.
DR EMBL; AF306780; AAG24448.1; -; Genomic_DNA.
DR EMBL; AF306781; AAG24449.1; -; Genomic_DNA.
DR EMBL; AF306782; AAG24450.1; -; Genomic_DNA.
DR EMBL; AF306783; AAG24451.1; -; Genomic_DNA.
DR EMBL; AF268967; AAF86457.1; -; Genomic_DNA.
DR EMBL; AF065404; AAD32414.1; -; Genomic_DNA.
DR EMBL; AE011190; AAM26109.1; -; Genomic_DNA.
DR EMBL; AE017336; AAT28905.2; -; Genomic_DNA.
DR EMBL; AJ413936; CAC93934.1; -; Genomic_DNA.
DR EMBL; AJ413937; CAC93935.1; -; Genomic_DNA.
DR EMBL; AB125961; BAD14937.1; -; Genomic_DNA.
DR PIR; I39934; I39934.
DR RefSeq; NP_052806.1; NC_001496.1.
DR RefSeq; WP_000746486.1; NZ_SDEF01000130.1.
DR RefSeq; WP_000746487.1; NZ_QAEM01000007.1.
DR RefSeq; WP_000746488.1; NZ_VTZH01000015.1.
DR PDB; 1ACC; X-ray; 2.10 A; A=30-764.
DR PDB; 1T6B; X-ray; 2.50 A; X=30-764.
DR PDB; 1TZN; X-ray; 4.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/O=203-764.
DR PDB; 1TZO; X-ray; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/O=203-764.
DR PDB; 3ETB; X-ray; 3.80 A; J/K/L/M=621-764.
DR PDB; 3INO; X-ray; 1.95 A; A/B=624-764.
DR PDB; 3J9C; EM; 2.90 A; A=203-764.
DR PDB; 3KWV; X-ray; 3.10 A; A/B/D/E=197-764.
DR PDB; 3MHZ; X-ray; 1.70 A; A=30-764.
DR PDB; 3Q8A; X-ray; 3.13 A; A=30-764.
DR PDB; 3Q8B; X-ray; 2.00 A; A=30-764.
DR PDB; 3Q8C; X-ray; 2.85 A; A=30-764.
DR PDB; 3Q8E; X-ray; 2.10 A; A=30-764.
DR PDB; 3Q8F; X-ray; 2.10 A; A=30-764.
DR PDB; 3TEW; X-ray; 1.45 A; A=30-764.
DR PDB; 3TEX; X-ray; 1.70 A; A=30-764.
DR PDB; 3TEY; X-ray; 2.12 A; A=30-764.
DR PDB; 3TEZ; X-ray; 1.83 A; A=30-764.
DR PDB; 4EE2; X-ray; 1.91 A; A=30-764.
DR PDB; 4H2A; X-ray; 1.62 A; A=30-764.
DR PDB; 4NAM; X-ray; 1.70 A; A=30-764.
DR PDB; 5FR3; X-ray; 1.94 A; A=43-764.
DR PDB; 6PSN; EM; 4.60 A; A/B/C/D/E/F/G=197-764.
DR PDB; 6UJI; X-ray; 5.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=197-764.
DR PDB; 6UZB; EM; 3.20 A; A/B/C/D/E/F/G=30-764.
DR PDB; 6UZD; EM; 3.40 A; A/B/C/D/E/F/G=30-764.
DR PDB; 6UZE; EM; 3.40 A; A/B/C/D/E/F/G=30-764.
DR PDB; 6VRA; EM; 3.30 A; A/B/C/D/E/F/G/H=33-764.
DR PDB; 6WJJ; EM; 3.80 A; A/B/C/D/E/F/G/H=33-764.
DR PDB; 6ZXJ; EM; 3.50 A; A/B/C/D/E/F/G=29-764.
DR PDB; 6ZXK; EM; 3.80 A; A/B/C/D/E/F/G=29-764.
DR PDB; 6ZXL; EM; 4.20 A; A/B/C/D/E/F/G=29-764.
DR PDB; 7KXR; EM; 3.30 A; A/B/C/D/E/F/G=203-764.
DR PDB; 7O85; EM; 3.30 A; A/D/G/J/M/P/S=203-643.
DR PDBsum; 1ACC; -.
DR PDBsum; 1T6B; -.
DR PDBsum; 1TZN; -.
DR PDBsum; 1TZO; -.
DR PDBsum; 3ETB; -.
DR PDBsum; 3INO; -.
DR PDBsum; 3J9C; -.
DR PDBsum; 3KWV; -.
DR PDBsum; 3MHZ; -.
DR PDBsum; 3Q8A; -.
DR PDBsum; 3Q8B; -.
DR PDBsum; 3Q8C; -.
DR PDBsum; 3Q8E; -.
DR PDBsum; 3Q8F; -.
DR PDBsum; 3TEW; -.
DR PDBsum; 3TEX; -.
DR PDBsum; 3TEY; -.
DR PDBsum; 3TEZ; -.
DR PDBsum; 4EE2; -.
DR PDBsum; 4H2A; -.
DR PDBsum; 4NAM; -.
DR PDBsum; 5FR3; -.
DR PDBsum; 6PSN; -.
DR PDBsum; 6UJI; -.
DR PDBsum; 6UZB; -.
DR PDBsum; 6UZD; -.
DR PDBsum; 6UZE; -.
DR PDBsum; 6VRA; -.
DR PDBsum; 6WJJ; -.
DR PDBsum; 6ZXJ; -.
DR PDBsum; 6ZXK; -.
DR PDBsum; 6ZXL; -.
DR PDBsum; 7KXR; -.
DR PDBsum; 7O85; -.
DR AlphaFoldDB; P13423; -.
DR SMR; P13423; -.
DR DIP; DIP-29841N; -.
DR IntAct; P13423; 16.
DR MINT; P13423; -.
DR BindingDB; P13423; -.
DR ChEMBL; CHEMBL5352; -.
DR DrugBank; DB09057; Anthrax immune globulin human.
DR DrugBank; DB08902; Raxibacumab.
DR DrugCentral; P13423; -.
DR TCDB; 1.C.42.1.1; the channel-forming bacillus anthracis protective antigen (bapa) family.
DR ABCD; P13423; 43 sequenced antibodies.
DR EnsemblBacteria; AAT28905; AAT28905; GBAA_pXO1_0164.
DR GeneID; 45025512; -.
DR KEGG; bar:GBAA_pXO1_0164; -.
DR HOGENOM; CLU_015269_0_0_9; -.
DR OMA; YINANVR; -.
DR Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
DR EvolutionaryTrace; P13423; -.
DR PHI-base; PHI:4090; -.
DR PRO; PR:P13423; -.
DR Proteomes; UP000000594; Plasmid pXO1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044164; C:host cell cytosol; IDA:UniProtKB.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0015267; F:channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IGI:UniProtKB.
DR GO; GO:0044533; P:positive regulation of apoptotic process in another organism; IGI:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0071806; P:protein transmembrane transport; IDA:UniProtKB.
DR GO; GO:0051844; P:translocation of peptides or proteins into symbiont; IDA:UniProtKB.
DR Gene3D; 2.60.120.240; -; 1.
DR Gene3D; 2.60.40.810; -; 1.
DR InterPro; IPR003896; Bacterial_exotoxin_B.
DR InterPro; IPR035331; Binary_toxB_3.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR InterPro; IPR035088; PA_Ca-bd.
DR InterPro; IPR027441; PA_dom4.
DR InterPro; IPR027439; PA_heptamer_dom.
DR InterPro; IPR037149; PA_heptamer_dom_sf.
DR Pfam; PF03495; Binary_toxB; 1.
DR Pfam; PF17475; Binary_toxB_2; 1.
DR Pfam; PF17476; Binary_toxB_3; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR01391; BINARYTOXINB.
DR SMART; SM00758; PA14; 1.
DR PROSITE; PS51820; PA14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cleavage on pair of basic residues;
KW Host cell membrane; Host endosome; Host membrane; Membrane; Metal-binding;
KW Plasmid; Reference proteome; Secreted; Signal; Toxin; Transmembrane;
KW Transmembrane beta strand; Virulence.
FT SIGNAL 1..29
FT /evidence="ECO:0000305|PubMed:9039918"
FT CHAIN 30..764
FT /note="Protective antigen"
FT /id="PRO_0000021996"
FT CHAIN 30..196
FT /note="Protective antigen PA-20"
FT /evidence="ECO:0000305|PubMed:11207581,
FT ECO:0000305|PubMed:8051159"
FT /id="PRO_0000021997"
FT CHAIN 197..764
FT /note="Protective antigen PA-63"
FT /evidence="ECO:0000305|PubMed:11207581,
FT ECO:0000305|PubMed:8051159"
FT /id="PRO_0000021998"
FT TRANSMEM 331..342
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:25778700,
FT ECO:0000269|PubMed:32047164, ECO:0007744|PDB:3J9C,
FT ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB,
FT ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE"
FT TRANSMEM 345..354
FT /note="Beta stranded"
FT /evidence="ECO:0000269|PubMed:25778700,
FT ECO:0000269|PubMed:32047164, ECO:0007744|PDB:3J9C,
FT ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB,
FT ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE"
FT DOMAIN 43..179
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT REGION 30..287
FT /note="Domain 1, calcium-binding; LF and EF binding sites"
FT /evidence="ECO:0000303|PubMed:9039918"
FT REGION 176..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..239
FT /note="Alpha-clamp"
FT /evidence="ECO:0000269|PubMed:21037566"
FT REGION 288..516
FT /note="Domain 2, membrane insertion and heptamerization"
FT /evidence="ECO:0000303|PubMed:9039918"
FT REGION 302..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..624
FT /note="Domain 3, heptamerization"
FT /evidence="ECO:0000303|PubMed:9039918"
FT REGION 625..764
FT /note="Domain 4, binding to the receptor"
FT /evidence="ECO:0000303|PubMed:9039918"
FT COMPBIAS 302..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15243628,
FT ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566,
FT ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164,
FT ECO:0000269|PubMed:9039918, ECO:0007744|PDB:1ACC,
FT ECO:0007744|PDB:1T6B, ECO:0007744|PDB:1TZN,
FT ECO:0007744|PDB:1TZO, ECO:0007744|PDB:3J9C,
FT ECO:0007744|PDB:3KWV, ECO:0007744|PDB:6PSN,
FT ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD,
FT ECO:0007744|PDB:6UZE"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15243628,
FT ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566,
FT ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164,
FT ECO:0000269|PubMed:9039918, ECO:0007744|PDB:1ACC,
FT ECO:0007744|PDB:1T6B, ECO:0007744|PDB:1TZN,
FT ECO:0007744|PDB:1TZO, ECO:0007744|PDB:3J9C,
FT ECO:0007744|PDB:3KWV, ECO:0007744|PDB:6PSN,
FT ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD,
FT ECO:0007744|PDB:6UZE"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15243628,
FT ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566,
FT ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164,
FT ECO:0000269|PubMed:9039918, ECO:0007744|PDB:1ACC,
FT ECO:0007744|PDB:1T6B, ECO:0007744|PDB:1TZO,
FT ECO:0007744|PDB:3J9C, ECO:0007744|PDB:3KWV,
FT ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB,
FT ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15243628,
FT ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566,
FT ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164,
FT ECO:0000269|PubMed:9039918, ECO:0007744|PDB:1ACC,
FT ECO:0007744|PDB:1T6B, ECO:0007744|PDB:1TZN,
FT ECO:0007744|PDB:1TZO, ECO:0007744|PDB:3J9C,
FT ECO:0007744|PDB:3KWV, ECO:0007744|PDB:6PSN,
FT ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD,
FT ECO:0007744|PDB:6UZE"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15243628,
FT ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566,
FT ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164,
FT ECO:0000269|PubMed:9039918, ECO:0007744|PDB:1ACC,
FT ECO:0007744|PDB:1T6B, ECO:0007744|PDB:1TZN,
FT ECO:0007744|PDB:1TZO, ECO:0007744|PDB:3J9C,
FT ECO:0007744|PDB:3KWV, ECO:0007744|PDB:6PSN,
FT ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD,
FT ECO:0007744|PDB:6UZE"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15243628,
FT ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566,
FT ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164,
FT ECO:0000269|PubMed:9039918, ECO:0007744|PDB:1ACC,
FT ECO:0007744|PDB:1T6B, ECO:0007744|PDB:1TZN,
FT ECO:0007744|PDB:1TZO, ECO:0007744|PDB:3J9C,
FT ECO:0007744|PDB:3KWV, ECO:0007744|PDB:6PSN,
FT ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD,
FT ECO:0007744|PDB:6UZE"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15243628,
FT ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566,
FT ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164,
FT ECO:0000269|PubMed:9039918, ECO:0007744|PDB:1ACC,
FT ECO:0007744|PDB:1T6B, ECO:0007744|PDB:1TZN,
FT ECO:0007744|PDB:1TZO, ECO:0007744|PDB:3J9C,
FT ECO:0007744|PDB:3KWV, ECO:0007744|PDB:6PSN,
FT ECO:0007744|PDB:6UZB, ECO:0007744|PDB:6UZD,
FT ECO:0007744|PDB:6UZE"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15326297,
FT ECO:0000269|PubMed:21037566, ECO:0000269|PubMed:25778700,
FT ECO:0000269|PubMed:32047164, ECO:0007744|PDB:1ACC,
FT ECO:0007744|PDB:1TZN, ECO:0007744|PDB:1TZO,
FT ECO:0007744|PDB:3J9C, ECO:0007744|PDB:3KWV,
FT ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB,
FT ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15243628,
FT ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566,
FT ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164,
FT ECO:0007744|PDB:1ACC, ECO:0007744|PDB:1T6B,
FT ECO:0007744|PDB:1TZN, ECO:0007744|PDB:1TZO,
FT ECO:0007744|PDB:3J9C, ECO:0007744|PDB:3KWV,
FT ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB,
FT ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15243628,
FT ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566,
FT ECO:0000269|PubMed:25778700, ECO:0000269|PubMed:32047164,
FT ECO:0007744|PDB:1ACC, ECO:0007744|PDB:1T6B,
FT ECO:0007744|PDB:1TZN, ECO:0007744|PDB:1TZO,
FT ECO:0007744|PDB:3J9C, ECO:0007744|PDB:3KWV,
FT ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB,
FT ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15243628,
FT ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:21037566,
FT ECO:0000269|PubMed:32047164, ECO:0007744|PDB:1ACC,
FT ECO:0007744|PDB:1T6B, ECO:0007744|PDB:1TZN,
FT ECO:0007744|PDB:1TZO, ECO:0007744|PDB:3KWV,
FT ECO:0007744|PDB:6PSN, ECO:0007744|PDB:6UZB,
FT ECO:0007744|PDB:6UZD, ECO:0007744|PDB:6UZE"
FT SITE 196..197
FT /note="Cleavage; by FURIN"
FT /evidence="ECO:0000269|PubMed:11207581,
FT ECO:0000269|PubMed:1438214, ECO:0000269|PubMed:1644824"
FT SITE 207
FT /note="Alpha-clamp"
FT /evidence="ECO:0000269|PubMed:21037566"
FT SITE 216
FT /note="Alpha-clamp"
FT /evidence="ECO:0000269|PubMed:21037566"
FT SITE 265
FT /note="Alpha-clamp"
FT /evidence="ECO:0000269|PubMed:21037566"
FT SITE 343..344
FT /note="Cleavage; by chymotrypsin; required for
FT translocation of LF and EF"
FT /evidence="ECO:0000269|PubMed:7961869"
FT SITE 456
FT /note="Phi-clamp"
FT /evidence="ECO:0000269|PubMed:16051798,
FT ECO:0000269|PubMed:25778700"
FT SITE 493
FT /note="Alpha-clamp"
FT /evidence="ECO:0000269|PubMed:21037566"
FT SITE 712
FT /note="Essential for binding to cell receptor"
FT /evidence="ECO:0000269|PubMed:12771151"
FT VARIANT 295
FT /note="M -> I (in strain: PAI)"
FT /evidence="ECO:0000269|PubMed:14985634"
FT VARIANT 392
FT /note="N -> D (in strain: PAI)"
FT /evidence="ECO:0000269|PubMed:14985634"
FT VARIANT 560
FT /note="F -> L (in Sverdlovsk sample)"
FT VARIANT 565
FT /note="P -> S (in strain: BA1024)"
FT /evidence="ECO:0000269|PubMed:10197996"
FT VARIANT 600
FT /note="A -> V (in strain: BA1024, V770-NP1-R, Carbosap and
FT Ferrara)"
FT /evidence="ECO:0000269|PubMed:10197996"
FT MUTAGEN 193..196
FT /note="RKKR->SNSS,SNKE: Abolished cleavage by FURIN and
FT abolished toxin activity."
FT /evidence="ECO:0000269|PubMed:1438214"
FT MUTAGEN 193
FT /note="R->A: Reduced cleavage by FURIN and reduced toxin
FT activity."
FT /evidence="ECO:0000269|PubMed:1438214"
FT MUTAGEN 194..196
FT /note="KKR->EGG: Abolished cleavage by FURIN and abolished
FT toxin activity."
FT /evidence="ECO:0000269|PubMed:1438214"
FT MUTAGEN 194..195
FT /note="KK->AA: Does not affect cleavage by FURIN and does
FT not affect toxin activity."
FT /evidence="ECO:0000269|PubMed:1438214"
FT MUTAGEN 207
FT /note="R->A: Abolished interaction with LF."
FT /evidence="ECO:0000269|PubMed:21037566"
FT MUTAGEN 213
FT /note="P->A: Decrease in the ability to bind to LF and
FT partially toxic at high concentrations."
FT /evidence="ECO:0000269|PubMed:12117959"
FT MUTAGEN 216
FT /note="L->A: Decrease in the ability to bind to LF and
FT partially toxic at high concentrations."
FT /evidence="ECO:0000269|PubMed:12117959"
FT MUTAGEN 229
FT /note="R->S: Abolished interaction with LF."
FT /evidence="ECO:0000269|PubMed:21037566"
FT MUTAGEN 231
FT /note="F->A: Loss of ability to bind to LF and completely
FT non-toxic."
FT /evidence="ECO:0000269|PubMed:12117959"
FT MUTAGEN 231
FT /note="F->S: Does not affect significantly interaction with
FT LF, while it impairs tranlocation of LF."
FT /evidence="ECO:0000269|PubMed:21037566"
FT MUTAGEN 232
FT /note="L->A: Loss of ability to bind to LF and completely
FT non-toxic."
FT /evidence="ECO:0000269|PubMed:12117959"
FT MUTAGEN 234
FT /note="P->A: Loss of ability to bind to LF and completely
FT non-toxic."
FT /evidence="ECO:0000269|PubMed:12117959"
FT MUTAGEN 234
FT /note="P->S: Does not affect significantly interaction with
FT LF."
FT /evidence="ECO:0000269|PubMed:21037566"
FT MUTAGEN 236
FT /note="I->A: Loss of ability to bind to LF and completely
FT non-toxic."
FT /evidence="ECO:0000269|PubMed:12117959"
FT MUTAGEN 236
FT /note="I->S: Abolished interaction with LF."
FT /evidence="ECO:0000269|PubMed:21037566"
FT MUTAGEN 239
FT /note="I->A: Decrease in the ability to bind to LF and
FT partially toxic at high concentrations."
FT /evidence="ECO:0000269|PubMed:12117959"
FT MUTAGEN 240
FT /note="H->A: Abolished interaction with LF."
FT /evidence="ECO:0000269|PubMed:21037566"
FT MUTAGEN 255
FT /note="W->A: No effect on LF-binding ability and as toxic
FT as the wild-type."
FT /evidence="ECO:0000269|PubMed:12117959"
FT MUTAGEN 265
FT /note="F->A: No effect on LF-binding ability and as toxic
FT as the wild-type."
FT /evidence="ECO:0000269|PubMed:12117959"
FT MUTAGEN 265
FT /note="F->S: Impaired translocation of LF."
FT /evidence="ECO:0000269|PubMed:21037566"
FT MUTAGEN 289
FT /note="P->A: Reduced toxicity in combination with lethal
FT factor. Decreased membrane insertion and translocation of
FT LF."
FT /evidence="ECO:0000269|PubMed:11356563"
FT MUTAGEN 342..344
FT /note="FFD->AAA: Decrease in toxicity probably due to slow
FT translocation of LF."
FT /evidence="ECO:0000269|PubMed:10085028"
FT MUTAGEN 342..343
FT /note="Missing: Loss of toxicity probably due to loss of
FT capability to translocate LF."
FT /evidence="ECO:0000269|PubMed:7961869"
FT MUTAGEN 342
FT /note="F->C: Loss of toxicity probably due to loss of
FT capability to translocate LF."
FT /evidence="ECO:0000269|PubMed:10085028"
FT MUTAGEN 344
FT /note="D->A: Decrease in toxicity probably due to slow
FT translocation of LF."
FT /evidence="ECO:0000269|PubMed:7961869"
FT MUTAGEN 375
FT /note="W->A: Loss of toxicity probably due to faulty
FT membrane insertion or translocation of LF/EF into the
FT cytosol."
FT /evidence="ECO:0000269|PubMed:11178978"
FT MUTAGEN 379
FT /note="M->A: No effect."
FT /evidence="ECO:0000269|PubMed:11178978"
FT MUTAGEN 381
FT /note="L->A: Loss of toxicity probably due to faulty
FT membrane insertion or translocation of LF/EF into the
FT cytosol."
FT /evidence="ECO:0000269|PubMed:11178978"
FT MUTAGEN 393
FT /note="I->C: Loss of capability to undergo conformational
FT changes that lead to pore formation and translocation."
FT /evidence="ECO:0000269|PubMed:14623961"
FT MUTAGEN 409
FT /note="T->C: Loss of capability to undergo conformational
FT changes that lead to pore formation and translocation."
FT /evidence="ECO:0000269|PubMed:14623961"
FT MUTAGEN 411
FT /note="S->C: Loss of capability to undergo conformational
FT changes that lead to pore formation and translocation."
FT /evidence="ECO:0000269|PubMed:14623961"
FT MUTAGEN 422
FT /note="T->C: Loss of capability to undergo conformational
FT changes that lead to pore formation and translocation."
FT /evidence="ECO:0000269|PubMed:14623961"
FT MUTAGEN 426
FT /note="K->A,D: Loss of capability to undergo conformational
FT changes that lead to pore formation and translocation."
FT /evidence="ECO:0000269|PubMed:11113126,
FT ECO:0000269|PubMed:14623961"
FT MUTAGEN 428
FT /note="N->C: Loss of capability to undergo conformational
FT changes that lead to pore formation and translocation."
FT /evidence="ECO:0000269|PubMed:14623961"
FT MUTAGEN 440
FT /note="Y->C: Loss of capability to undergo conformational
FT changes that lead to pore formation and translocation."
FT /evidence="ECO:0000269|PubMed:14623961"
FT MUTAGEN 451
FT /note="N->C: Loss of capability to undergo conformational
FT changes that lead to pore formation and translocation."
FT /evidence="ECO:0000269|PubMed:14623961"
FT MUTAGEN 454
FT /note="D->A,K: Loss of capability to undergo conformational
FT changes that lead to pore formation and translocation."
FT /evidence="ECO:0000269|PubMed:11113126,
FT ECO:0000269|PubMed:14623961"
FT MUTAGEN 456
FT /note="F->A: Loss of capability to undergo conformational
FT changes that lead to pore formation and translocation."
FT /evidence="ECO:0000269|PubMed:11113126,
FT ECO:0000269|PubMed:14623961"
FT MUTAGEN 456
FT /note="F->C: Abolished ability for mediate LF and EF
FT protein translocation."
FT /evidence="ECO:0000269|PubMed:16051798"
FT MUTAGEN 512
FT /note="Q->A: Loss of heptamerization capability."
FT /evidence="ECO:0000269|PubMed:11222612"
FT MUTAGEN 541
FT /note="D->A: Loss of heptamerization capability."
FT /evidence="ECO:0000269|PubMed:11222612"
FT MUTAGEN 543
FT /note="L->A: Decrease in heptamerization capability."
FT /evidence="ECO:0000269|PubMed:11222612"
FT MUTAGEN 581
FT /note="F->A: Loss of toxicity due to defective
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:11554763"
FT MUTAGEN 583
FT /note="F->A: Decrease in toxicity due to defective
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:11554763"
FT MUTAGEN 591
FT /note="I->A: Loss of toxicity due to defective
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:11554763"
FT MUTAGEN 595
FT /note="L->A: Loss of toxicity due to defective
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:11554763"
FT MUTAGEN 603
FT /note="I->A: Loss of toxicity due to defective
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:11554763"
FT MUTAGEN 621
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:11222612"
FT MUTAGEN 686
FT /note="N->A: Decrease in toxicity due to decrease in cell
FT binding."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 708
FT /note="K->A: No effect on toxicity."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 709
FT /note="K->A: Slight decrease in toxicity."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 710
FT /note="Y->A: Great decrease in toxicity due to decrease in
FT cell binding."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 711
FT /note="N->A: Loss of toxicity due to decrease in cell
FT binding."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 712
FT /note="D->A: Loss of toxicity due to decrease in cell
FT binding."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 713
FT /note="K->A: No effect on toxicity."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 714
FT /note="L->A: No effect on toxicity."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 715
FT /note="P->A: Great decrease in toxicity due to decrease in
FT cell binding."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 716
FT /note="L->A: Decrease in toxicity due to decrease in cell
FT binding."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 717
FT /note="Y->A: No effect on toxicity."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 718
FT /note="I->A: Decrease in toxicity due to decrease in cell
FT binding."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 719
FT /note="S->A: No effect on toxicity."
FT /evidence="ECO:0000269|PubMed:10085028"
FT MUTAGEN 720
FT /note="N->A: No effect on toxicity."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 721
FT /note="P->A: No effect on toxicity."
FT /evidence="ECO:0000269|PubMed:12771151"
FT MUTAGEN 722
FT /note="N->A: No effect on toxicity."
FT /evidence="ECO:0000269|PubMed:12771151"
FT CONFLICT 314
FT /note="Q -> E (in Ref. 1; AAA22637)"
FT /evidence="ECO:0000305"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:4H2A"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 60..71
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1ACC"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:4H2A"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:3TEW"
FT TURN 241..244
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:3Q8A"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 291..302
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6VRA"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 331..340
FT /evidence="ECO:0007829|PDB:3J9C"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6UZB"
FT STRAND 345..354
FT /evidence="ECO:0007829|PDB:3J9C"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 375..379
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:3J9C"
FT STRAND 386..397
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:4EE2"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:3TEW"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:3TEW"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:3J9C"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:6UZB"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:3KWV"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 465..474
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 487..492
FT /evidence="ECO:0007829|PDB:3TEW"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 497..505
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 510..516
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 517..522
FT /evidence="ECO:0007829|PDB:3TEW"
FT TURN 524..527
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:7O85"
FT HELIX 542..546
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 552..560
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 565..568
FT /evidence="ECO:0007829|PDB:3MHZ"
FT STRAND 570..575
FT /evidence="ECO:0007829|PDB:6UZD"
FT HELIX 576..578
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 579..583
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 585..597
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 603..605
FT /evidence="ECO:0007829|PDB:3TEW"
FT TURN 607..609
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:3MHZ"
FT STRAND 617..622
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 638..644
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 655..658
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 662..666
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 668..676
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 678..680
FT /evidence="ECO:0007829|PDB:3KWV"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 689..691
FT /evidence="ECO:0007829|PDB:4EE2"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:3TEW"
FT TURN 699..701
FT /evidence="ECO:0007829|PDB:3KWV"
FT STRAND 703..708
FT /evidence="ECO:0007829|PDB:3TEW"
FT TURN 709..713
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 723..731
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 732..734
FT /evidence="ECO:0007829|PDB:3TEW"
FT STRAND 741..743
FT /evidence="ECO:0007829|PDB:1ACC"
FT STRAND 753..759
FT /evidence="ECO:0007829|PDB:3TEW"
FT HELIX 760..763
FT /evidence="ECO:0007829|PDB:3TEW"
SQ SEQUENCE 764 AA; 85811 MW; 3AE1EFBF48FAA03F CRC64;
MKKRKVLIPL MALSTILVSS TGNLEVIQAE VKQENRLLNE SESSSQGLLG YYFSDLNFQA
PMVVTSSTTG DLSIPSSELE NIPSENQYFQ SAIWSGFIKV KKSDEYTFAT SADNHVTMWV
DDQEVINKAS NSNKIRLEKG RLYQIKIQYQ RENPTEKGLD FKLYWTDSQN KKEVISSDNL
QLPELKQKSS NSRKKRSTSA GPTVPDRDND GIPDSLEVEG YTVDVKNKRT FLSPWISNIH
EKKGLTKYKS SPEKWSTASD PYSDFEKVTG RIDKNVSPEA RHPLVAAYPI VHVDMENIIL
SKNEDQSTQN TDSQTRTISK NTSTSRTHTS EVHGNAEVHA SFFDIGGSVS AGFSNSNSST
VAIDHSLSLA GERTWAETMG LNTADTARLN ANIRYVNTGT APIYNVLPTT SLVLGKNQTL
ATIKAKENQL SQILAPNNYY PSKNLAPIAL NAQDDFSSTP ITMNYNQFLE LEKTKQLRLD
TDQVYGNIAT YNFENGRVRV DTGSNWSEVL PQIQETTARI IFNGKDLNLV ERRIAAVNPS
DPLETTKPDM TLKEALKIAF GFNEPNGNLQ YQGKDITEFD FNFDQQTSQN IKNQLAELNA
TNIYTVLDKI KLNAKMNILI RDKRFHYDRN NIAVGADESV VKEAHREVIN SSTEGLLLNI
DKDIRKILSG YIVEIEDTEG LKEVINDRYD MLNISSLRQD GKTFIDFKKY NDKLPLYISN
PNYKVNVYAV TKENTIINPS ENGDTSTNGI KKILIFSKKG YEIG
