CYAA_BORPE
ID CYAA_BORPE Reviewed; 1706 AA.
AC P0DKX7; P15318;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Bifunctional hemolysin/adenylate cyclase;
DE AltName: Full=AC-HLY;
DE AltName: Full=ACT;
DE AltName: Full=Cyclolysin;
DE Contains:
DE RecName: Full=Calmodulin-sensitive adenylate cyclase;
DE EC=4.6.1.1 {ECO:0000269|PubMed:2050107, ECO:0000269|PubMed:2542030};
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
DE Contains:
DE RecName: Full=Hemolysin;
DE Flags: Precursor;
GN Name=cya; Synonyms=cyaA; OrderedLocusNames=BP0760;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-58; LYS-65 AND TRP-242.
RX PubMed=2542030; DOI=10.1002/j.1460-2075.1989.tb03459.x;
RA Glaser P., Elmaoglou-Lazaridou A., Krin E., Ladant D., Barzu O.,
RA Danchin A.;
RT "Identification of residues essential for catalysis and binding of
RT calmodulin in Bordetella pertussis adenylate cyclase by site-directed
RT mutagenesis.";
RL EMBO J. 8:967-972(1989).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-188; ASP-190; HIS-298
RP AND GLU-301.
RX PubMed=2050107; DOI=10.1002/j.1460-2075.1991.tb07692.x;
RA Glaser P., Munier H., Gilles A.-M., Krin E., Porumb T., Barzu O.,
RA Sarfati R., Pellecuer C., Danchin A.;
RT "Functional consequences of single amino acid substitutions in calmodulin-
RT activated adenylate cyclase of Bordetella pertussis.";
RL EMBO J. 10:1683-1688(1991).
RN [4]
RP DOMAINS.
RX PubMed=2007407; DOI=10.1111/j.1432-1033.1991.tb15838.x;
RA Munier H., Gilles A.-M., Glaser P., Danchin A., Sarfati R., Barzu O.;
RT "Isolation and characterization of catalytic and calmodulin-binding domains
RT of Bordetella pertussis adenylate cyclase.";
RL Eur. J. Biochem. 196:469-474(1991).
RN [5]
RP REVIEW.
RX PubMed=8418825;
RA Danchin A.;
RT "Phylogeny of adenylyl cyclases.";
RL Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8077197; DOI=10.1016/s0021-9258(17)31674-5;
RA Szabo G., Gray M.C., Hewlett E.L.;
RT "Adenylate cyclase toxin from Bordetella pertussis produces ion conductance
RT across artificial lipid bilayers in a calcium- and polarity-dependent
RT manner.";
RL J. Biol. Chem. 269:22496-22499(1994).
RN [7]
RP PALMITOYLATION AT LYS-983.
RX PubMed=7939682; DOI=10.1126/science.7939682;
RA Hackett M., Guo L., Shabanowitz J., Hunt D.F., Hewlett E.L.;
RT "Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella
RT pertussis.";
RL Science 266:433-435(1994).
RN [8]
RP PALMITOYLATION AT LYS-860.
RX PubMed=10196151; DOI=10.1074/jbc.274.16.10777;
RA Basar T., Havlicek V., Bezouskova S., Halada P., Hackett M., Sebo P.;
RT "The conserved lysine 860 in the additional fatty-acylation site of
RT Bordetella pertussis adenylate cyclase is crucial for toxin function
RT independently of its acylation status.";
RL J. Biol. Chem. 274:10777-10783(1999).
RN [9]
RP PALMITOYLATION AT LYS-860 AND LYS-983.
RX PubMed=11031260; DOI=10.1074/jbc.m006463200;
RA Basar T., Havlicek V., Bezouskova S., Hackett M., Sebo P.;
RT "Acylation of lysine 983 is sufficient for toxin activity of Bordetella
RT pertussis adenylate cyclase. Substitutions of alanine 140 modulate
RT acylation site selectivity of the toxin acyltransferase CyaC.";
RL J. Biol. Chem. 276:348-354(2001).
RN [10]
RP PALMITOYLATION AT LYS-983.
RX PubMed=27993565; DOI=10.1016/j.bbamem.2016.12.011;
RA Meetum K., Imtong C., Katzenmeier G., Angsuthanasombat C.;
RT "Acylation of the Bordetella pertussis CyaA-hemolysin: Functional
RT implications for efficient membrane insertion and pore formation.";
RL Biochim. Biophys. Acta 1859:312-318(2017).
RN [11]
RP PALMITOYLATION AT LYS-983.
RX PubMed=29625104; DOI=10.1016/j.bbrc.2018.04.007;
RA Raksanoh V., Prangkio P., Imtong C., Thamwiriyasati N., Suvarnapunya K.,
RA Shank L., Angsuthanasombat C.;
RT "Structural requirement of the hydrophobic region of the Bordetella
RT pertussis CyaA-hemolysin for functional association with CyaC-
RT acyltransferase in toxin acylation.";
RL Biochem. Biophys. Res. Commun. 499:862-867(2018).
RN [12]
RP PALMITOYLATION AT LYS-983.
RX PubMed=33011179; DOI=10.1016/j.abb.2020.108615;
RA Yentongchai M., Thamwiriyasati N., Imtong C., Li H.C., Angsuthanasombat C.;
RT "Preferential modification of CyaA-hemolysin by CyaC-acyltransferase
RT through the catalytic Ser30-His33 dyad in esterolysis of palmitoyl-donor
RT substrate devoid of acyl carrier proteins.";
RL Arch. Biochem. Biophys. 694:108615-108615(2020).
RN [13]
RP PALMITOYLATION AT LYS-860 AND LYS-983, AND MUTAGENESIS OF LYS-860.
RX PubMed=32461253; DOI=10.1074/jbc.ra120.014122;
RA Osickova A., Khaliq H., Masin J., Jurnecka D., Sukova A., Fiser R.,
RA Holubova J., Stanek O., Sebo P., Osicka R.;
RT "Acyltransferase-mediated selection of the length of the fatty acyl chain
RT and of the acylation site governs activation of bacterial RTX toxins.";
RL J. Biol. Chem. 295:9268-9280(2020).
CC -!- FUNCTION: Bifunctional adenylate cyclase toxin-hemolysin that plays a
CC crucial role in host colonization (PubMed:2542030, PubMed:2050107). It
CC causes whooping cough by acting on mammalian cells by elevating cAMP-
CC concentration and thus disrupts normal cell function (PubMed:2542030,
CC PubMed:2050107). {ECO:0000269|PubMed:2050107,
CC ECO:0000269|PubMed:2542030}.
CC -!- FUNCTION: [Calmodulin-sensitive adenylate cyclase]: Adenylate cyclase
CC that is activated by host intracellular calmodulin and catalyzes un-
CC regulated conversion of ATP to cAMP, thereby impairing microbicidal
CC functions of immune effector cells and inducing apoptosis of lung
CC macrophages. {ECO:0000269|PubMed:2050107, ECO:0000269|PubMed:2542030}.
CC -!- FUNCTION: [Hemolysin]: Hemolysin that forms small cation-selective
CC membrane channels, leading to hemolytic activity (PubMed:8077197). The
CC hemolytic activity of CyaA is weak compared with that of the HlyA of
CC E.coli (By similarity). {ECO:0000250|UniProtKB:J7QLC0,
CC ECO:0000269|PubMed:8077197}.
CC -!- CATALYTIC ACTIVITY: [Calmodulin-sensitive adenylate cyclase]:
CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC Evidence={ECO:0000269|PubMed:2050107, ECO:0000269|PubMed:2542030};
CC -!- ACTIVITY REGULATION: [Calmodulin-sensitive adenylate cyclase]:
CC Activated by host calmodulin. {ECO:0000269|PubMed:2542030}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2542030}.
CC -!- SUBCELLULAR LOCATION: [Hemolysin]: Host cell membrane
CC {ECO:0000305|PubMed:8077197}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- DOMAIN: The Gly-rich region is probably involved in binding calcium,
CC which is required for target cell-binding or cytolytic activity.
CC -!- PTM: Released in a processed form. {ECO:0000269|PubMed:2542030}.
CC -!- PTM: [Hemolysin]: Palmitoylated at Lys-860 and Lys-983 by CyaC
CC (PubMed:10196151, PubMed:7939682, PubMed:11031260, PubMed:29625104,
CC PubMed:33011179, PubMed:32461253). The toxin only becomes active when
CC modified in position Lys-983: palmitoylation is required for efficient
CC membrane insertion and pore formation of the acylated Hemolysin chain
CC (PubMed:7939682, PubMed:11031260, PubMed:27993565, PubMed:32461253).
CC {ECO:0000269|PubMed:10196151, ECO:0000269|PubMed:11031260,
CC ECO:0000269|PubMed:27993565, ECO:0000269|PubMed:29625104,
CC ECO:0000269|PubMed:32461253, ECO:0000269|PubMed:33011179,
CC ECO:0000269|PubMed:7939682}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the adenylyl cyclase
CC class-2 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the RTX prokaryotic
CC toxin family. {ECO:0000305}.
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DR EMBL; BX640413; CAE41066.1; -; Genomic_DNA.
DR PIR; S00893; OYBRC.
DR RefSeq; NP_879578.1; NC_002929.2.
DR RefSeq; WP_010929995.1; NZ_CP039022.1.
DR PDB; 1YRT; X-ray; 2.10 A; A=1-364.
DR PDB; 1YRU; X-ray; 2.50 A; A=1-364.
DR PDB; 1ZOT; X-ray; 2.20 A; A=7-364.
DR PDB; 2COL; X-ray; 2.20 A; A=7-362.
DR PDB; 5CXL; X-ray; 1.45 A; A/B=1529-1681.
DR PDB; 6SUS; X-ray; 1.76 A; A=1371-1690.
DR PDB; 6YNS; X-ray; 3.94 A; N/O/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l=458-481.
DR PDB; 6YNU; X-ray; 3.12 A; B/D=458-481.
DR PDBsum; 1YRT; -.
DR PDBsum; 1YRU; -.
DR PDBsum; 1ZOT; -.
DR PDBsum; 2COL; -.
DR PDBsum; 5CXL; -.
DR PDBsum; 6SUS; -.
DR PDBsum; 6YNS; -.
DR PDBsum; 6YNU; -.
DR AlphaFoldDB; P0DKX7; -.
DR BMRB; P0DKX7; -.
DR SASBDB; P0DKX7; -.
DR SMR; P0DKX7; -.
DR IntAct; P0DKX7; 1.
DR STRING; 257313.BP0760; -.
DR ABCD; P0DKX7; 4 sequenced antibodies.
DR GeneID; 45387797; -.
DR KEGG; bpe:BP0760; -.
DR PATRIC; fig|257313.5.peg.813; -.
DR eggNOG; COG2931; Bacteria.
DR HOGENOM; CLU_239696_0_0_4; -.
DR OMA; CDTPHKD; -.
DR BRENDA; 4.6.1.1; 899.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0005576; C:extracellular region; 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:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008294; F:calcium- and calmodulin-responsive adenylate cyclase activity; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0015267; F:channel activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006171; P:cAMP biosynthetic process; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:CACAO.
DR Gene3D; 2.150.10.10; -; 5.
DR Gene3D; 3.90.1760.10; -; 1.
DR InterPro; IPR035099; Anthrax_toxin_C-terminal.
DR InterPro; IPR005165; Anthrax_toxin_edema_cen.
DR InterPro; IPR037017; Anthrax_toxin_edema_cen_sf.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR018504; RTX_N.
DR InterPro; IPR003995; RTX_toxin_determinant-A.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF03497; Anthrax_toxA; 1.
DR Pfam; PF00353; HemolysinCabind; 8.
DR Pfam; PF02382; RTX; 1.
DR PRINTS; PR01488; RTXTOXINA.
DR SUPFAM; SSF51120; SSF51120; 5.
DR SUPFAM; SSF81298; SSF81298; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 5.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calcium; Calmodulin-binding; cAMP biosynthesis;
KW Cytolysis; Hemolysis; Host cell membrane; Host membrane; Lipoprotein;
KW Lyase; Membrane; Myristate; Nucleotide-binding; Palmitate;
KW Reference proteome; Repeat; Secreted; Toxin; Transmembrane; Virulence;
KW Whooping cough.
FT CHAIN 1..312
FT /note="Calmodulin-sensitive adenylate cyclase"
FT /id="PRO_0000001320"
FT CHAIN 313..1706
FT /note="Hemolysin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000001321"
FT REPEAT 1014..1031
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 1032..1049
FT /note="Hemolysin-type calcium-binding 2"
FT REPEAT 1050..1067
FT /note="Hemolysin-type calcium-binding 3"
FT REPEAT 1155..1172
FT /note="Hemolysin-type calcium-binding 4"
FT REPEAT 1173..1190
FT /note="Hemolysin-type calcium-binding 5"
FT REPEAT 1279..1296
FT /note="Hemolysin-type calcium-binding 6"
FT REPEAT 1297..1314
FT /note="Hemolysin-type calcium-binding 7"
FT REPEAT 1315..1332
FT /note="Hemolysin-type calcium-binding 8"
FT REPEAT 1335..1352
FT /note="Hemolysin-type calcium-binding 9"
FT REPEAT 1411..1428
FT /note="Hemolysin-type calcium-binding 10"
FT REPEAT 1429..1446
FT /note="Hemolysin-type calcium-binding 11"
FT REPEAT 1447..1464
FT /note="Hemolysin-type calcium-binding 12"
FT REPEAT 1468..1484
FT /note="Hemolysin-type calcium-binding 13"
FT REPEAT 1537..1554
FT /note="Hemolysin-type calcium-binding 14"
FT REPEAT 1555..1572
FT /note="Hemolysin-type calcium-binding 15"
FT REPEAT 1573..1590
FT /note="Hemolysin-type calcium-binding 16"
FT REPEAT 1603..1620
FT /note="Hemolysin-type calcium-binding 17"
FT REGION 1..399
FT /note="A, catalytic"
FT /evidence="ECO:0000305|PubMed:2007407"
FT REGION 383..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..912
FT /note="B, Ala/Gly-rich"
FT /evidence="ECO:0000305|PubMed:2007407"
FT REGION 500..698
FT /note="Required for interaction with CyaC"
FT /evidence="ECO:0000269|PubMed:29625104"
FT REGION 913..1656
FT /note="C"
FT /evidence="ECO:0000305|PubMed:2007407"
FT REGION 1657..1706
FT /note="D, Asp/Gly-rich"
FT /evidence="ECO:0000305|PubMed:2007407"
FT BINDING 349..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT LIPID 860
FT /note="N6-palmitoyl lysine"
FT /evidence="ECO:0000269|PubMed:10196151,
FT ECO:0000269|PubMed:11031260, ECO:0000269|PubMed:32461253"
FT LIPID 983
FT /note="N6-palmitoyl lysine"
FT /evidence="ECO:0000269|PubMed:11031260,
FT ECO:0000269|PubMed:27993565, ECO:0000269|PubMed:29625104,
FT ECO:0000269|PubMed:32461253, ECO:0000269|PubMed:33011179,
FT ECO:0000269|PubMed:7939682"
FT MUTAGEN 58
FT /note="K->Q: Abolished adenylate cyclase activity."
FT /evidence="ECO:0000269|PubMed:2542030"
FT MUTAGEN 65
FT /note="K->Q: Abolished adenylate cyclase activity."
FT /evidence="ECO:0000269|PubMed:2542030"
FT MUTAGEN 188
FT /note="D->E,N,Y,H: Loss of adenylate cyclase activity."
FT /evidence="ECO:0000269|PubMed:2050107"
FT MUTAGEN 190
FT /note="D->N,Y,H: Loss of adenylate cyclase activity."
FT /evidence="ECO:0000269|PubMed:2050107"
FT MUTAGEN 242
FT /note="W->D,G,R,V: Reduced affinity for altered affinity
FT for calmodulin without affecting the adenylate cyclase
FT activity."
FT /evidence="ECO:0000269|PubMed:2542030"
FT MUTAGEN 298
FT /note="H->R,P,L: Loss of adenylate cyclase activity."
FT /evidence="ECO:0000269|PubMed:2050107"
FT MUTAGEN 301
FT /note="E->Q,K: Loss of adenylate cyclase activity."
FT /evidence="ECO:0000269|PubMed:2050107"
FT MUTAGEN 860
FT /note="K->R: Does not affect ability of Hemolysin chain to
FT be activated by CyaC."
FT /evidence="ECO:0000269|PubMed:32461253"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1YRT"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 90..105
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:1ZOT"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 235..252
FT /evidence="ECO:0007829|PDB:1YRT"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 274..289
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1YRT"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:1YRT"
FT TURN 348..354
FT /evidence="ECO:0007829|PDB:1YRT"
FT HELIX 460..480
FT /evidence="ECO:0007829|PDB:6YNU"
FT STRAND 1418..1420
FT /evidence="ECO:0007829|PDB:6SUS"
FT STRAND 1427..1429
FT /evidence="ECO:0007829|PDB:6SUS"
FT STRAND 1436..1438
FT /evidence="ECO:0007829|PDB:6SUS"
FT STRAND 1445..1447
FT /evidence="ECO:0007829|PDB:6SUS"
FT STRAND 1454..1456
FT /evidence="ECO:0007829|PDB:6SUS"
FT STRAND 1463..1465
FT /evidence="ECO:0007829|PDB:6SUS"
FT STRAND 1474..1476
FT /evidence="ECO:0007829|PDB:6SUS"
FT STRAND 1483..1485
FT /evidence="ECO:0007829|PDB:6SUS"
FT STRAND 1500..1503
FT /evidence="ECO:0007829|PDB:6SUS"
FT TURN 1504..1507
FT /evidence="ECO:0007829|PDB:6SUS"
FT STRAND 1508..1511
FT /evidence="ECO:0007829|PDB:6SUS"
FT STRAND 1514..1523
FT /evidence="ECO:0007829|PDB:6SUS"
FT STRAND 1526..1528
FT /evidence="ECO:0007829|PDB:6SUS"
FT STRAND 1535..1537
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1544..1546
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1553..1555
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1562..1564
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1571..1573
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1580..1582
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1589..1593
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1598..1601
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1610..1615
FT /evidence="ECO:0007829|PDB:5CXL"
FT HELIX 1617..1619
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1620..1625
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1628..1633
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1639..1642
FT /evidence="ECO:0007829|PDB:5CXL"
FT TURN 1643..1647
FT /evidence="ECO:0007829|PDB:5CXL"
FT HELIX 1649..1651
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1654..1658
FT /evidence="ECO:0007829|PDB:5CXL"
FT STRAND 1661..1664
FT /evidence="ECO:0007829|PDB:5CXL"
FT HELIX 1665..1674
FT /evidence="ECO:0007829|PDB:5CXL"
SQ SEQUENCE 1706 AA; 177521 MW; C1FD3D46CABCEF39 CRC64;
MQQSHQAGYA NAADRESGIP AAVLDGIKAV AKEKNATLMF RLVNPHSTSL IAEGVATKGL
GVHAKSSDWG LQAGYIPVNP NLSKLFGRAP EVIARADNDV NSSLAHGHTA VDLTLSKERL
DYLRQAGLVT GMADGVVASN HAGYEQFEFR VKETSDGRYA VQYRRKGGDD FEAVKVIGNA
AGIPLTADID MFAIMPHLSN FRDSARSSVT SGDSVTDYLA RTRRAASEAT GGLDRERIDL
LWKIARAGAR SAVGTEARRQ FRYDGDMNIG VITDFELEVR NALNRRAHAV GAQDVVQHGT
EQNNPFPEAD EKIFVVSATG ESQMLTRGQL KEYIGQQRGE GYVFYENRAY GVAGKSLFDD
GLGAAPGVPS GRSKFSPDVL ETVPASPGLR RPSLGAVERQ DSGYDSLDGV GSRSFSLGEV
SDMAAVEAAE LEMTRQVLHA GARQDDAEPG VSGASAHWGQ RALQGAQAVA AAQRLVHAIA
LMTQFGRAGS TNTPQEAASL SAAVFGLGEA SSAVAETVSG FFRGSSRWAG GFGVAGGAMA
LGGGIAAAVG AGMSLTDDAP AGQKAAAGAE IALQLTGGTV ELASSIALAL AAARGVTSGL
QVAGASAGAA AGALAAALSP MEIYGLVQQS HYADQLDKLA QESSAYGYEG DALLAQLYRD
KTAAEGAVAG VSAVLSTVGA AVSIAAAASV VGAPVAVVTS LLTGALNGIL RGVQQPIIEK
LANDYARKID ELGGPQAYFE KNLQARHEQL ANSDGLRKML ADLQAGWNAS SVIGVQTTEI
SKSALELAAI TGNADNLKSV DVFVDRFVQG ERVAGQPVVL DVAAGGIDIA SRKGERPALT
FITPLAAPGE EQRRRTKTGK SEFTTFVEIV GKQDRWRIRD GAADTTIDLA KVVSQLVDAN
GVLKHSIKLD VIGGDGDDVV LANASRIHYD GGAGTNTVSY AALGRQDSIT VSADGERFNV
RKQLNNANVY REGVATQTTA YGKRTENVQY RHVELARVGQ LVEVDTLEHV QHIIGGAGND
SITGNAHDNF LAGGSGDDRL DGGAGNDTLV GGEGQNTVIG GAGDDVFLQD LGVWSNQLDG
GAGVDTVKYN VHQPSEERLE RMGDTGIHAD LQKGTVEKWP ALNLFSVDHV KNIENLHGSR
LNDRIAGDDQ DNELWGHDGN DTIRGRGGDD ILRGGLGLDT LYGEDGNDIF LQDDETVSDD
IDGGAGLDTV DYSAMIHPGR IVAPHEYGFG IEADLSREWV RKASALGVDY YDNVRNVENV
IGTSMKDVLI GDAQANTLMG QGGDDTVRGG DGDDLLFGGD GNDMLYGDAG NDTLYGGLGD
DTLEGGAGND WFGQTQAREH DVLRGGDGVD TVDYSQTGAH AGIAAGRIGL GILADLGAGR
VDKLGEAGSS AYDTVSGIEN VVGTELADRI TGDAQANVLR GAGGADVLAG GEGDDVLLGG
DGDDQLSGDA GRDRLYGEAG DDWFFQDAAN AGNLLDGGDG RDTVDFSGPG RGLDAGAKGV
FLSLGKGFAS LMDEPETSNV LRNIENAVGS ARDDVLIGDA GANVLNGLAG NDVLSGGAGD
DVLLGDEGSD LLSGDAGNDD LFGGQGDDTY LFGVGYGHDT IYESGGGHDT IRINAGADQL
WFARQGNDLE IRILGTDDAL TVHDWYRDAD HRVEIIHAAN QAVDQAGIEK LVEAMAQYPD
PGAAAAAPPA ARVPDTLMQS LAVNWR
