TOLC_ECOLI
ID TOLC_ECOLI Reviewed; 493 AA.
AC P02930; Q2M9G5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Outer membrane protein TolC;
DE AltName: Full=Multidrug efflux pump subunit TolC;
DE AltName: Full=Outer membrane factor TolC;
DE Flags: Precursor;
GN Name=tolC; Synonyms=colE1-i, mtcB, mukA, refI, toc, weeA;
GN OrderedLocusNames=b3035, JW5503;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6312426; DOI=10.1093/nar/11.18.6487;
RA Hackett J., Reeves P.;
RT "Primary structure of the tolC gene that codes for an outer membrane
RT protein of Escherichia coli K12.";
RL Nucleic Acids Res. 11:6487-6495(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2216730; DOI=10.1093/nar/18.18.5547;
RA Niki H., Imamura R., Ogura T., Hiraga S.;
RT "Nucleotide sequence of the tolC gene of Escherichia coli.";
RL Nucleic Acids Res. 18:5547-5547(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RC STRAIN=K12;
RX PubMed=6303857; DOI=10.1016/0014-5793(83)80518-3;
RA Hackett J., Misra R., Reeves P.;
RT "The TolC protein of Escherichia coli K12 is synthesised in a precursor
RT form.";
RL FEBS Lett. 156:307-310(1983).
RN [6]
RP PROTEIN SEQUENCE OF 23-34, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=6337123; DOI=10.1128/jb.153.2.693-699.1983;
RA Morona R., Manning P.A., Reeves P.;
RT "Identification and characterization of the TolC protein, an outer membrane
RT protein from Escherichia coli.";
RL J. Bacteriol. 153:693-699(1983).
RN [7]
RP PROTEIN SEQUENCE OF 23-34.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP PROTEIN SEQUENCE OF 23-27.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9629924; DOI=10.1002/elps.1150190539;
RA Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M.,
RA Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.;
RT "Extraction of membrane proteins by differential solubilization for
RT separation using two-dimensional gel electrophoresis.";
RL Electrophoresis 19:837-844(1998).
RN [9]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9044294; DOI=10.1046/j.1365-2958.1997.d01-1880.x;
RA Koronakis V., Li J., Koronakis E., Stauffer K.;
RT "Structure of TolC, the outer membrane component of the bacterial type I
RT efflux system, derived from two-dimensional crystals.";
RL Mol. Microbiol. 23:617-626(1997).
RN [10]
RP FUNCTION IN ACREF-TOLC EFFLUX SYSTEM.
RX PubMed=11274125; DOI=10.1128/jb.183.8.2646-2653.2001;
RA Kobayashi K., Tsukagoshi N., Aono R.;
RT "Suppression of hypersensitivity of Escherichia coli acrB mutant to organic
RT solvents by integrational activation of the acrEF operon with the IS1 or
RT IS2 element.";
RL J. Bacteriol. 183:2646-2653(2001).
RN [11]
RP FUNCTION IN ACRAB-TOLC EFFLUX SYSTEM, INTERACTION WITH ACRA, SUBUNIT,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=15228545; DOI=10.1111/j.1365-2958.2004.04158.x;
RA Touze T., Eswaran J., Bokma E., Koronakis E., Hughes C., Koronakis V.;
RT "Interactions underlying assembly of the Escherichia coli AcrAB-TolC
RT multidrug efflux system.";
RL Mol. Microbiol. 53:697-706(2004).
RN [12]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [13]
RP FUNCTION IN MACAB-TOLC EFFLUX SYSTEM, SUBUNIT, AND INTERACTION WITH MACA.
RX PubMed=18955484; DOI=10.1074/jbc.m806964200;
RA Lin H.T., Bavro V.N., Barrera N.P., Frankish H.M., Velamakanni S.,
RA van Veen H.W., Robinson C.V., Borges-Walmsley M.I., Walmsley A.R.;
RT "MacB ABC transporter is a dimer whose ATPase activity and macrolide-
RT binding capacity are regulated by the membrane fusion protein MacA.";
RL J. Biol. Chem. 284:1145-1154(2009).
RN [14]
RP SUBUNIT.
RX PubMed=19342493; DOI=10.1073/pnas.0900693106;
RA Symmons M.F., Bokma E., Koronakis E., Hughes C., Koronakis V.;
RT "The assembled structure of a complete tripartite bacterial multidrug
RT efflux pump.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7173-7178(2009).
RN [15]
RP INTERACTION WITH ACRA; EMRA AND MACA.
RX PubMed=19805313; DOI=10.1073/pnas.0906601106;
RA Tikhonova E.B., Dastidar V., Rybenkov V.V., Zgurskaya H.I.;
RT "Kinetic control of TolC recruitment by multidrug efflux complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16416-16421(2009).
RN [16]
RP INTERACTION WITH MACA.
RX PubMed=21325274; DOI=10.1074/jbc.m110.202598;
RA Xu Y., Song S., Moeller A., Kim N., Piao S., Sim S.H., Kang M., Yu W.,
RA Cho H.S., Chang I., Lee K., Ha N.C.;
RT "Functional implications of an intermeshing cogwheel-like interaction
RT between TolC and MacA in the action of macrolide-specific efflux pump
RT MacAB-TolC.";
RL J. Biol. Chem. 286:13541-13549(2011).
RN [17]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21778229; DOI=10.1074/jbc.m111.245696;
RA Fontaine F., Fuchs R.T., Storz G.;
RT "Membrane localization of small proteins in Escherichia coli.";
RL J. Biol. Chem. 286:32464-32474(2011).
RN [18]
RP FUNCTION IN COLICIN E1 IMPORT.
RX PubMed=23176499; DOI=10.1042/bst20120211;
RA Zakharov S.D., Sharma O., Zhalnina M., Yamashita E., Cramer W.A.;
RT "Pathways of colicin import: utilization of BtuB, OmpF porin and the TolC
RT drug-export protein.";
RL Biochem. Soc. Trans. 40:1463-1468(2012).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-450, AND DOMAIN.
RX PubMed=10879525; DOI=10.1038/35016007;
RA Koronakis V., Sharff A., Koronakis E., Luisi B., Hughes C.;
RT "Crystal structure of the bacterial membrane protein TolC central to
RT multidrug efflux and protein export.";
RL Nature 405:914-919(2000).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 23-493 IN COMPLEX WITH
RP HEXAAMMINECOBALT(3+), ACTIVITY REGULATION, AND MUTAGENESIS OF ASP-393 AND
RP ASP-396.
RX PubMed=15342230; DOI=10.1016/j.jmb.2004.07.088;
RA Higgins M.K., Eswaran J., Edwards P., Schertler G.F., Hughes C.,
RA Koronakis V.;
RT "Structure of the ligand-blocked periplasmic entrance of the bacterial
RT multidrug efflux protein TolC.";
RL J. Mol. Biol. 342:697-702(2004).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 3-450 OF MUTANT PHE-384/GLU-389,
RP AND MUTAGENESIS OF TYR-384 AND ARG-389.
RX PubMed=18406332; DOI=10.1016/j.molcel.2008.02.015;
RA Bavro V.N., Pietras Z., Furnham N., Perez-Cano L., Fernandez-Recio J.,
RA Pei X.Y., Misra R., Luisi B.;
RT "Assembly and channel opening in a bacterial drug efflux machine.";
RL Mol. Cell 30:114-121(2008).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 23-450 OF MUTANTS.
RX PubMed=21245342; DOI=10.1073/pnas.1012588108;
RA Pei X.Y., Hinchliffe P., Symmons M.F., Koronakis E., Benz R., Hughes C.,
RA Koronakis V.;
RT "Structures of sequential open states in a symmetrical opening transition
RT of the TolC exit duct.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2112-2117(2011).
CC -!- FUNCTION: Outer membrane channel, which is required for the function of
CC several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and
CC MacAB-TolC. These systems are involved in export of antibiotics and
CC other toxic compounds from the cell. TolC is also involved in import of
CC colicin E1 into the cells. {ECO:0000269|PubMed:11274125,
CC ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:18955484,
CC ECO:0000269|PubMed:23176499, ECO:0000269|PubMed:6337123}.
CC -!- ACTIVITY REGULATION: In vitro, inhibited by hexaamminecobalt(3+).
CC {ECO:0000269|PubMed:15342230}.
CC -!- SUBUNIT: Homotrimer. Part of tripartite efflux systems, which are
CC composed of an inner membrane transporter, a periplasmic membrane
CC fusion protein, and an outer membrane component, TolC. The complexes
CC form a large protein conduit and can translocate molecules across both
CC the inner and outer membranes. TolC interacts with the membrane fusion
CC proteins AcrA, EmrA and MacA. {ECO:0000269|PubMed:15228545,
CC ECO:0000269|PubMed:15342230, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:18955484, ECO:0000269|PubMed:19342493,
CC ECO:0000269|PubMed:19805313, ECO:0000269|PubMed:21325274,
CC ECO:0000269|PubMed:9044294}.
CC -!- INTERACTION:
CC P02930; P0AE06: acrA; NbExp=2; IntAct=EBI-875614, EBI-875601;
CC P02930; P75830: macA; NbExp=3; IntAct=EBI-875614, EBI-551961;
CC P02930; P02930: tolC; NbExp=6; IntAct=EBI-875614, EBI-875614;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:15228545,
CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21778229,
CC ECO:0000269|PubMed:6337123, ECO:0000269|PubMed:9044294}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:15228545,
CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21778229,
CC ECO:0000269|PubMed:6337123, ECO:0000269|PubMed:9044294}.
CC -!- DOMAIN: Forms a continuous, solvent-accessible conduit: a 'channel-
CC tunnel' over 140 Angstroms long that spans both the outer membrane and
CC periplasmic space. The periplasmic or proximal end of the tunnel is
CC sealed by sets of coiled helices. {ECO:0000269|PubMed:10879525}.
CC -!- DISRUPTION PHENOTYPE: Cannot grow on efflux substrates novobiocin or
CC fusidic acid. {ECO:0000269|PubMed:15228545}.
CC -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69203.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA24751.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA37982.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X00016; CAA24914.1; -; Genomic_DNA.
DR EMBL; X54049; CAA37982.1; ALT_INIT; Genomic_DNA.
DR EMBL; U28377; AAA69203.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76071.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77091.1; -; Genomic_DNA.
DR EMBL; V01505; CAA24751.1; ALT_INIT; Genomic_DNA.
DR PIR; A65091; MMECTC.
DR RefSeq; NP_417507.2; NC_000913.3.
DR RefSeq; WP_000735278.1; NZ_STEB01000001.1.
DR PDB; 1EK9; X-ray; 2.10 A; A/B/C=23-450.
DR PDB; 1TQQ; X-ray; 2.75 A; A/B/C=23-493.
DR PDB; 2VDD; X-ray; 3.30 A; A/B/C=1-450.
DR PDB; 2VDE; X-ray; 3.20 A; A/B/C=1-450.
DR PDB; 2WMZ; X-ray; 2.90 A; A/B/C=23-450.
DR PDB; 2XMN; X-ray; 2.85 A; A/B/C=23-450.
DR PDB; 5NG5; EM; 6.50 A; C/F/I=1-493.
DR PDB; 5NIK; EM; 3.30 A; A/B/C=23-493.
DR PDB; 5NIL; EM; 5.30 A; A/B/C=23-493.
DR PDB; 5O66; EM; 5.90 A; A/B/C=1-493.
DR PDB; 5V5S; EM; 6.50 A; A/B/C=23-464.
DR PDB; 6WXH; EM; 3.09 A; A/B/C=1-493.
DR PDB; 6WXI; EM; 2.84 A; A/B/C=1-493.
DR PDBsum; 1EK9; -.
DR PDBsum; 1TQQ; -.
DR PDBsum; 2VDD; -.
DR PDBsum; 2VDE; -.
DR PDBsum; 2WMZ; -.
DR PDBsum; 2XMN; -.
DR PDBsum; 5NG5; -.
DR PDBsum; 5NIK; -.
DR PDBsum; 5NIL; -.
DR PDBsum; 5O66; -.
DR PDBsum; 5V5S; -.
DR PDBsum; 6WXH; -.
DR PDBsum; 6WXI; -.
DR AlphaFoldDB; P02930; -.
DR SMR; P02930; -.
DR BioGRID; 4263248; 406.
DR BioGRID; 851838; 1.
DR ComplexPortal; CPX-2107; MacAB-TolC ABC transporter complex.
DR ComplexPortal; CPX-2119; MdtABC-TolC multidrug efflux transport complex.
DR ComplexPortal; CPX-4263; AcrAB-TolC multidrug efflux transport complex.
DR ComplexPortal; CPX-4264; AcrAD-TolC multidrug efflux transport complex.
DR ComplexPortal; CPX-4265; AcrEF-TolC multidrug efflux transport complex.
DR ComplexPortal; CPX-4268; EmrAB-TolC multidrug efflux transport system.
DR ComplexPortal; CPX-4273; EmrKY-TolC multidrug efflux transport system.
DR DIP; DIP-11007N; -.
DR IntAct; P02930; 7.
DR MINT; P02930; -.
DR STRING; 511145.b3035; -.
DR ChEMBL; CHEMBL3309023; -.
DR DrugBank; DB03350; Cobalt hexammine ion.
DR TCDB; 1.B.17.1.1; the outer membrane factor (omf) family.
DR SWISS-2DPAGE; P02930; -.
DR jPOST; P02930; -.
DR PaxDb; P02930; -.
DR PRIDE; P02930; -.
DR EnsemblBacteria; AAC76071; AAC76071; b3035.
DR EnsemblBacteria; BAE77091; BAE77091; BAE77091.
DR GeneID; 66673066; -.
DR GeneID; 947521; -.
DR KEGG; ecj:JW5503; -.
DR KEGG; eco:b3035; -.
DR PATRIC; fig|1411691.4.peg.3696; -.
DR EchoBASE; EB1002; -.
DR eggNOG; COG1538; Bacteria.
DR HOGENOM; CLU_012817_0_2_6; -.
DR InParanoid; P02930; -.
DR OMA; YNAKQQL; -.
DR PhylomeDB; P02930; -.
DR BioCyc; EcoCyc:EG11009-MON; -.
DR BioCyc; MetaCyc:EG11009-MON; -.
DR EvolutionaryTrace; P02930; -.
DR PRO; PR:P02930; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:1990281; C:efflux pump complex; IPI:ComplexPortal.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IDA:CAFA.
DR GO; GO:1990196; C:MacAB-TolC complex; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0098567; C:periplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005216; F:ion channel activity; IDA:CAFA.
DR GO; GO:0015288; F:porin activity; IDA:EcoCyc.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:CAFA.
DR GO; GO:0015721; P:bile acid and bile salt transport; IMP:EcoCyc.
DR GO; GO:0042930; P:enterobactin transport; IGI:EcoliWiki.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:CAFA.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:0014070; P:response to organic cyclic compound; IMP:EcoliWiki.
DR GO; GO:0009636; P:response to toxic substance; IMP:EcoCyc.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:EcoCyc.
DR GO; GO:0140330; P:xenobiotic detoxification by transmembrane export across the cell outer membrane; IDA:ComplexPortal.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IDA:ComplexPortal.
DR InterPro; IPR003423; OMP_efflux.
DR InterPro; IPR010130; T1SS_OMP_TolC.
DR Pfam; PF02321; OEP; 2.
DR TIGRFAMs; TIGR01844; type_I_sec_TolC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell outer membrane;
KW Direct protein sequencing; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:6337123,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9629924"
FT CHAIN 23..493
FT /note="Outer membrane protein TolC"
FT /id="PRO_0000013352"
FT TOPO_DOM 23..62
FT /note="Periplasmic"
FT TRANSMEM 63..74
FT /note="Beta stranded; Name=S1"
FT TOPO_DOM 75..82
FT /note="Extracellular"
FT TRANSMEM 83..96
FT /note="Beta stranded; Name=S2"
FT TOPO_DOM 97..268
FT /note="Periplasmic"
FT TRANSMEM 269..279
FT /note="Beta stranded; Name=S4"
FT TOPO_DOM 280..300
FT /note="Extracellular"
FT TRANSMEM 301..311
FT /note="Beta stranded; Name=S5"
FT TOPO_DOM 312..493
FT /note="Periplasmic"
FT REPEAT 23..230
FT /note="1"
FT REPEAT 231..446
FT /note="2"
FT REGION 270..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 384
FT /note="Y->F: Partial channel opening. Increases sensitivity
FT to vancomycin, by allowing its passive diffusion across the
FT outer membrane; when associated with E-389."
FT /evidence="ECO:0000269|PubMed:18406332"
FT MUTAGEN 389
FT /note="R->E: Partial channel opening. Increases sensitivity
FT to vancomycin, by allowing its passive diffusion across the
FT outer membrane; when associated with F-382."
FT /evidence="ECO:0000269|PubMed:18406332"
FT MUTAGEN 393
FT /note="D->A: Decreases inhibition by hexaamminecobalt(3+)."
FT /evidence="ECO:0000269|PubMed:15342230"
FT MUTAGEN 396
FT /note="D->A: Decreases inhibition by hexaamminecobalt(3+)."
FT /evidence="ECO:0000269|PubMed:15342230"
FT CONFLICT 178
FT /note="N -> K (in Ref. 1; CAA24914)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="V -> L (in Ref. 2; CAA37982)"
FT /evidence="ECO:0000305"
FT CONFLICT 203..204
FT /note="QL -> HV (in Ref. 1; CAA24914)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..215
FT /note="EL -> GT (in Ref. 1; CAA24914)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..270
FT /note="QIRQAQDGHLPTL -> KFARRRMVTYRLW (in Ref. 1;
FT CAA24914)"
FT /evidence="ECO:0000305"
FT CONFLICT 278..295
FT /note="ISDTSYSGSKTRGAAGTQ -> FLTPLIAVRKPCAAVP (in Ref. 1;
FT CAA24914)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="K -> T (in Ref. 1; CAA24914)"
FT /evidence="ECO:0000305"
FT CONFLICT 335..354
FT /note="SEQLESAHRSVVQTVRSSFN -> ASTWKVPIVASCQRAFCFS (in Ref.
FT 1; CAA24914)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..370
FT /note="AYKQAV -> RYTQAA (in Ref. 1; CAA24914)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..411
FT /note="TLYNAKQELANA -> SCTAQARAGNP (in Ref. 1; CAA24914)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="V -> I (in Ref. 1; CAA24914)"
FT /evidence="ECO:0000305"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:1EK9"
FT HELIX 37..57
FT /evidence="ECO:0007829|PDB:1EK9"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1EK9"
FT STRAND 63..75
FT /evidence="ECO:0007829|PDB:1EK9"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1EK9"
FT STRAND 83..98
FT /evidence="ECO:0007829|PDB:1EK9"
FT HELIX 100..167
FT /evidence="ECO:0007829|PDB:1EK9"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2VDE"
FT HELIX 173..208
FT /evidence="ECO:0007829|PDB:1EK9"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:1EK9"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:1EK9"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:1EK9"
FT HELIX 243..263
FT /evidence="ECO:0007829|PDB:1EK9"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:1EK9"
FT STRAND 269..279
FT /evidence="ECO:0007829|PDB:1EK9"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1EK9"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:1EK9"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:6WXI"
FT STRAND 302..316
FT /evidence="ECO:0007829|PDB:1EK9"
FT HELIX 319..385
FT /evidence="ECO:0007829|PDB:1EK9"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:2VDD"
FT HELIX 391..426
FT /evidence="ECO:0007829|PDB:1EK9"
FT HELIX 431..439
FT /evidence="ECO:0007829|PDB:1EK9"
FT STRAND 441..448
FT /evidence="ECO:0007829|PDB:1EK9"
SQ SEQUENCE 493 AA; 53741 MW; 6F97B4C62A848FE1 CRC64;
MKKLLPILIG LSLSGFSSLS QAENLMQVYQ QARLSNPELR KSAADRDAAF EKINEARSPL
LPQLGLGADY TYSNGYRDAN GINSNATSAS LQLTQSIFDM SKWRALTLQE KAAGIQDVTY
QTDQQTLILN TATAYFNVLN AIDVLSYTQA QKEAIYRQLD QTTQRFNVGL VAITDVQNAR
AQYDTVLANE VTARNNLDNA VEQLRQITGN YYPELAALNV ENFKTDKPQP VNALLKEAEK
RNLSLLQARL SQDLAREQIR QAQDGHLPTL DLTASTGISD TSYSGSKTRG AAGTQYDDSN
MGQNKVGLSF SLPIYQGGMV NSQVKQAQYN FVGASEQLES AHRSVVQTVR SSFNNINASI
SSINAYKQAV VSAQSSLDAM EAGYSVGTRT IVDVLDATTT LYNAKQELAN ARYNYLINQL
NIKSALGTLN EQDLLALNNA LSKPVSTNPE NVAPQTPEQN AIADGYAPDS PAPVVQQTSA
RTTTSNGHNP FRN
