ID   TOLC_VIBCH              Reviewed;         438 AA.
AC   Q9K2Y1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Outer membrane protein TolC;
DE   AltName: Full=Multidrug efflux pump subunit TolC;
DE   Flags: Precursor;
GN   Name=tolC; OrderedLocusNames=VC_2436;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN EXPORT, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=11402016; DOI=10.1128/iai.69.7.4681-4685.2001;
RA   Bina J.E., Mekalanos J.J.;
RT   "Vibrio cholerae tolC is required for bile resistance and colonization.";
RL   Infect. Immun. 69:4681-4685(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: Outer membrane channel, which is required for the function of
CC       several efflux systems (By similarity). Required to export RtxA
CC       cytotoxin. {ECO:0000250, ECO:0000269|PubMed:11402016}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Increased sensitivity to bile salts and other
CC       detergents, erythromycin and novobiocin, but not to chloramphenicol,
CC       nalidixic acid, or tetracycline. Highly attenuated in mouse in vivo
CC       growth competition assays. {ECO:0000269|PubMed:11402016}.
CC   -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
CC       family. {ECO:0000305}.
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DR   EMBL; AF282892; AAF91468.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF95579.1; -; Genomic_DNA.
DR   PIR; B82077; B82077.
DR   RefSeq; NP_232066.1; NC_002505.1.
DR   RefSeq; WP_000735329.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9K2Y1; -.
DR   SMR; Q9K2Y1; -.
DR   STRING; 243277.VC_2436; -.
DR   TCDB; 2.A.6.2.30; the resistance-nodulation-cell division (rnd) superfamily.
DR   DNASU; 2612978; -.
DR   EnsemblBacteria; AAF95579; AAF95579; VC_2436.
DR   KEGG; vch:VC_2436; -.
DR   PATRIC; fig|243277.26.peg.2320; -.
DR   eggNOG; COG1538; Bacteria.
DR   HOGENOM; CLU_012817_0_2_6; -.
DR   OMA; YNAKQQL; -.
DR   BioCyc; MetaCyc:FY484_RS12115-MON; -.
DR   BioCyc; VCHO:VC2436-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990281; C:efflux pump complex; IBA:GO_Central.
DR   GO; GO:0015562; F:efflux transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015288; F:porin activity; IBA:GO_Central.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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   Antibiotic resistance; Cell outer membrane; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane beta strand; Transport; Virulence.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..438
FT                   /note="Outer membrane protein TolC"
FT                   /id="PRO_0000013354"
SQ   SEQUENCE   438 AA;  47751 MW;  79BDDF309953C1D5 CRC64;
     MKKLLPLFVS AALGTLSSAV WAENLAEIYN QAKENDPQLL SVAAQRDAAF EAVTSSRSAL
     LPQINLTAGY NINRSDQAPR ESDLLSAGIN FSQELYQRSS WVSLDTAEKK ARQADSQYAA
     TQQGLILRVA KAYFEVLRAQ DNLEFVRAEK AAVGRQLEQT KQRFEVGLSA ITDVHDAQAQ
     FDGVLADEVL AENSLTNSYE ALREITGQEY SKLAVLDTKR FAASRTTESS EALIEKAQQQ
     NLSLLAARIS QDVARDNISL ASSGHLPSLT LDGGYNYGNN SNDNAKNTSG EEYNDFKIGV
     NLKVPLYTGG NTTSLTKQAE FAYVAASQDL EAAYRSVVKD VRAYNNNINA SIGALRAYEQ
     AVISAKSALE ATEAGFDVGT RTIVDVLDAT RRLYDANKNL SNARYDYILS VLQLRQAIGT
     LSEQDVMDVN AGLKVAKK