TOLC_SALEN
ID TOLC_SALEN Reviewed; 491 AA.
AC Q54001;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Outer membrane protein TolC;
DE AltName: Full=Multidrug efflux pump subunit TolC;
DE Flags: Precursor;
GN Name=tolC; Synonyms=sinA;
OS Salmonella enteritidis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=149539;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=CDC5;
RX PubMed=8801424; DOI=10.1111/j.1365-2958.1995.mmi_17040701.x;
RA Stone B.J., Miller V.L.;
RT "Salmonella enteritidis has a homologue of tolC that is required for
RT virulence in BALB/c mice.";
RL Mol. Microbiol. 17:701-712(1995).
CC -!- FUNCTION: Outer membrane channel, which is required for the function of
CC several efflux systems (By similarity). Required for virulence.
CC {ECO:0000250, ECO:0000269|PubMed:8801424}.
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 -!- INDUCTION: Constitutively expressed (at protein level).
CC {ECO:0000269|PubMed:8801424}.
CC -!- DISRUPTION PHENOTYPE: Non-invasive for a number of mammalian cell
CC lines; avirulent by oral infection of BALB/c mice. Increased
CC sensitivity to acridine orange and novibiocin. Decreased resistance to
CC bile salts and SDS. {ECO:0000269|PubMed:8801424}.
CC -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
CC family. {ECO:0000305}.
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DR EMBL; U25178; AAC43973.1; -; Genomic_DNA.
DR PIR; S70190; S70190.
DR AlphaFoldDB; Q54001; -.
DR SMR; Q54001; -.
DR PRIDE; Q54001; -.
DR PHI-base; PHI:6553; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
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; Signal;
KW Transmembrane; Transmembrane beta strand; Transport; Virulence.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..491
FT /note="Outer membrane protein TolC"
FT /id="PRO_0000013353"
FT REGION 267..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 53726 MW; 58F0FB64C0257FA4 CRC64;
MQMKKLLPIL IGLSLSGFST LSQAENLMQV YQQARLSNPE LRKSAADRDA AFEKINEARS
PLLPQLGLGA DYTYSNGYRD ANGINSNETS ASLQLTQTLF DMSKWRGLTL QEKAAGIQDV
TYQTDQQTLI LNTANAYFKV LNAIDVLSYT QAQKEAIYRQ LDQTTQRFNV GLVAITDVQN
ARAQYDTVLA NEVTVRNNLD NAVEELRQVT GNYYPELASL NVEHFKTDKP KAVNALLKEA
ENRNLSLLQA RLSQDLAREQ IRQAQDGHLP TLNLTPSTGI SDTSYSGSKT NAAQYDDSNM
GQNKIGLNFS LPLYQGGMVN SQVKQAQYNF VGASEQLESA HRSVVQTVRS SFNNINASIS
SINAYKQAVV SAQSSLDAME AGYSVGTRTI VDVLDATTTL YDAKQQLANA RYTYLINQLN
IKYALGTLNE QDLLALNSTL GKPIPTSPES VAPETPDQDC AADGYNAHSA APAVQPTAAR
ANSNNGNPFR H