TCPE_VIBCH
ID TCPE_VIBCH Reviewed; 340 AA.
AC P0C6C9; P29487; Q9JQ06;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Toxin coregulated pilus biosynthesis protein E;
DE AltName: Full=TCP pilus biosynthesis protein TcpE;
GN Name=tcpE; OrderedLocusNames=VC_0836;
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].
RC STRAIN=Classical Inaba Z17561 / Serotype O1;
RX PubMed=8097178; DOI=10.1016/0378-1119(93)90589-u;
RA Ogierman M.A., Zabihi S., Mourtzios L., Manning P.A.;
RT "Genetic organization and sequence of the promoter-distal region of the tcp
RT gene cluster of Vibrio cholerae.";
RL Gene 126:51-60(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8097177; DOI=10.1016/0378-1119(93)90588-t;
RA Kaufman M.R., Shaw C.E., Jones I.D., Taylor R.K.;
RT "Biogenesis and regulation of the Vibrio cholerae toxin-coregulated pilus:
RT analogies to other virulence factor secretory systems.";
RL Gene 126:43-49(1993).
RN [3]
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: Probably involved in cholera toxin receptor (GM1) interaction
CC in order to bring the cells within close proximity of the ganglioside
CC for efficient toxin delivery.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GSP F family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-15 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X64098; CAA45463.1; -; Genomic_DNA.
DR EMBL; M93963; AAA27563.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF93999.1; -; Genomic_DNA.
DR PIR; JN0525; JN0525.
DR PIR; JN0527; JN0527.
DR RefSeq; NP_230484.1; NC_002505.1.
DR RefSeq; WP_000691946.1; NZ_LT906614.1.
DR PDB; 4HHX; X-ray; 1.88 A; A=1-116.
DR PDBsum; 4HHX; -.
DR AlphaFoldDB; P0C6C9; -.
DR SMR; P0C6C9; -.
DR STRING; 243277.VC_0836; -.
DR TCDB; 3.A.15.2.2; the outer membrane protein secreting main terminal branch (mtb) family.
DR DNASU; 2614503; -.
DR EnsemblBacteria; AAF93999; AAF93999; VC_0836.
DR GeneID; 57739538; -.
DR KEGG; vch:VC_0836; -.
DR PATRIC; fig|243277.26.peg.797; -.
DR eggNOG; COG1459; Bacteria.
DR HOGENOM; CLU_063664_0_0_6; -.
DR OMA; YQFCADM; -.
DR BioCyc; VCHO:VC0836-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IBA:GO_Central.
DR Gene3D; 1.20.81.30; -; 2.
DR InterPro; IPR003004; GspF/PilC.
DR InterPro; IPR001992; T2SS_GspF/T4SS_PilC_CS.
DR InterPro; IPR018076; T2SS_GspF_dom.
DR InterPro; IPR042094; T2SS_GspF_sf.
DR PANTHER; PTHR30012; PTHR30012; 1.
DR Pfam; PF00482; T2SSF; 2.
DR PROSITE; PS00874; T2SP_F; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..340
FT /note="Toxin coregulated pilus biosynthesis protein E"
FT /id="PRO_0000207844"
FT TRANSMEM 108..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 204
FT /note="V -> A (in Ref. 2; AAA27563)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="D -> E (in Ref. 2; AAA27563)"
FT /evidence="ECO:0000305"
FT CONFLICT 240..241
FT /note="WL -> CV (in Ref. 2; AAA27563)"
FT /evidence="ECO:0000305"
FT HELIX 6..20
FT /evidence="ECO:0007829|PDB:4HHX"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:4HHX"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:4HHX"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:4HHX"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:4HHX"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4HHX"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:4HHX"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:4HHX"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:4HHX"
SQ SEQUENCE 340 AA; 38068 MW; 96DE4B3B7DAE18E4 CRC64;
MKIISKKYRL ELYSMLVDLL NDNIPLYDAL NKIQNEGVGI YDKNFIKSIE LIKDRMKSNS
SLTDALTGLI PDKEVLMINV AENSGKISSG IAAIRKNIID ADEIKSKAIS SMITPSVMLI
VTMVVIAGYS VKVFPTFESV LPVSRWPGVT QALYNLGFSL YEGLWIKVLI FVAIFITILV
FMSKNITGNF RDGFLDKLPP FNFVKHIAAT EFLANMSMLL DSRVPFKEGL DIVDHKTTRW
LSSHLQRMKA NMQEGLDYKQ ALDTNLLDKK MLLTMAVYSE LPNFSDVMQK LAIEANINLH
KKIATLAGVM KNISLITLAL SVIWIFGAIF SLVDKLSSSL
