TCPA_VIBCH
ID TCPA_VIBCH Reviewed; 224 AA.
AC Q60153;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Toxin coregulated pilin;
DE AltName: Full=Pilus colonization factor;
DE Flags: Precursor;
GN Name=tcpA; OrderedLocusNames=VC_0828;
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=El Tor H1 / Serotype O1;
RX PubMed=8621096; DOI=10.1016/0378-1119(95)00744-x;
RA Ogierman M.A., Voss E., Meaney C., Faast R., Attridge S.R., Manning P.A.;
RT "Comparison of the promoter proximal regions of the toxin-co-regulated tcp
RT gene cluster in classical and El Tor strains of Vibrio cholerae O1.";
RL Gene 170:9-16(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor H1 / Serotype O1;
RX PubMed=7854116; DOI=10.1111/j.1365-2958.1994.tb00492.x;
RA Rhine J.A., Taylor R.K.;
RT "TcpA pilin sequences and colonization requirements for O1 and O139 Vibrio
RT cholerae.";
RL Mol. Microbiol. 13:1013-1020(1994).
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).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=2902187; DOI=10.1084/jem.168.4.1487;
RA Herrington D.A., Hall R.H., Losonsky G., Mekalanos J.J., Taylor R.K.,
RA Levine M.M.;
RT "Toxin, toxin-coregulated pili, and the toxR regulon are essential for
RT Vibrio cholerae pathogenesis in humans.";
RL J. Exp. Med. 168:1487-1492(1988).
RN [5]
RP FUNCTION, MUTAGENESIS OF GLY-25; LEU-29 AND VAL-45, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=8594332; DOI=10.1111/j.1365-2958.1995.mmi_17061133.x;
RA Chiang S.L., Taylor R.K., Koomey M., Mekalanos J.J.;
RT "Single amino acid substitutions in the N-terminus of Vibrio cholerae TcpA
RT affect colonization, autoagglutination, and serum resistance.";
RL Mol. Microbiol. 17:1133-1142(1995).
RN [6]
RP INDUCTION BY TOXT.
RX PubMed=12270810; DOI=10.1128/jb.184.20.5533-5544.2002;
RA Hulbert R.R., Taylor R.K.;
RT "Mechanism of ToxT-dependent transcriptional activation at the Vibrio
RT cholerae tcpA promoter.";
RL J. Bacteriol. 184:5533-5544(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 54-224, FUNCTION, AND MUTAGENESIS
RP OF CYS-145.
RX PubMed=20545841; DOI=10.1111/j.1365-2958.2010.07244.x;
RA Lim M.S., Ng D., Zong Z., Arvai A.S., Taylor R.K., Tainer J.A., Craig L.;
RT "Vibrio cholerae El Tor TcpA crystal structure and mechanism for pilus-
RT mediated microcolony formation.";
RL Mol. Microbiol. 77:755-770(2010).
CC -!- FUNCTION: Major component of the toxin co-regulated pilus (tcp) which
CC is a type IV pilus essential for bacterial aggregation and subsequent
CC colonization in the host small intestine. {ECO:0000269|PubMed:20545841,
CC ECO:0000269|PubMed:2902187, ECO:0000269|PubMed:8594332}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250}. Membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- INDUCTION: By ToxT that is required for tcpA transcriptional
CC activation. Mechanistically, interacts directly with the tcpA promoter
CC to mediate activation. {ECO:0000269|PubMed:12270810}.
CC -!- DOMAIN: The leader sequence region and some other sequence
CC particularities suggest that TcpA may represent a novel class of pilin,
CC and imply the existence of a novel signal peptidase.
CC -!- DISRUPTION PHENOTYPE: Deletion mutation abolishes Vibrio cholerae
CC colonizing capacity (PubMed:2902187). It also shows loss of observable
CC pili (PubMed:8594332). {ECO:0000269|PubMed:2902187,
CC ECO:0000269|PubMed:8594332}.
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DR EMBL; X74730; CAA52745.1; -; Genomic_DNA.
DR EMBL; U09807; AAA85786.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF93991.1; -; Genomic_DNA.
DR PIR; JC4719; JC4719.
DR RefSeq; NP_230476.1; NC_002505.1.
DR RefSeq; WP_001176374.1; NZ_LT906614.1.
DR PDB; 3HRV; X-ray; 1.50 A; A/B=54-224.
DR PDBsum; 3HRV; -.
DR AlphaFoldDB; Q60153; -.
DR SMR; Q60153; -.
DR STRING; 243277.VC_0828; -.
DR DNASU; 2614495; -.
DR EnsemblBacteria; AAF93991; AAF93991; VC_0828.
DR GeneID; 57739531; -.
DR KEGG; vch:VC_0828; -.
DR PATRIC; fig|243277.26.peg.789; -.
DR eggNOG; COG2165; Bacteria.
DR HOGENOM; CLU_1320422_0_0_6; -.
DR OMA; QWDYVEA; -.
DR BioCyc; VCHO:VC0828-MON; -.
DR EvolutionaryTrace; Q60153; -.
DR PHI-base; PHI:700; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0043230; C:extracellular organelle; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0015627; C:type II protein secretion system complex; IBA:GO_Central.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IBA:GO_Central.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR010271; TcpA.
DR Pfam; PF07963; N_methyl; 1.
DR Pfam; PF05946; TcpA; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Fimbrium; Membrane; Methylation;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT PROPEP 1..25
FT /note="Atypical leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000024190"
FT CHAIN 26..224
FT /note="Toxin coregulated pilin"
FT /id="PRO_0000024191"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000305"
FT MOD_RES 26
FT /note="N-methylmethionine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT DISULFID 145..211
FT /evidence="ECO:0000250"
FT MUTAGEN 25
FT /note="G->T: Loss of autoagglutination and pili."
FT /evidence="ECO:0000269|PubMed:8594332"
FT MUTAGEN 29
FT /note="L->M: Loss of autoagglutination and pili."
FT /evidence="ECO:0000269|PubMed:8594332"
FT MUTAGEN 45
FT /note="V->T: Loss of autoagglutination but pili remain
FT intact."
FT /evidence="ECO:0000269|PubMed:8594332"
FT MUTAGEN 145
FT /note="C->S: Loss of autoagglutination and pili."
FT /evidence="ECO:0000269|PubMed:20545841"
FT HELIX 56..76
FT /evidence="ECO:0007829|PDB:3HRV"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:3HRV"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:3HRV"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:3HRV"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3HRV"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3HRV"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3HRV"
FT STRAND 128..140
FT /evidence="ECO:0007829|PDB:3HRV"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:3HRV"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3HRV"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:3HRV"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:3HRV"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:3HRV"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3HRV"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3HRV"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:3HRV"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:3HRV"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:3HRV"
SQ SEQUENCE 224 AA; 23279 MW; 7E871F63D52BC180 CRC64;
MQLLKQLFKK KFVKEEHDKK TGQEGMTLLE VIIVLGIMGV VSAGVVTLAQ RAIDSQNMTK
AAQNLNSVQI AMTQTYRSLG NYPATANANA ATQLANGLVS LGKVSADEAK NPFTGTAMGI
FSFPRNSAAN KAFAITVGGL TQAQCKTLVT SVGDMFPFIN VKEGAFAAVA DLGDFETSVA
DAATGAGVIK SIAPGSANLN LTNITHVEKL CTGTAPFTVA FGNS
