TCPA_VIBCL
ID TCPA_VIBCL Reviewed; 224 AA.
AC P23024;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Toxin coregulated pilin;
DE AltName: Full=Pilus colonization factor;
DE Flags: Precursor;
GN Name=tcpA;
OS Vibrio cholerae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Classical Inaba Z17561 / Serotype O1;
RX PubMed=2576015; DOI=10.1016/0378-1119(89)90486-1;
RA Faast R., Ogierman M.A., Stroeher U.H., Manning P.A.;
RT "Nucleotide sequence of the structural gene, tcpA, for a major pilin
RT subunit of Vibrio cholerae.";
RL Gene 85:227-231(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Classical Inaba Z17561 / 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 [3]
RP PROTEIN SEQUENCE OF 26-50.
RX PubMed=2883655; DOI=10.1073/pnas.84.9.2833;
RA Taylor R.K., Miller V.L., Furlong D.B., Mekalanos J.J.;
RT "Use of phoA gene fusions to identify a pilus colonization factor
RT coordinately regulated with cholera toxin.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2833-2837(1987).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 33-224.
RX PubMed=12769840; DOI=10.1016/s1097-2765(03)00170-9;
RA Craig L., Taylor R.K., Pique M.E., Adair B.D., Arvai A.S., Singh M.,
RA Lloyd S.J., Shin D.S., Getzoff E.D., Yeager M., Forest K.T., Tainer J.A.;
RT "Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio
RT cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin.";
RL Mol. Cell 11:1139-1150(2003).
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.
CC {ECO:0000250|UniProtKB:Q60153}.
CC -!- SUBCELLULAR LOCATION: Fimbrium. Membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
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.
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DR EMBL; M33514; AAA88688.1; -; Genomic_DNA.
DR EMBL; X64098; CAA45455.1; -; Genomic_DNA.
DR RefSeq; WP_001176378.1; NZ_QJUC01000020.1.
DR PDB; 1OQV; X-ray; 1.30 A; A/B/C=54-224.
DR PDBsum; 1OQV; -.
DR AlphaFoldDB; P23024; -.
DR SMR; P23024; -.
DR EvolutionaryTrace; P23024; -.
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 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; Direct protein sequencing; Disulfide bond; Fimbrium;
KW Membrane; Methylation; Transmembrane; Transmembrane helix.
FT PROPEP 1..25
FT /note="Atypical leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070,
FT ECO:0000269|PubMed:2883655"
FT /id="PRO_0000024192"
FT CHAIN 26..224
FT /note="Toxin coregulated pilin"
FT /id="PRO_0000024193"
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 CONFLICT 57
FT /note="I -> N (in Ref. 2; CAA45455)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="N -> I (in Ref. 2; CAA45455)"
FT /evidence="ECO:0000305"
FT HELIX 56..76
FT /evidence="ECO:0007829|PDB:1OQV"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1OQV"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:1OQV"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:1OQV"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1OQV"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1OQV"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1OQV"
FT STRAND 128..140
FT /evidence="ECO:0007829|PDB:1OQV"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:1OQV"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1OQV"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:1OQV"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:1OQV"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:1OQV"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1OQV"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:1OQV"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:1OQV"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1OQV"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:1OQV"
SQ SEQUENCE 224 AA; 23328 MW; E7468D3E272276B5 CRC64;
MQLLKQLFKK KFVKEEHDKK TGQEGMTLLE VIIVLGIMGV VSAGVVTLAQ RAIDSQIMTK
AAQSLNSIQV ALTQTYRGLG NYPATADATA ASKLTSGLVS LGKISSDEAK NPFNGTNMNI
FSFPRNAAAN KAFAISVDGL TQAQCKTLIT SVGDMFPYIA IKAGGAVALA DLGDFENSAA
AAETGVGVIK SIAPASKNLD LTNITHVEKL CKGTAPFGVA FGNS
