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P23024 (TCPA_VIBCL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Toxin coregulated pilin
Alternative name(s):
Pilus colonization factor
Gene names
Name:tcpA
OrganismVibrio cholerae
Taxonomic identifier666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Constituent of pili, which may be involved in adhesion of V.cholerae to the host intestinal epithelium.

Subcellular location

Fimbrium.

Domain

The leader sequence region and some other sequence particularities suggest that TcpA may represent a novel class of pilin, and imply the existence of a novel signal peptidase.

Ontologies

Keywords
   Cellular componentFimbrium
   PTMDisulfide bond
Methylation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular organelle

Inferred from electronic annotation. Source: InterPro

pilus

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 2525Atypical leader peptide
PRO_0000024192
Chain26 – 224199Toxin coregulated pilin
PRO_0000024193

Amino acid modifications

Modified residue261N-methylmethionine Potential
Disulfide bond145 ↔ 211

Experimental info

Sequence conflict571I → N in CAA45455. Ref.2
Sequence conflict1141N → I in CAA45455. Ref.2

Secondary structure

................................. 224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23024 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: E7468D3E272276B5

FASTA22423,328
        10         20         30         40         50         60 
MQLLKQLFKK KFVKEEHDKK TGQEGMTLLE VIIVLGIMGV VSAGVVTLAQ RAIDSQIMTK 

        70         80         90        100        110        120 
AAQSLNSIQV ALTQTYRGLG NYPATADATA ASKLTSGLVS LGKISSDEAK NPFNGTNMNI 

       130        140        150        160        170        180 
FSFPRNAAAN KAFAISVDGL TQAQCKTLIT SVGDMFPYIA IKAGGAVALA DLGDFENSAA 

       190        200        210        220 
AAETGVGVIK SIAPASKNLD LTNITHVEKL CKGTAPFGVA FGNS 

« Hide

References

[1]"Nucleotide sequence of the structural gene, tcpA, for a major pilin subunit of Vibrio cholerae."
Faast R., Ogierman M.A., Stroeher U.H., Manning P.A.
Gene 85:227-231(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Classical Inaba Z17561 / Serotype O1.
[2]"Comparison of the promoter proximal regions of the toxin-co-regulated tcp gene cluster in classical and El Tor strains of Vibrio cholerae O1."
Ogierman M.A., Voss E., Meaney C., Faast R., Attridge S.R., Manning P.A.
Gene 170:9-16(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Classical Inaba Z17561 / Serotype O1.
[3]"Use of phoA gene fusions to identify a pilus colonization factor coordinately regulated with cholera toxin."
Taylor R.K., Miller V.L., Furlong D.B., Mekalanos J.J.
Proc. Natl. Acad. Sci. U.S.A. 84:2833-2837(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-50.
[4]"Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin."
Craig L., Taylor R.K., Pique M.E., Adair B.D., Arvai A.S., Singh M., Lloyd S.J., Shin D.S., Getzoff E.D., Yeager M., Forest K.T., Tainer J.A.
Mol. Cell 11:1139-1150(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 33-224.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33514 Genomic DNA. Translation: AAA88688.1.
X64098 Genomic DNA. Translation: CAA45455.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OQVX-ray1.30A/B/C54-224[»]
1QQZmodel-A/B/C/D/E/F26-222[»]
ProteinModelPortalP23024.
SMRP23024. Positions 54-224.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR012902. N_methyl_site.
IPR010271. TcpA.
[Graphical view]
PfamPF05946. TcpA. 1 hit.
[Graphical view]
TIGRFAMsTIGR02532. IV_pilin_GFxxxE. 1 hit.
PROSITEPS00409. PROKAR_NTER_METHYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23024.

Entry information

Entry nameTCPA_VIBCL
AccessionPrimary (citable) accession number: P23024
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 3, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references