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O68839

- O68839_VIBCL

UniProt

O68839 - O68839_VIBCL

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Protein

Type 4 prepilin-like proteins leader peptide-processing enzyme

Gene
pilD
Organism
Vibrio cholerae
Status
Unreviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Cleaves type-4 fimbrial leader sequence and methylates the N-terminal (generally Phe) residue By similarity.

Catalytic activityi

Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: InterPro
  2. methyltransferase activity Source: UniProtKB-KW

GO - Biological processi

  1. pathogenesis Source: TIGR
  2. protein secretion Source: TIGR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, MethyltransferaseUniRule annotation, ProteaseUniRule annotation, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Type 4 prepilin-like proteins leader peptide-processing enzymeUniRule annotation (EC:2.1.1.-UniRule annotation, EC:3.4.23.43UniRule annotation)
Gene namesi
Name:pilDImported
OrganismiVibrio choleraeImported
Taxonomic identifieri666 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Interactioni

Protein-protein interaction databases

STRINGi243277.VC2426.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A24 family.UniRule annotation

Keywords - Domaini

TransmembraneUniRule annotation

Family and domain databases

InterProiIPR010627. Pept_A24A_N.
IPR014032. Peptidase_A24A_bac.
IPR000045. Prepilin_IV_endopep_pep.
[Graphical view]
PfamiPF06750. DiS_P_DiS. 1 hit.
PF01478. Peptidase_A24. 1 hit.
[Graphical view]
PRINTSiPR00864. PREPILNPTASE.

Sequencei

Sequence statusi: Complete.

O68839-1 [UniParc]FASTAAdd to Basket

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MELFYFYPWL FPVLATLFGL IVGSFLNVVI YRLPKIMERE WRAECAASFP    50
EYGITPPEGK LTLSLPRSTC PHCQTPIRVI DNIPLLSWLA LRGQCSHCKA 100
PISARYPLIE LLTALMSLVI ATHFPFGVFA VALLFFSYVL IAATFIDFDT 150
LLLPDQLTLP LLWGGIALAL LGFSPVSLSD AVIGAMAGYL SLWSIYWLFK 200
LLTGKEGMGY GDFKLLAALG AWLGWQQLPV IVLLSSVVGV IFGLIQLRQQ 250
KKGIDMAFPF GPYLAIAGWF ALLWGDKVID WYFTTWVGQP L 291
Length:291
Mass (Da):32,434
Last modified:August 1, 1998 - v1
Checksum:i9A1ECD8D730A6EEF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF055371 Genomic DNA. Translation: AAC63504.1.
AF109904 Genomic DNA. Translation: AAD21032.1.
PIRiB82078.

Genome annotation databases

PATRICi20083869. VBIVibCho83274_2309.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF055371 Genomic DNA. Translation: AAC63504.1 .
AF109904 Genomic DNA. Translation: AAD21032.1 .
PIRi B82078.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243277.VC2426.

Protocols and materials databases

DNASUi 2612968.
Structural Biology Knowledgebase Search...

Genome annotation databases

PATRICi 20083869. VBIVibCho83274_2309.

Family and domain databases

InterProi IPR010627. Pept_A24A_N.
IPR014032. Peptidase_A24A_bac.
IPR000045. Prepilin_IV_endopep_pep.
[Graphical view ]
Pfami PF06750. DiS_P_DiS. 1 hit.
PF01478. Peptidase_A24. 1 hit.
[Graphical view ]
PRINTSi PR00864. PREPILNPTASE.
ProtoNeti Search...

Publicationsi

  1. "Identification of the Vibrio cholerae type 4 prepilin peptidase required for cholera toxin secretion and pilus formation."
    Marsh J.W., Taylor R.K.
    Mol. Microbiol. 29:1481-1492(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C6706str2Imported.
  2. "Genetic characterization of a new type IV-A pilus gene cluster found in both classical and El Tor biotypes of Vibrio cholerae."
    Fullner K.J., Mekalanos J.J.
    Infect. Immun. 67:1393-1404(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiO68839_VIBCL
AccessioniPrimary (citable) accession number: O68839
Secondary accession number(s): Q7DCT3
Entry historyi
Integrated into UniProtKB/TrEMBL: August 1, 1998
Last sequence update: August 1, 1998
Last modified: May 14, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Multifunctional enzymeUniRule annotation

External Data

Dasty 3

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