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O68839 (O68839_VIBCL) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Type 4 prepilin-like proteins leader peptide-processing enzyme RuleBase RU003794
EC=2.1.1.- RuleBase RU003794
EC=3.4.23.43 RuleBase RU003794
Gene names
Name:pilD EMBL AAD21032.1
OrganismVibrio cholerae EMBL AAC63504.1
Taxonomic identifier666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cleaves type-4 fimbrial leader sequence and methylates the N-terminal (generally Phe) residue By similarity. RuleBase RU003794

Catalytic activity

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. RuleBase RU003794

Subcellular location

Membrane; Multi-pass membrane protein By similarity RuleBase RU003794.

Sequence similarities

Belongs to the peptidase A24 family. RuleBase RU003793

Sequences

Sequence LengthMass (Da)Tools
O68839 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 9A1ECD8D730A6EEF

FASTA29132,434
        10         20         30         40         50         60 
MELFYFYPWL FPVLATLFGL IVGSFLNVVI YRLPKIMERE WRAECAASFP EYGITPPEGK 

        70         80         90        100        110        120 
LTLSLPRSTC PHCQTPIRVI DNIPLLSWLA LRGQCSHCKA PISARYPLIE LLTALMSLVI 

       130        140        150        160        170        180 
ATHFPFGVFA VALLFFSYVL IAATFIDFDT LLLPDQLTLP LLWGGIALAL LGFSPVSLSD 

       190        200        210        220        230        240 
AVIGAMAGYL SLWSIYWLFK LLTGKEGMGY GDFKLLAALG AWLGWQQLPV IVLLSSVVGV 

       250        260        270        280        290 
IFGLIQLRQQ KKGIDMAFPF GPYLAIAGWF ALLWGDKVID WYFTTWVGQP L

« Hide

References

[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: C6706str2 EMBL AAC63504.1.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF055371 Genomic DNA. Translation: AAC63504.1.
AF109904 Genomic DNA. Translation: AAD21032.1.
PIRB82078.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING243277.VC2426.

Protocols and materials databases

DNASU2612968.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC20083869. VBIVibCho83274_2309.

Phylogenomic databases

ProtClustDBCLSK874797.

Family and domain databases

InterProIPR010627. Pept_A24A_N.
IPR014032. Peptidase_A24A_bac.
IPR000045. Prepilin_IV_endopep_pep.
[Graphical view]
PfamPF06750. DiS_P_DiS. 1 hit.
PF01478. Peptidase_A24. 1 hit.
[Graphical view]
PRINTSPR00864. PREPILNPTASE.
ProtoNetSearch...

Entry information

Entry nameO68839_VIBCL
AccessionPrimary (citable) accession number: O68839
Secondary accession number(s): Q7DCT3
Entry history
Integrated into UniProtKB/TrEMBL: August 1, 1998
Last sequence update: August 1, 1998
Last modified: May 29, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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