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Q1C5H7 (PEPB_YERPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Peptidase B

EC=3.4.11.23
Alternative name(s):
Aminopeptidase B
Gene names
Name:pepB
Ordered Locus Names:YPA_2330
OrganismYersinia pestis bv. Antiqua (strain Antiqua) [Complete proteome] [HAMAP]
Taxonomic identifier360102 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Probably plays an important role in intracellular peptide degradation By similarity. HAMAP-Rule MF_00504

Catalytic activity

Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp but may be other amino acids, including Leu, Met, His, Cys and Gln. HAMAP-Rule MF_00504

Cofactor

Binds 2 manganese ions per subunit By similarity.

Subunit structure

Homohexamer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase M17 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: HAMAP

manganese ion binding

Inferred from electronic annotation. Source: HAMAP

metalloexopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Peptidase B HAMAP-Rule MF_00504
PRO_0000258500

Sites

Active site2081 Potential
Active site2821 Potential
Metal binding1961Manganese 2 By similarity
Metal binding2011Manganese 1 By similarity
Metal binding2011Manganese 2 By similarity
Metal binding2191Manganese 2 By similarity
Metal binding2781Manganese 1 By similarity
Metal binding2801Manganese 1 By similarity
Metal binding2801Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1C5H7 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 57FDBB6B4DB67F2D

FASTA43246,531
        10         20         30         40         50         60 
MTTEIMQISL SHNPADARWG EKALISTNDQ GVTIHLTSHD QLGGIQRAAR KIDGQGIKQV 

        70         80         90        100        110        120 
KLAGEGWGLE QSWAFWQGFR GPKGQRSVVW AELPANEKTE LEQRLKIIDW VRDTINAPAE 

       130        140        150        160        170        180 
DLGPEQLAKN AIDLLCAVSC DAVSYRITKG EDLREQNYAG IYTVGRGSDR APVLLALDYN 

       190        200        210        220        230        240 
PTGNPDAPVM ACLVGKGITF DSGGYSLKQS AFMDSMKSDM GGAATLTGAL ALAAARGLKE 

       250        260        270        280        290        300 
RVKLYLCCAD NMVSGNAFKL GDIIRYRNGK TVEIMNTDAE GRLVLADGLI DASEQNAPLI 

       310        320        330        340        350        360 
IDAATLTGAA KTALGNDYHA LFSFDDELAQ ALLNSAHSEH ELFWRLPLAE FHRSQLPSNF 

       370        380        390        400        410        420 
AELNNVAGGA YSAGASTAAA FLSHFVKNYQ QGWLHIDCSA TYRKSAVDQW SAGATGLGVR 

       430 
TVANLLLAQA KQ 

« Hide

References

[1]"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen."
Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.
J. Bacteriol. 188:4453-4463(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Antiqua.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000308 Genomic DNA. Translation: ABG14295.1.
RefSeqYP_652240.1. NC_008150.1.

3D structure databases

ProteinModelPortalQ1C5H7.
ModBaseSearch...

Protein-protein interaction databases

STRING360102.YPA_2330.

Proteomic databases

PRIDEQ1C5H7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG14295; ABG14295; YPA_2330.
GeneID4121210.
KEGGypa:YPA_2330.
PATRIC18584214. VBIYerPes1796_2918.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0260.
HOGENOMHOG000243130.
KOK07751.
OMAKLAGDGW.
ProtClustDBPRK05015.

Family and domain databases

HAMAPMF_00504. Aminopeptidase_M17.
InterProIPR011356. Leucine_aapep/pepB.
IPR008330. Pept_M17_PepB.
IPR000819. Peptidase_M17_C.
[Graphical view]
PANTHERPTHR11963:SF3. PTHR11963:SF3. 1 hit.
PfamPF12404. DUF3663. 1 hit.
PF00883. Peptidase_M17. 1 hit.
[Graphical view]
PIRSFPIRSF036388. Ctsl_amnpptdse_B. 1 hit.
PRINTSPR00481. LAMNOPPTDASE.
PROSITEPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePEPB_YERPA
AccessionPrimary (citable) accession number: Q1C5H7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 11, 2006
Last modified: May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families