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P58474 (PEPB_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Putative peptidase B

EC=3.4.11.23
Alternative name(s):
Aminopeptidase B
Gene names
Name:pepB
Ordered Locus Names:HI_0875
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Protein existenceUncertain

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. HAMAP-Rule MF_00504

Subunit structure

Homohexamer By similarity. HAMAP-Rule MF_00504

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00504.

Sequence similarities

Belongs to the peptidase M17 family.

Caution

Could be the product of a pseudogene.

Sequence caution

The sequence L42023 differs from that shown. Reason: Frameshift at position 340. This may be a natural frameshift.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metalloexopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Putative peptidase B HAMAP-Rule MF_00504
PRO_0000165836

Sites

Active site2101 Potential
Active site2841 Potential
Metal binding1981Manganese 2 By similarity
Metal binding2031Manganese 1 By similarity
Metal binding2031Manganese 2 By similarity
Metal binding2211Manganese 2 By similarity
Metal binding2801Manganese 1 By similarity
Metal binding2821Manganese 1 By similarity
Metal binding2821Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P58474 [UniParc].

Last modified December 13, 2001. Version 1.
Checksum: A5A592E51EB18B58

FASTA43447,285
        10         20         30         40         50         60 
MQITLSNTLA NDAWGKNAIL SFDSNKAMIH LKNNGKTDRT LVQQAARKLR GQGIKEVELV 

        70         80         90        100        110        120 
GEKWDLEFCW AFYQGFYTAK QDYAIEFPHL DDEPQDELLA RIECGDFVRG IINEPAQSLT 

       130        140        150        160        170        180 
PVKLVERAAE FILNQADIYN EKSAVSFKII SGEELEQQGY HGIWTVGKGS ANLPAMLQLD 

       190        200        210        220        230        240 
FNPTQDSNAP VLACLVGKGI TFDSGGYSIK PSDGMSTMRT DMGGAALLTG ALGFAIARGL 

       250        260        270        280        290        300 
NQRVKLYLCC AENLVSNNAF KLGDIITYKN GVSAEVLNTD AEGRLVLADG LIEADNQNPG 

       310        320        330        340        350        360 
FIIDCATLTG AAKSAVGNDY HSVLSMDDEL VKNLFQSAQA ENEPFWRLPF EDFHRSQINS 

       370        380        390        400        410        420 
SFADIANIGS VPVGAGASTA TAFLSYFVKN YKQNWLHIDC SATYRKSGSD LWSVGATGIG 

       430 
VQTLANLMLS RSLK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalP58474.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OMAWGEKATL.

Family and domain databases

HAMAPMF_00504. Aminopeptidase_M17.
InterProIPR011356. Leucine_aapep/pepB.
IPR008330. Pept_M17_PepB.
IPR000819. Peptidase_M17_C.
[Graphical view]
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_HAEIN
AccessionPrimary (citable) accession number: P58474
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: December 13, 2001
Last modified: June 11, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names