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P45172 (PEPT_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 100. 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:
Peptidase T

EC=3.4.11.4
Alternative name(s):
Aminotripeptidase
Short name=Tripeptidase
Tripeptide aminopeptidase
Gene names
Name:pepT
Ordered Locus Names:HI_1348
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cleaves the N-terminal amino acid of tripeptides By similarity. HAMAP-Rule MF_00550

Catalytic activity

Release of the N-terminal residue from a tripeptide. HAMAP-Rule MF_00550

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_00550

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00550.

Sequence similarities

Belongs to the peptidase M20B family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptide metabolic process

Inferred from electronic annotation. Source: InterPro

proteolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

tripeptide aminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 412412Peptidase T HAMAP-Rule MF_00550
PRO_0000185298

Sites

Active site861 By similarity
Active site1791Proton acceptor By similarity
Metal binding841Zinc 1 By similarity
Metal binding1461Zinc 1 By similarity
Metal binding1461Zinc 2 By similarity
Metal binding1801Zinc 2 By similarity
Metal binding2021Zinc 1 By similarity
Metal binding3851Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P45172 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7922E34B2B904A49

FASTA41245,986
        10         20         30         40         50         60 
MISQIDKTEL LERFLHYVSF HTQSKPNAKH SPSSVGQMKL AMQLQKELIQ LGLENVEVSK 

        70         80         90        100        110        120 
YAVVTAFLPA NDPNLTKTIG LVAHLDTSPQ CSGKNVRPEV IEEYRGGDIA LGIGEEFISP 

       130        140        150        160        170        180 
VYYSFMQKLV GQTLIVTDGT TLLGADNKAG IAEIMTALSI LQKENIPHCN IRVAFTPDEE 

       190        200        210        220        230        240 
IGLGIHYFPM EKFSCDWAYT IDGGEVGELE YENFNAATAK VRFFGRNIHT GYAKGKMLNA 

       250        260        270        280        290        300 
LTLACEFQQV FPVDEVPEKT DGKVGFYHLE DFSGDIEQVE LTYLIRDFDE QNFAQRKAFI 

       310        320        330        340        350        360 
KNQVEKFNAK KGLKKPIELE IQDSYQNMYD VVKNVPQSIE LADRAMKAVG IKPNHKPIRG 

       370        380        390        400        410 
GTDGAFLASK GLACPNIFTG GYNFHSKHEL VSLQGMENTV QVIIEMLKCK DL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC22995.1.
PIRC64118.
RefSeqNP_439499.1. NC_000907.1.

3D structure databases

ProteinModelPortalP45172.
SMRP45172. Positions 9-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI1348.

Protein family/group databases

MEROPSM20.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22995; AAC22995; HI_1348.
GeneID950265.
KEGGhin:HI1348.
PATRIC20191381. VBIHaeInf48452_1401.

Phylogenomic databases

eggNOGCOG2195.
KOK01258.
OMAGRNIHTG.
OrthoDBEOG6SV59Q.
ProtClustDBPRK05469.

Family and domain databases

Gene3D3.30.70.360. 1 hit.
HAMAPMF_00550. Aminopeptidase_M20.
InterProIPR001261. ArgE/DapE_CS.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
IPR010161. Peptidase_M20B.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFPIRSF037215. Peptidase_M20B. 1 hit.
SUPFAMSSF55031. SSF55031. 1 hit.
TIGRFAMsTIGR01882. peptidase-T. 1 hit.
PROSITEPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePEPT_HAEIN
AccessionPrimary (citable) accession number: P45172
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 100 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