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ECOLI:PEPD

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) pepD (synonyms: pepH)
Protein Name(s) Cytosol non-specific dipeptidase

Aminoacyl-histidine dipeptidase Beta-alanyl-histidine dipeptidase Carnosinase Cysteinylglycinase Peptidase D Xaa-His dipeptidase X-His dipeptidase

External Links
UniProt P15288
EMBL M34034
U70214
U00096
AP009048
X14790
PIR JU0300
RefSeq NP_414772.1
YP_488532.1
ProteinModelPortal P15288
SMR P15288
DIP DIP-10456N
IntAct P15288
MINT MINT-1252343
STRING 511145.b0237
MEROPS M20.007
SWISS-2DPAGE P15288
PaxDb P15288
PRIDE P15288
EnsemblBacteria AAC73341
BAA77906
GeneID 12930771
945013
KEGG ecj:Y75_p0228
eco:b0237
PATRIC 32115589
EchoBASE EB0689
EcoGene EG10695
eggNOG COG2195
HOGENOM HOG000282306
InParanoid P15288
KO K01270
OMA KGGYPGW
OrthoDB EOG6BCSRT
PhylomeDB P15288
BioCyc EcoCyc:EG10695-MONOMER
ECOL316407:JW0227-MONOMER
MetaCyc:EG10695-MONOMER
PRO PR:P15288
Proteomes UP000000318
UP000000625
Genevestigator P15288
GO GO:0016805
GO:0070573
GO:0008270
GO:0043171
InterPro IPR002933
IPR011650
IPR001160
Pfam PF07687
PF01546
PIRSF PIRSF016599
PRINTS PR00934
TIGRFAMs TIGR01893

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0070573

metallodipeptidase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10695
PANTHER:PTN000865961

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10695
PANTHER:PTN000865961

C

Seeded From UniProt

complete

involved_in

GO:0043171

peptide catabolic process

PMID:355237[2]

ECO:0000316

genetic interaction evidence used in manual assertion

EcoliWiki:pepA
EcoliWiki:pepB
EcoliWiki:pepN
EcoliWiki:pepQ

P

Seeded From UniProt

complete

enables

GO:0070573

metallodipeptidase activity

PMID:7988883[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016805

dipeptidase activity

PMID:355237[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:22094925[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001160

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002933

F

Seeded From UniProt

complete

enables

GO:0103046

alanylglutamate dipeptidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.4.13.18

F

Seeded From UniProt

complete

enables

GO:0102008

cytosolic dipeptidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.4.13.18

F

Seeded From UniProt

complete

enables

GO:0016805

dipeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0224

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0482

F

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. 2.0 2.1 Miller, CG & Schwartz, G (1978) Peptidase-deficient mutants of Escherichia coli. J. Bacteriol. 135 603-11 PubMed GONUTS page
  3. Schroeder, U et al. (1994) Peptidase D of Escherichia coli K-12, a metallopeptidase of low substrate specificity. FEMS Microbiol. Lett. 123 153-9 PubMed GONUTS page
  4. Sevcenco, AM et al. (2011) Exploring the microbial metalloproteome using MIRAGE. Metallomics 3 1324-30 PubMed GONUTS page
  5. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  6. Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page