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ECOLI:AMPA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) pepA (synonyms: carP, xerB)
Protein Name(s) Cytosol aminopeptidase

Aminopeptidase A/I Leucine aminopeptidase LAP Leucyl aminopeptidase

External Links
UniProt P68767
EMBL X15130
X86443
U14003
U00096
AP009048
PIR S04462
RefSeq NP_418681.1
YP_492398.1
PDB 1GYT
PDBsum 1GYT
ProteinModelPortal P68767
SMR P68767
DIP DIP-47860N
IntAct P68767
STRING 511145.b4260
MEROPS M17.003
MoonProt P68767
PaxDb P68767
PRIDE P68767
EnsemblBacteria AAC77217
BAE78257
GeneID 12933732
948791
KEGG ecj:Y75_p4143
eco:b4260
PATRIC 32124091
EchoBASE EB0688
EcoGene EG10694
eggNOG COG0260
HOGENOM HOG000243132
InParanoid P68767
KO K01255
OMA HELINAS
OrthoDB EOG6FV8B3
PhylomeDB P68767
BioCyc EcoCyc:EG10694-MONOMER
ECOL316407:JW4217-MONOMER
MetaCyc:EG10694-MONOMER
EvolutionaryTrace P68767
PRO PR:P68767
Proteomes UP000000318
UP000000625
Genevestigator P68767
GO GO:0005737
GO:0004177
GO:0003677
GO:0001073
GO:0030145
GO:0008235
GO:0006310
GO:0043171
GO:0006276
GO:0042150
GO:0031564
GO:0006351
HAMAP MF_00181
InterPro IPR011356
IPR000819
IPR023042
IPR008283
Pfam PF00883
PF02789
PRINTS PR00481
PROSITE PS00631

Annotations

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

involved_in

GO:0043171

peptide catabolic process

PMID:355237[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042150

plasmid recombination

PMID:2670557[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006276

plasmid maintenance

PMID:2670557[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004177

aminopeptidase activity

PMID:2670557[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

PMID:7616564[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0001073

transcription antitermination factor activity, DNA binding

PMID:7616564[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

PMID:2670557[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006351

transcription, DNA-templated

PMID:15049810[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0031564

transcription antitermination

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0001073

P

Seeded From UniProt

complete

enables

GO:0004177

aminopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000819
InterPro:IPR008283
InterPro:IPR011356

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011356

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:IPR000819
InterPro:IPR008283

P

Seeded From UniProt

complete

enables

GO:0008235

metalloexopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011356

F

Seeded From UniProt

complete

involved_in

GO:0019538

protein metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011356

P

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011356

F

Seeded From UniProt

complete

enables

GO:0004177

aminopeptidase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079211

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079211

C

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079211

F

Seeded From UniProt

complete

enables

GO:0008235

metalloexopeptidase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079211

F

Seeded From UniProt

complete

enables

GO:0004177

aminopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0031

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: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

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

Notes

References

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

  1. Miller, CG & Schwartz, G (1978) Peptidase-deficient mutants of Escherichia coli. J. Bacteriol. 135 603-11 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 Stirling, CJ et al. (1989) xerB, an Escherichia coli gene required for plasmid ColE1 site-specific recombination, is identical to pepA, encoding aminopeptidase A, a protein with substantial similarity to bovine lens leucine aminopeptidase. EMBO J. 8 1623-7 PubMed GONUTS page
  3. 3.0 3.1 Charlier, D et al. (1995) carP, involved in pyrimidine regulation of the Escherichia coli carbamoylphosphate synthetase operon encodes a sequence-specific DNA-binding protein identical to XerB and PepA, also required for resolution of ColEI multimers. J. Mol. Biol. 250 392-406 PubMed GONUTS page
  4. Gourlay, SC & Colloms, SD (2004) Control of Cre recombination by regulatory elements from Xer recombination systems. Mol. Microbiol. 52 53-65 PubMed GONUTS page