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pepP Xaa-Pro aminopeptidase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947385, updated on 26-Mar-2025
Official Symbol
pepP
Official Full Name
Xaa-Pro aminopeptidase
Primary source
ECOCYC:EG10697
Locus tag
b2908
See related
ASAP:ABE-0009549
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK2903
Summary
Overexpression causes abnormal biofilm architecture. [More information is available at EcoGene: EG10697]. Aminopeptidase P is an exopeptidase that cleaves the amino-terminal residue from polypeptides, as long as the following residue is a proline . [More information is available at EcoCyc: EG10697].
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Sequence:
NC_000913.3 (3053515..3054840, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene protein YqfI Neighboring gene 2-octaprenylphenol 6-hydroxylase Neighboring gene 2-octaprenyl-6-methoxyphenol 4-hydroxylase Neighboring gene PF03695 family protein YgfB Neighboring gene cell division protein ZapA

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Aminopeptidase-P. Yaron A, et al. Biochem Biophys Res Commun, 1968 Aug 21. PMID 4878817
  2. Novel 3-amino-2-hydroxy acids containing protease inhibitors. Part 1: Synthesis and kinetic characterization as aminopeptidase P inhibitors. Stöckel-Maschek A, et al. Bioorg Med Chem, 2005 Aug 15. PMID 15993089
  3. Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin. Graham SC, et al. Acta Crystallogr D Biol Crystallogr, 2004 Oct. PMID 15388923
  4. A continuous fluorimetric assay for aminopeptidase P detailed analysis of product inhibition. Stöckel-Maschek A, et al. Anal Biochem, 2003 Nov 1. PMID 14705781
  5. An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution. Graham SC, et al. Acta Crystallogr D Biol Crystallogr, 2003 May. PMID 12777807

See all (30) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Thioproline formation as a driver of formaldehyde toxicity in Escherichia coli.
    Title: Thioproline formation as a driver of formaldehyde toxicity in Escherichia coli.
  2. analysis of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu
    Title: Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu.
  3. Mutation of the conserved active site residues His243 and His361 revealed that both are required for catalysis.
    Title: Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis.
  4. N-terminus verified by Edman degradation on mature peptide
    Title: Cloning and expression of aminopeptidase P gene from Escherichia coli HB101 and characterization of expressed enzyme.
  5. x-ray crystallographic structure of aminopeptidase P in complex with the inhibitor apstatin
    Title: Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin.
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Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables aminopeptidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables aminopeptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables aminopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables manganese ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables manganese ion binding IEA
Inferred from Electronic Annotation
more info
  
enables manganese ion binding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables metalloaminopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables metalloexopeptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables metalloexopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables metallopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables peptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in protein homotetramerization IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in proteolysis IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol HDA PubMed 
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
part_of protein-containing complex IDA
Inferred from Direct Assay
more info
 PubMed 
Preferred Names
Xaa-Pro aminopeptidase

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    3053515..3054840 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417384.1 Xaa-Pro aminopeptidase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417384.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A1V2GG45
    Conserved Domains (1) summary
    PRK10879
    Location:4 → 441
    PRK10879; proline aminopeptidase P II; Provisional
Nucleotide Protein
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