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pepA aminopeptidase A/I [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948791, updated on 25-Jun-2025
Official Symbol
pepA
Official Full Name
aminopeptidase A/I
Primary source
ECOCYC:EG10694
Locus tag
b4260
See related
ASAP:ABE-0013953
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
carP; ECK4253; xerB
Summary
PepA has a broad specificity for successive removal of many N-terminal amino acids, although leucine is preferred as the residue N-terminal to the cleavage site. [More information is available at EcoGene: EG10694]. Aminopeptidase A/I is a peptidase that binds DNA and is required for maintenance of plasmid monomers, which is critical for proper plasmid segregation . [More information is available at EcoCyc: EG10694].
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Sequence:
NC_000913.3 (4484440..4485951, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene valine--tRNA ligase Neighboring gene DNA polymerase III subunit chi Neighboring gene protein YtgB Neighboring gene protein YtgA

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Insights into the architecture and stoichiometry of Escherichia coli PepA*DNA complexes involved in transcriptional control and site-specific DNA recombination by atomic force microscopy. Minh PN, et al. Nucleic Acids Res, 2009 Apr. PMID 19136463, Free PMC Article
  2. carP, a novel gene regulating the transcription of the carbamoylphosphate synthetase operon of Escherichia coli. Roovers M, et al. J Mol Biol, 1988 Dec 20. PMID 3065518
  3. 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. Charlier D, et al. J Mol Biol, 1995 Jul 21. PMID 7616564
  4. X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination. Sträter N, et al. EMBO J, 1999 Aug 16. PMID 10449417, Free PMC Article
  5. A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase. Sträter N, et al. Proc Natl Acad Sci U S A, 1999 Sep 28. PMID 10500145, Free PMC Article

See all (41) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. in vitro topology studies performed with DNA minicircles demonstrate that PepA binding constrains a single positive supercoil in the carP1 control region. Such a topological event is understood to constitute an impediment to transcription initiation and may serve as a mechanism to regulate gene expression.
    Title: The trigger enzyme PepA (aminopeptidase A) of Escherichia coli, a transcriptional repressor that generates positive supercoiling.
  2. Data show that PepA can effectively process heptapeptide-nucleotide microcin C (McC).
    Title: Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C.
  3. N-terminus verified by Edman degradation on complete protein
    Title: 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.
  4. Random PepA mutants unable to support efficient Xer recombination are reported.
    Title: Mutagenesis of PepA suggests a new model for the Xer/cer synaptic complex.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables DNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
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 transcription antitermination factor activity, DNA binding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within DNA-templated transcription IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within DNA-templated transcription IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within peptide catabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within plasmid maintenance IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within plasmid recombination IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in proteolysis IBA
Inferred from Biological aspect of Ancestor
more info
  
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
Preferred Names
aminopeptidase A/I
NP_418681.1

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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
    4484440..4485951 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418681.1 aminopeptidase A/I [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_418681.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A5B9ALR5, A0A6C9QGK6, Q7X4V5
    Conserved Domains (1) summary
    PRK00913
    Location:1 → 495
    PRK00913; multifunctional aminopeptidase A; Provisional
Nucleotide Protein
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