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Protein

Cytosol aminopeptidase

Gene

pepA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Required for plasmid ColE1 site-specific recombination but not in its aminopeptidase activity. Could act as a structural component of the putative nucleoprotein complex in which the Xer recombination reaction takes place.

Catalytic activityi

Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Enzyme regulationi

Inhibited by zinc and EDTA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi270 – 2701Manganese 2Curated
Metal bindingi275 – 2751Manganese 1Curated
Metal bindingi275 – 2751Manganese 2Curated
Active sitei282 – 2821Sequence analysis
Metal bindingi293 – 2931Manganese 2Curated
Metal bindingi352 – 3521Manganese 1Curated
Metal bindingi354 – 3541Manganese 1Curated
Metal bindingi354 – 3541Manganese 2Curated
Active sitei356 – 3561Sequence analysis

GO - Molecular functioni

  • aminopeptidase activity Source: EcoliWiki
  • DNA binding Source: EcoliWiki
  • manganese ion binding Source: UniProtKB-HAMAP
  • metalloexopeptidase activity Source: UniProtKB-HAMAP
  • transcription antitermination factor activity, DNA binding Source: EcoliWiki

GO - Biological processi

  • negative regulation of transcription, DNA-templated Source: EcoCyc
  • peptide catabolic process Source: EcoliWiki
  • plasmid maintenance Source: EcoliWiki
  • plasmid recombination Source: EcoliWiki
  • transcription, DNA-templated Source: EcoCyc
  • transcription antitermination Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10694-MONOMER.
ECOL316407:JW4217-MONOMER.
MetaCyc:EG10694-MONOMER.

Protein family/group databases

MEROPSiM17.003.
MoonProtiP68767.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosol aminopeptidase (EC:3.4.11.1)
Alternative name(s):
Aminopeptidase A/I
Leucine aminopeptidase (EC:3.4.11.10)
Short name:
LAP
Leucyl aminopeptidase
Gene namesi
Name:pepA
Synonyms:carP, xerB
Ordered Locus Names:b4260, JW4217
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10694. pepA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi354 – 3541E → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503Cytosol aminopeptidasePRO_0000165750Add
BLAST

Proteomic databases

EPDiP68767.
PaxDbiP68767.
PRIDEiP68767.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi4262726. 7 interactions.
DIPiDIP-47860N.
IntActiP68767. 5 interactions.
STRINGi511145.b4260.

Structurei

Secondary structure

1
503
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi10 – 123Combined sources
Beta strandi18 – 236Combined sources
Turni24 – 263Combined sources
Helixi30 – 367Combined sources
Beta strandi39 – 413Combined sources
Helixi42 – 498Combined sources
Beta strandi59 – 646Combined sources
Beta strandi69 – 779Combined sources
Helixi86 – 10217Combined sources
Beta strandi106 – 1105Combined sources
Helixi112 – 1143Combined sources
Helixi122 – 13716Combined sources
Beta strandi156 – 1605Combined sources
Helixi164 – 1663Combined sources
Helixi167 – 19226Combined sources
Turni195 – 1973Combined sources
Helixi200 – 21314Combined sources
Turni214 – 2174Combined sources
Beta strandi218 – 2236Combined sources
Helixi225 – 2306Combined sources
Helixi234 – 2418Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi248 – 2558Combined sources
Beta strandi265 – 27511Combined sources
Helixi287 – 2948Combined sources
Helixi295 – 31016Combined sources
Beta strandi313 – 32513Combined sources
Beta strandi337 – 3393Combined sources
Beta strandi345 – 3473Combined sources
Helixi355 – 36511Combined sources
Helixi366 – 3694Combined sources
Beta strandi372 – 3787Combined sources
Helixi382 – 3887Combined sources
Turni389 – 3913Combined sources
Beta strandi392 – 3987Combined sources
Helixi400 – 41314Combined sources
Beta strandi417 – 4193Combined sources
Helixi424 – 4274Combined sources
Helixi428 – 4303Combined sources
Beta strandi433 – 4397Combined sources
Helixi446 – 45510Combined sources
Beta strandi463 – 4675Combined sources
Turni469 – 4713Combined sources
Beta strandi472 – 4743Combined sources
Helixi476 – 4783Combined sources
Helixi486 – 49611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYTX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-503[»]
ProteinModelPortaliP68767.
SMRiP68767. Positions 1-503.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68767.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M17 family.Curated

Phylogenomic databases

eggNOGiENOG4105BZ6. Bacteria.
COG0260. LUCA.
HOGENOMiHOG000243132.
InParanoidiP68767.
KOiK01255.
OMAiAICEMKL.
OrthoDBiEOG6FV8B3.
PhylomeDBiP68767.

Family and domain databases

HAMAPiMF_00181. Cytosol_peptidase_M17.
InterProiIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PfamiPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSiPR00481. LAMNOPPTDASE.
PROSITEiPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P68767-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG
60 70 80 90 100
ELEGKPGQTL LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL
110 120 130 140 150
NDTGSMEAVC FLTELHVKGR NNYWKVRQAV ETAKETLYSF DQLKTNKSEP
160 170 180 190 200
RRPLRKMVFN VPTRRELTSG ERAIQHGLAI AAGIKAAKDL GNMPPNICNA
210 220 230 240 250
AYLASQARQL ADSYSKNVIT RVIGEQQMKE LGMHSYLAVG QGSQNESLMS
260 270 280 290 300
VIEYKGNASE DARPIVLVGK GLTFDSGGIS IKPSEGMDEM KYDMCGAAAV
310 320 330 340 350
YGVMRMVAEL QLPINVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN
360 370 380 390 400
TDAEGRLVLC DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMANHN
410 420 430 440 450
PLAHELIAAS EQSGDRAWRL PLGDEYQEQL ESNFADMANI GGRPGGAITA
460 470 480 490 500
GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG ATGRPVALLA QFLLNRAGFN

GEE
Length:503
Mass (Da):54,880
Last modified:December 21, 2004 - v1
Checksum:i643DED17EAC44DCD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15130 Genomic DNA. Translation: CAA33225.1.
X86443 Genomic DNA. Translation: CAA60164.1.
U14003 Genomic DNA. Translation: AAA97157.1.
U00096 Genomic DNA. Translation: AAC77217.1.
AP009048 Genomic DNA. Translation: BAE78257.1.
PIRiS04462. APECA.
RefSeqiNP_418681.1. NC_000913.3.
WP_000397144.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77217; AAC77217; b4260.
BAE78257; BAE78257; BAE78257.
GeneIDi948791.
KEGGiecj:JW4217.
eco:b4260.
PATRICi32124091. VBIEscCol129921_4390.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15130 Genomic DNA. Translation: CAA33225.1.
X86443 Genomic DNA. Translation: CAA60164.1.
U14003 Genomic DNA. Translation: AAA97157.1.
U00096 Genomic DNA. Translation: AAC77217.1.
AP009048 Genomic DNA. Translation: BAE78257.1.
PIRiS04462. APECA.
RefSeqiNP_418681.1. NC_000913.3.
WP_000397144.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYTX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-503[»]
ProteinModelPortaliP68767.
SMRiP68767. Positions 1-503.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262726. 7 interactions.
DIPiDIP-47860N.
IntActiP68767. 5 interactions.
STRINGi511145.b4260.

Protein family/group databases

MEROPSiM17.003.
MoonProtiP68767.

Proteomic databases

EPDiP68767.
PaxDbiP68767.
PRIDEiP68767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77217; AAC77217; b4260.
BAE78257; BAE78257; BAE78257.
GeneIDi948791.
KEGGiecj:JW4217.
eco:b4260.
PATRICi32124091. VBIEscCol129921_4390.

Organism-specific databases

EchoBASEiEB0688.
EcoGeneiEG10694. pepA.

Phylogenomic databases

eggNOGiENOG4105BZ6. Bacteria.
COG0260. LUCA.
HOGENOMiHOG000243132.
InParanoidiP68767.
KOiK01255.
OMAiAICEMKL.
OrthoDBiEOG6FV8B3.
PhylomeDBiP68767.

Enzyme and pathway databases

BioCyciEcoCyc:EG10694-MONOMER.
ECOL316407:JW4217-MONOMER.
MetaCyc:EG10694-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP68767.
PROiP68767.

Family and domain databases

HAMAPiMF_00181. Cytosol_peptidase_M17.
InterProiIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PfamiPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSiPR00481. LAMNOPPTDASE.
PROSITEiPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Stirling C.J., Colloms S., Collins J.F., Szatmari G., Sherratt D.J.
    EMBO J. 8:1623-1627(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20.
    Strain: K12.
  2. "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., Hassanzadeh G., Kholti A., Gigot D., Pierard A., Glansdorff N.
    J. Mol. Biol. 250:392-406(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Peptidase activity of Escherichia coli aminopeptidase A is not required for its role in Xer site-specific recombination."
    McCulloch R., Burke M.E., Sherratt D.J.
    Mol. Microbiol. 12:241-251(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-354.
  7. "X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination."
    Strater N., Sherratt D.J., Colloms S.D.
    EMBO J. 18:4513-4522(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Entry informationi

Entry nameiAMPA_ECOLI
AccessioniPrimary (citable) accession number: P68767
Secondary accession number(s): P11648, Q2M649
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: March 16, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The ligation for manganese is based on the ligation for zinc, an inhibitor, in the crystallographic structure reported in PubMed:10449417. The ligation for manganese in the active form of the enzyme may differ.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.