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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

Probably involved in the processing and regular turnover of intracellular proteins (PubMed:20067529). 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 (PubMed:8057849).1 Publication1 Publication

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)DescriptionActionsGraphical viewLength
Metal bindingi270Manganese 2Curated1
Metal bindingi275Manganese 1Curated1
Metal bindingi275Manganese 2Curated1
Active sitei282Sequence analysis1
Metal bindingi293Manganese 2Curated1
Metal bindingi352Manganese 1Curated1
Metal bindingi354Manganese 1Curated1
Metal bindingi354Manganese 2Curated1
Active sitei356Sequence analysis1

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
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10694. pepA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

A quadruple peptidase disruption (pepA, pepB, pepD and pepN) does not grow in M9 minimal medium, grows better when supplemented with casamino acids (PubMed:20067529).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi354E → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001657501 – 503Cytosol aminopeptidaseAdd BLAST503

Proteomic databases

EPDiP68767.
PaxDbiP68767.
PRIDEiP68767.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

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

Structurei

Secondary structure

1503
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi10 – 12Combined sources3
Beta strandi18 – 23Combined sources6
Turni24 – 26Combined sources3
Helixi30 – 36Combined sources7
Beta strandi39 – 41Combined sources3
Helixi42 – 49Combined sources8
Beta strandi59 – 64Combined sources6
Beta strandi69 – 77Combined sources9
Helixi86 – 102Combined sources17
Beta strandi106 – 110Combined sources5
Helixi112 – 114Combined sources3
Helixi122 – 137Combined sources16
Beta strandi156 – 160Combined sources5
Helixi164 – 166Combined sources3
Helixi167 – 192Combined sources26
Turni195 – 197Combined sources3
Helixi200 – 213Combined sources14
Turni214 – 217Combined sources4
Beta strandi218 – 223Combined sources6
Helixi225 – 230Combined sources6
Helixi234 – 241Combined sources8
Beta strandi243 – 245Combined sources3
Beta strandi248 – 255Combined sources8
Beta strandi265 – 275Combined sources11
Helixi287 – 294Combined sources8
Helixi295 – 310Combined sources16
Beta strandi313 – 325Combined sources13
Beta strandi337 – 339Combined sources3
Beta strandi345 – 347Combined sources3
Helixi355 – 365Combined sources11
Helixi366 – 369Combined sources4
Beta strandi372 – 378Combined sources7
Helixi382 – 388Combined sources7
Turni389 – 391Combined sources3
Beta strandi392 – 398Combined sources7
Helixi400 – 413Combined sources14
Beta strandi417 – 419Combined sources3
Helixi424 – 427Combined sources4
Helixi428 – 430Combined sources3
Beta strandi433 – 439Combined sources7
Helixi446 – 455Combined sources10
Beta strandi463 – 467Combined sources5
Turni469 – 471Combined sources3
Beta strandi472 – 474Combined sources3
Helixi476 – 478Combined sources3
Helixi486 – 496Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GYTX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-503[»]
ProteinModelPortaliP68767.
SMRiP68767.
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.
PhylomeDBiP68767.

Family and domain databases

CDDicd00433. Peptidase_M17. 1 hit.
HAMAPiMF_00181. Cytosol_peptidase_M17. 1 hit.
InterProiIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PANTHERiPTHR11963. PTHR11963. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GYTX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-503[»]
ProteinModelPortaliP68767.
SMRiP68767.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262726. 7 interactors.
DIPiDIP-47860N.
IntActiP68767. 5 interactors.
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.
PhylomeDBiP68767.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP68767.
PROiP68767.

Family and domain databases

CDDicd00433. Peptidase_M17. 1 hit.
HAMAPiMF_00181. Cytosol_peptidase_M17. 1 hit.
InterProiIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PANTHERiPTHR11963. PTHR11963. 1 hit.
PfamiPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSiPR00481. LAMNOPPTDASE.
PROSITEiPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 107 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.