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P68768

- AMPA_ECO57

UniProt

P68768 - AMPA_ECO57

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Protein
Cytosol aminopeptidase
Gene
pepA, carP, xerB, Z5872, ECs5237
Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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 By similarity.UniRule annotation

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.UniRule annotation
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

Cofactori

Binds 2 manganese ions per subunit By similarity.UniRule annotation

Enzyme regulationi

Inhibited by zinc and EDTA By similarity.UniRule annotation

Sites

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

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-HAMAP
  2. manganese ion binding Source: UniProtKB-HAMAP
  3. metalloexopeptidase activity Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciECOL386585:GJFA-5245-MONOMER.
ECOO157:PEPA-MONOMER.

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:Z5872, ECs5237
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503Cytosol aminopeptidaseUniRule annotation
PRO_0000165752Add
BLAST

Proteomic databases

PRIDEiP68768.

Interactioni

Subunit structurei

Homohexamer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi155864.Z5872.

Structurei

3D structure databases

ProteinModelPortaliP68768.
SMRiP68768. Positions 1-503.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M17 family.

Phylogenomic databases

eggNOGiCOG0260.
HOGENOMiHOG000243132.
KOiK01255.
OMAiANEAKMS.
OrthoDBiEOG6FV8B3.

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.

P68768-1 [UniParc]FASTAAdd to Basket

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MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG    50
ELEGKPGQTL LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL 100
NDTGSMEAVC FLTELHVKGR NNYWKVRQAV ETAKETLYSF DQLKTNKSEP 150
RRPLRKMVFN VPTRRELTSG ERAIQHGLAI AAGIKAAKDL GNMPPNICNA 200
AYLASQARQL ADSYSKNVIT RVIGEQQMKE LGMHSYLAVG QGSQNESLMS 250
VIEYKGNASE DARPIVLVGK GLTFDSGGIS IKPSEGMDEM KYDMCGAAAV 300
YGVMRMVAEL QLPINVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN 350
TDAEGRLVLC DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMANHN 400
PLAHELIAAS EQSGDRAWRL PLGDEYQEQL ESNFADMANI GGRPGGAITA 450
GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG ATGRPVALLA QFLLNRAGFN 500
GEE 503
Length:503
Mass (Da):54,880
Last modified:December 21, 2004 - v1
Checksum:i643DED17EAC44DCD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG59459.1.
BA000007 Genomic DNA. Translation: BAB38660.1.
PIRiE91283.
G86124.
RefSeqiNP_290893.1. NC_002655.2.
NP_313264.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG59459; AAG59459; Z5872.
BAB38660; BAB38660; BAB38660.
GeneIDi913804.
959777.
KEGGiece:Z5872.
ecs:ECs5237.
PATRICi18360111. VBIEscCol44059_5188.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG59459.1 .
BA000007 Genomic DNA. Translation: BAB38660.1 .
PIRi E91283.
G86124.
RefSeqi NP_290893.1. NC_002655.2.
NP_313264.1. NC_002695.1.

3D structure databases

ProteinModelPortali P68768.
SMRi P68768. Positions 1-503.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 155864.Z5872.

Proteomic databases

PRIDEi P68768.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG59459 ; AAG59459 ; Z5872 .
BAB38660 ; BAB38660 ; BAB38660 .
GeneIDi 913804.
959777.
KEGGi ece:Z5872.
ecs:ECs5237.
PATRICi 18360111. VBIEscCol44059_5188.

Phylogenomic databases

eggNOGi COG0260.
HOGENOMi HOG000243132.
KOi K01255.
OMAi ANEAKMS.
OrthoDBi EOG6FV8B3.

Enzyme and pathway databases

BioCyci ECOL386585:GJFA-5245-MONOMER.
ECOO157:PEPA-MONOMER.

Family and domain databases

HAMAPi MF_00181. Cytosol_peptidase_M17.
InterProi IPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view ]
Pfami PF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view ]
PRINTSi PR00481. LAMNOPPTDASE.
PROSITEi PS00631. CYTOSOL_AP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiAMPA_ECO57
AccessioniPrimary (citable) accession number: P68768
Secondary accession number(s): P11648
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: June 11, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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