Cytosol aminopeptidase - Escherichia coli (strain K12)

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P68767 (AMPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 71. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytosol aminopeptidase
EC=3.4.11.1

Alternative name(s):
Aminopeptidase A/I
Leucine aminopeptidase
Short name=LAP
EC=3.4.11.10
Leucyl aminopeptidase

Gene names

Name:	pepA
Synonyms:	carP, xerB
Ordered Locus Names:	b4260, JW4217

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. HAMAP MF_00181
Catalytic activity	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. HAMAP MF_00181 Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
Cofactor	Binds 2 manganese ions per subunit By similarity. HAMAP MF_00181
Enzyme regulation	Inhibited by zinc and EDTA. HAMAP MF_00181
Subunit structure	Homohexamer.
Sequence similarities	Belongs to the peptidase M17 family.
Caution	The ligation for manganese is based on the ligation for zinc, an inhibitor, in the crystallographic structure reported in Ref.7. The ligation for manganese in the active form of the enzyme may differ.

Ontologies

Keywords
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	peptide catabolic process Inferred from mutant phenotype. Source: EcoliWiki plasmid recombination Inferred from mutant phenotype Ref.1. Source: EcoliWiki proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	DNA binding Inferred from direct assay Ref.2. Source: EcoliWiki aminopeptidase activity Inferred from direct assay Ref.1. Source: EcoliWiki manganese ion binding Inferred from electronic annotation. Source: InterPro metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 503

503

Cytosol aminopeptidase HAMAP MF_00181

PRO_0000165750

Sites

Active site

282

Potential

Active site

356

Potential

Metal binding

270

Manganese 2 Probable

Metal binding

275

Manganese 1 Probable

Metal binding

275

Manganese 2 Probable

Metal binding

293

Manganese 2 Probable

Metal binding

352

Manganese 1 Probable

Metal binding

354

Manganese 1 Probable

Metal binding

354

Manganese 2 Probable

Experimental info

Mutagenesis

354

E → A: Loss of activity. Ref.6

Secondary structure

503

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P68767 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 643DED17EAC44DCD
Show »

FASTA

503

54,880

        10         20         30         40         50         60 
MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG ELEGKPGQTL 

        70         80         90        100        110        120 
LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL NDTGSMEAVC FLTELHVKGR 

       130        140        150        160        170        180 
NNYWKVRQAV ETAKETLYSF DQLKTNKSEP RRPLRKMVFN VPTRRELTSG ERAIQHGLAI 

       190        200        210        220        230        240 
AAGIKAAKDL GNMPPNICNA AYLASQARQL ADSYSKNVIT RVIGEQQMKE LGMHSYLAVG 

       250        260        270        280        290        300 
QGSQNESLMS VIEYKGNASE DARPIVLVGK GLTFDSGGIS IKPSEGMDEM KYDMCGAAAV 

       310        320        330        340        350        360 
YGVMRMVAEL QLPINVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN TDAEGRLVLC 

       370        380        390        400        410        420 
DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMANHN PLAHELIAAS EQSGDRAWRL 

       430        440        450        460        470        480 
PLGDEYQEQL ESNFADMANI GGRPGGAITA GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG 

       490        500 
ATGRPVALLA QFLLNRAGFN GEE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2670557] [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: 7616564] [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: 7610040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 8057849] [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: 10449417] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

APECA. S04462.

RefSeq

NP_418681.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GYT	X-ray	2.50	A/B/C/D/E/F/G/H/I/J/K/L	1-503	[»]

ProteinModelPortal

P68767.

SMR

P68767. Positions 1-503.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47860N.

IntAct

P68767. 5 interactions.

Protein family/group databases

MEROPS

M17.003.

Proteomic databases

PRIDE

P68767.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001584; EBESCP00000001584; EBESCG00000001312.
EBESCT00000017905; EBESCP00000017196; EBESCG00000016961.

GeneID

948791.

GenomeReviews

Gene locus JW4217 in contig AP009048_GR.
Gene locus b4260 in contig U00096_GR.

KEGG

ecj:JW4217.
eco:b4260.

PATRIC

32124091. VBIEscCol129921_4390.

Organism-specific databases

EchoBASE

EB0688.

EcoGene

EG10694. pepA.

Phylogenomic databases

eggNOG

COG0260.

GeneTree

EBGT00050000011358.

HOGENOM

HBG742580.

OMA

NSGLMST.

PhylomeDB

P68767.

ProtClustDB

PRK00913.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10694-MONOMER.
MetaCyc:EG10694-MONOMER.

Gene expression databases

Genevestigator

P68767.

Family and domain databases

HAMAP

MF_00181. Cytosol_peptidase_M17.
[Tree]

InterPro

IPR011356. Peptidase_M17.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_cytosol_amino.
IPR008283. Peptidase_M17_N.
[Graphical view]

K01255.

PANTHER

PTHR11963:SF3. Peptidase_M17. 1 hit.

Pfam

PF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]

PRINTS

PR00481. LAMNOPPTDASE.

PROSITE

PS00631. CYTOSOL_AP. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AMPA_ECOLI

Accession

Primary (citable) accession number: P68767
Secondary accession number(s): P11648, Q2M649

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	December 21, 2004
Last modified:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

UniProtKB/Swiss-Prot annotation

A primer on UniProtKB/Swiss-Prot annotation

Peptidase families

Classification of peptidase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents