Cytosol aminopeptidase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P68767 (AMPA_ECOLI)

Last modified November 24, 2009. Version 50. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Cytosol aminopeptidase
    EC=3.4.11.1
Alternative name(s):
    Leucine aminopeptidase
      Short name=LAP
    Leucyl aminopeptidase
    Aminopeptidase A/I

Gene names

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

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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
Cofactor	Binds 2 manganese ions per subunit By similarity.
Enzyme regulation	Inhibited by zinc and EDTA. HAMAP MF_00181
Subunit structure	Homohexamer. HAMAP MF_00181
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.

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Ontologies

Keywords
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: HAMAP metalloexopeptidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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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...

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Sequences

Sequence

Length

Mass (Da)

Tools

P68767-1 [UniParc].

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

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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).

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Cross-references

Sequence databases

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

AP_004756.1.
NP_418681.1.

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P68767.

Protein family/group databases

MEROPS

M17.003.

Proteomic databases

PRIDE

P68767.

Genome annotation databases

GeneID

948791.

GenomeReviews

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

KEGG

ecj:JW4217.
eco:b4260.

Organism-specific databases

EchoBASE

EB0688.

EcoGene

EG10694. pepA.

CMR

Search...

Phylogenomic databases

HOGENOM

P68767.

OMA

LGHHNSG

Enzyme and pathway databases

BioCyc

EcoCyc:EG10694-MON.
ECOL168927:B4260-MON.

Gene expression databases

Genevestigator

P68767.

Family and domain databases

HAMAP

MF_00181.
[Tree]

InterPro

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

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...

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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:	November 24, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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