Cytosol aminopeptidase - Escherichia coli O157:H7

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P68768 (AMPA_ECO57)

Last modified November 3, 2009. Version 33. History...

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

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

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

Hide | Top

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:	Z5872, ECs5237

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

Hide | Top

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 By similarity.
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 By similarity.
Subunit structure	Homohexamer By similarity.
Sequence similarities	Belongs to the peptidase M17 family.

Hide | Top

Ontologies

Keywords
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome
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...

Hide | Top

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_0000165752

Sites

Active site

282

Potential

Active site

356

Potential

Metal binding

270

Manganese 2 By similarity

Metal binding

275

Manganese 1 By similarity

Metal binding

275

Manganese 2 By similarity

Metal binding

293

Manganese 2 By similarity

Metal binding

352

Manganese 1 By similarity

Metal binding

354

Manganese 1 By similarity

Metal binding

354

Manganese 2 By similarity

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P68768-1 [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

Hide | Top

References

[1]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] 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: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases
	AE005174 Genomic DNA. Translation: AAG59459.1. BA000007 Genomic DNA. Translation: BAB38660.1.
PIR	E91283. G86124.
RefSeq	NP_290893.1. NP_313264.1.
3D structure databases
SMR	P68768. Positions 1-503.
ModBase	Search...
Proteomic databases
PRIDE	P68768.
Genome annotation databases
GeneID	913804. 959777.
GenomeReviews	Gene locus Z5872 in contig AE005174_GR. Gene locus ECs5237 in contig BA000007_GR.
KEGG	ece:Z5872. ecs:ECs5237.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P68768.
OMA	LGHHNSG
Enzyme and pathway databases
BioCyc	ECOL83334:ECS5237-MON.
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...

Hide | Top

Entry information

Entry name

AMPA_ECO57

Accession

Primary (citable) accession number: P68768
Secondary accession number(s): P11648

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	December 21, 2004
Last modified:	November 3, 2009
This is version 33 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)

Hide | Top

Relevant documents

UniProtKB/Swiss-Prot annotation

A primer on UniProtKB/Swiss-Prot annotation

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents