Q0T9D1 (AMPA_ECOL5) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable cytosol aminopeptidase
EC=3.4.11.1

Alternative name(s):
Leucine aminopeptidase
Short name=LAP
EC=3.4.11.10
Leucyl aminopeptidase

Gene names

Name:	pepA
Ordered Locus Names:	ECP_4509

Organism

Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

362663 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity. HAMAP-Rule 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-Rule 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.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the peptidase M17 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 503	503	Probable cytosol aminopeptidase HAMAP-Rule MF_00181		PRO_1000019915
Sites
	Active site	282	1	Potential
	Active site	356	1	Potential
	Metal binding	270	1	Manganese 2 By similarity
	Metal binding	275	1	Manganese 1 By similarity
	Metal binding	275	1	Manganese 2 By similarity
	Metal binding	293	1	Manganese 2 By similarity
	Metal binding	352	1	Manganese 1 By similarity
	Metal binding	354	1	Manganese 1 By similarity
	Metal binding	354	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0T9D1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 643DED17EAC44DCD	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

References

[1]

"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536." Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J. Mol. Microbiol. 61:584-595(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 536 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000247 Genomic DNA. Translation: ABG72448.1.
RefSeq	YP_672349.1. NC_008253.1.
3D structure databases
ProteinModelPortal	Q0T9D1.
SMR	Q0T9D1. Positions 1-503.
ModBase	Search...
Protein-protein interaction databases
STRING	362663.ECP_4509.
Proteomic databases
PRIDE	Q0T9D1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABG72448; ABG72448; ECP_4509.
GeneID	4188573.
KEGG	ecp:ECP_4509.
PATRIC	18199968. VBIEscCol77757_4559.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0260.
HOGENOM	HOG000243132.
KO	K01255.
OMA	LMSVMEY.
PhylomeDB	Q0T9D1.
ProtClustDB	PRK00913.
Enzyme and pathway databases
BioCyc	ECOL362663:GIY5-4551-MONOMER.
Family and domain databases
HAMAP	MF_00181. Cytosol_peptidase_M17.
InterPro	IPR011356. Leucine_aapep/pepB. IPR000819. Peptidase_M17_C. IPR023042. Peptidase_M17_leu_NH2_pept. IPR008283. Peptidase_M17_N. [Graphical view]
PANTHER	PTHR11963:SF3. PTHR11963:SF3. 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_ECOL5

Accession

Primary (citable) accession number: Q0T9D1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program