A3N1A7 (AMPA_ACTP2) 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:	APL_1101

Organism

Actinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]

Taxonomic identifier

416269 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	499 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 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
Subcellular location	Cytoplasm By similarity HAMAP MF_00181.
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: UniProtKB-KW 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 – 499	499	Probable cytosol aminopeptidase HAMAP MF_00181		PRO_1000019874
Sites
	Active site	281	1	Potential
	Active site	355	1	Potential
	Metal binding	269	1	Manganese 2 By similarity
	Metal binding	274	1	Manganese 1 By similarity
	Metal binding	274	1	Manganese 2 By similarity
	Metal binding	292	1	Manganese 2 By similarity
	Metal binding	351	1	Manganese 1 By similarity
	Metal binding	353	1	Manganese 1 By similarity
	Metal binding	353	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3N1A7 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 24171F47813D7EE4	FASTA	499	54,219
	10 20 30 40 50 60 MEFSVKNGSV EKQRTACLVV GVYEPRRLSA AAEQLDKLSE GYISTLLRRG DLEGKAGQTL 70 80 90 100 110 120 LLHNVPNVPA DRVLLVGCGK ERELTERQYK QIIQKMVQAV SETGSMEVVC FLTELHVKGR 130 140 150 160 170 180 TSYWNVRFAI EAIQESLYSY NDFKSIKPEV RREFRRVIFN VANRKDLADA ERALEHGKAI 190 200 210 220 230 240 STGVAFAKNV ANCPPNVCNP AYLAELAKGL AAEYDNIRTT VIDEAEMAAL GMNAYLAVSR 250 260 270 280 290 300 GSQNPAYLSV IEYKNHPNPD AKPIVLVGKG LTFDSGGISI KPSDSMDEMK YDMGGAASVY 310 320 330 340 350 360 GTMKALAEMK LPLNVIGVLA GCENMPDGNA YRPGDILTTM NGLTVEVLNT DAEGRLVLCD 370 380 390 400 410 420 TLTYVERFEP ELVIDMATLT GACMIALGAH NSGLMSTSNV LANELLNAAE QADDKAWRLP 430 440 450 460 470 480 LGEEYQEQLK SNFADLANIG GRLGGAITAG QFLSNFTKKY SWAHLDIAGT AWKSGAAKGA 490 TGRPVSLLSQ FLINKANNQ

References

[1]	"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)." Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E. J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: L20.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000569 Genomic DNA. Translation: ABN74193.1.
RefSeq	YP_001053798.1. NC_009053.1.
3D structure databases
ProteinModelPortal	A3N1A7.
SMR	A3N1A7. Positions 1-496.
ModBase	Search...
Protein-protein interaction databases
STRING	A3N1A7.
Protein family/group databases
MEROPS	M17.003.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4848868.
GenomeReviews	Gene locus APL_1101 in contig CP000569_GR.
KEGG	apl:APL_1101.
PATRIC	20747114. VBIActPle94089_1149.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0260.
HOGENOM	HBG742580.
OMA	NSGLMST.
PhylomeDB	A3N1A7.
ProtClustDB	PRK00913.
Enzyme and pathway databases
BioCyc	APLE416269:APL_1101-MONOMER.
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]
KO	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_ACTP2

Accession

Primary (citable) accession number: A3N1A7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	April 3, 2007
Last modified:	December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program