P45334 (AMPA_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
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:	HI_1705

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	491 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 Reference 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 – 491	491	Cytosol aminopeptidase HAMAP MF_00181		PRO_0000165758
Sites
	Active site	275	1	Potential
	Active site	349	1	Potential
	Metal binding	263	1	Manganese 2 By similarity
	Metal binding	268	1	Manganese 1 By similarity
	Metal binding	268	1	Manganese 2 By similarity
	Metal binding	286	1	Manganese 2 By similarity
	Metal binding	345	1	Manganese 1 By similarity
	Metal binding	347	1	Manganese 1 By similarity
	Metal binding	347	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45334 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 71376DDB1B0076EB	FASTA	491	53,529
	10 20 30 40 50 60 MKYQAKNTAL SQATDCIVLG VYENNKFSKS FNEIDQLTQG YLNDLVKSGE LTGKLAQTVL 70 80 90 100 110 120 LRDLQGLSAK RLLIVGCGKK GELTERQYKQ IIQAVLKTLK ETNTREVISY LTEIELKDRD 130 140 150 160 170 180 LYWNIRFAIE TIEHTNYQFD HFKSQKAETS VLESFIFNTD CAQAQQAISH ANAISSGIKA 190 200 210 220 230 240 ARDIANMPPN ICNPAYLAEQ AKNLAENSTA LSLKVVDEEE MAKLGMNAYL AVSKGSENRA 250 260 270 280 290 300 YMSVLTFNNA PDKNAKPIVL VGKGLTFDAG GISLKPAADM DEMKYDMCGA ASVFGTMKTI 310 320 330 340 350 360 AQLNLPLNVI GVLAGCENLP DGNAYRPGDI LTTMNGLTVE VLNTDAEGRL VLCDTLTYVE 370 380 390 400 410 420 RFEPELVIDV ATLTGACVVA LGQHNSGLVS TDNNLANALL QAATETTDKA WRLPLSEEYQ 430 440 450 460 470 480 EQLKSPFADL ANIGGRWGGA ITAGAFLSNF TKKYRWAHLD IAGTAWLQGA NKGATGRPVS 490 LLTQFLINQV K

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC23351.1.
PIR	C64137.
RefSeq	NP_439847.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P45334.
SMR	P45334. Positions 1-490.
ModBase	Search...
Protein family/group databases
MEROPS	M17.003.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	949712.
GenomeReviews	Gene locus HI_1705 in contig L42023_GR.
KEGG	hin:HI1705.
NMPDR	fig|71421.1.peg.1618.
PATRIC	20192161. VBIHaeInf48452_1784.
TIGR	HI_1705.
Phylogenomic databases
HOGENOM	HBG742580.
OMA	KYDWAHL.
ProtClustDB	PRK00913.
Enzyme and pathway databases
BioCyc	HINF71421:HI_1705-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_HAEIN

Accession

Primary (citable) accession number: P45334

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program