ID AMPA_HAEIN Reviewed; 491 AA. AC P45334; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 28-JAN-2026, entry version 143. DE RecName: Full=Cytosol aminopeptidase; DE EC=3.4.11.1; DE AltName: Full=Leucine aminopeptidase; DE Short=LAP; DE EC=3.4.11.10; DE AltName: Full=Leucyl aminopeptidase; GN Name=pepA; OrderedLocusNames=HI_1705; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Presumably involved in the processing and regular turnover of CC intracellular proteins. Catalyzes the removal of unsubstituted N- CC terminal amino acids from various peptides (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa CC is preferably Leu, but may be other amino acids including Pro CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and CC methyl esters are also readily hydrolyzed, but rates on arylamides CC are exceedingly low.; EC=3.4.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal amino acid, preferentially leucine, CC but not glutamic or aspartic acids.; EC=3.4.11.10; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42023; AAC23351.1; -; Genomic_DNA. DR PIR; C64137; C64137. DR AlphaFoldDB; P45334; -. DR SMR; P45334; -. DR STRING; 71421.HI_1705; -. DR MEROPS; M17.003; -. DR EnsemblBacteria; AAC23351; AAC23351; HI_1705. DR KEGG; hin:HI_1705; -. DR PATRIC; fig|71421.8.peg.1784; -. DR eggNOG; COG0260; Bacteria. DR HOGENOM; CLU_013734_2_2_6; -. DR OrthoDB; 9809354at2; -. DR PhylomeDB; P45334; -. DR BioCyc; HINF71421:G1GJ1-1721-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004177; F:aminopeptidase activity; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR CDD; cd00433; Peptidase_M17; 1. DR FunFam; 3.40.630.10:FF:000004; Probable cytosol aminopeptidase; 1. DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1. DR InterPro; IPR011356; Leucine_aapep/pepB. DR InterPro; IPR043472; Macro_dom-like. DR InterPro; IPR000819; Peptidase_M17_C. DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept. DR InterPro; IPR008283; Peptidase_M17_N. DR NCBIfam; NF002073; PRK00913.1-2; 1. DR NCBIfam; NF002074; PRK00913.1-4; 1. DR NCBIfam; NF002077; PRK00913.2-4; 1. DR PANTHER; PTHR11963:SF23; CYTOSOL AMINOPEPTIDASE; 1. DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1. DR Pfam; PF00883; Peptidase_M17; 1. DR Pfam; PF02789; Peptidase_M17_N; 1. DR PRINTS; PR00481; LAMNOPPTDASE. DR SUPFAM; SSF52949; Macro domain-like; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR PROSITE; PS00631; CYTOSOL_AP; 1. PE 3: Inferred from homology; KW Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease; KW Reference proteome. FT CHAIN 1..491 FT /note="Cytosol aminopeptidase" FT /id="PRO_0000165758" FT ACT_SITE 275 FT /evidence="ECO:0000255" FT ACT_SITE 349 FT /evidence="ECO:0000255" FT BINDING 263 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 268 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 268 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 286 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 345 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 347 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 347 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 491 AA; 53529 MW; 71376DDB1B0076EB CRC64; MKYQAKNTAL SQATDCIVLG VYENNKFSKS FNEIDQLTQG YLNDLVKSGE LTGKLAQTVL LRDLQGLSAK RLLIVGCGKK GELTERQYKQ IIQAVLKTLK ETNTREVISY LTEIELKDRD LYWNIRFAIE TIEHTNYQFD HFKSQKAETS VLESFIFNTD CAQAQQAISH ANAISSGIKA ARDIANMPPN ICNPAYLAEQ AKNLAENSTA LSLKVVDEEE MAKLGMNAYL AVSKGSENRA YMSVLTFNNA PDKNAKPIVL VGKGLTFDAG GISLKPAADM DEMKYDMCGA ASVFGTMKTI AQLNLPLNVI GVLAGCENLP DGNAYRPGDI LTTMNGLTVE VLNTDAEGRL VLCDTLTYVE RFEPELVIDV ATLTGACVVA LGQHNSGLVS TDNNLANALL QAATETTDKA WRLPLSEEYQ EQLKSPFADL ANIGGRWGGA ITAGAFLSNF TKKYRWAHLD IAGTAWLQGA NKGATGRPVS LLTQFLINQV K //