ID AMPA_LEGPC Reviewed; 483 AA. AC A5IAU5; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 1. DT 22-FEB-2023, entry version 81. DE RecName: Full=Probable cytosol aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181}; DE EC=3.4.11.1 {ECO:0000255|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181}; DE Short=LAP {ECO:0000255|HAMAP-Rule:MF_00181}; DE EC=3.4.11.10 {ECO:0000255|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181}; GN Name=pepA {ECO:0000255|HAMAP-Rule:MF_00181}; OrderedLocusNames=LPC_0510; OS Legionella pneumophila (strain Corby). OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Legionellaceae; Legionella. OX NCBI_TaxID=400673; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Corby; RA Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., RA Steinert M., Buchrieser C., Hacker J., Heuner K.; RT "Identification and characterization of a new conjugation/ type IVA RT secretion system (trb/tra) of L. pneumophila Corby localized on a mobile RT genomic island."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000255|HAMAP- CC Rule:MF_00181}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00181}; 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00181}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}. CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000255|HAMAP- CC Rule:MF_00181}. 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; CP000675; ABQ54495.1; -; Genomic_DNA. DR RefSeq; WP_011947549.1; NC_009494.2. DR AlphaFoldDB; A5IAU5; -. DR SMR; A5IAU5; -. DR MEROPS; M17.003; -. DR KEGG; lpc:LPC_0510; -. DR HOGENOM; CLU_013734_0_1_6; -. DR OMA; MKNTGPR; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; IEA:UniProtKB-KW. DR CDD; cd00433; Peptidase_M17; 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 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. FT CHAIN 1..483 FT /note="Probable cytosol aminopeptidase" FT /id="PRO_1000203833" FT ACT_SITE 264 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT ACT_SITE 338 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 252 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 257 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 257 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 275 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 334 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 336 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 336 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" SQ SEQUENCE 483 AA; 52613 MW; 695CC2F46D38ACE6 CRC64; MNYGLTHTPS LTMSECLVLG VFSDLALPDF ATAIDNEQKG LIKKLCQRVP EPGNTVWQTD VEGHSLLIIQ CGKKEEFSAN SLQKRVGEIT EALIKQRFSS ATVCLPRLNQ ESAEWQLEQM IVQIDNLRYQ LLDFKTKHAK SHKLESVIFH LPGATEKSLE MAKAIVTGVE FCRDLANMPA NICTPTYLGE QAISLSKQFD QISCQVMGPE EIKEMGMGAL LAVAQGSDQP PRLIDIHYHG NKNSTPVILV GKGITFDSGG LSIKPANAMD EMKYDMSGAA SVLGVIKACA LLKLPINLIG IIASAENLIS GSAVKSGDIV TTMSGQTVEI INTDAEGRLV LADALTYAER YNPDFVIDIA TLTGAIIVAL GNIATGYMTR DEQLAKSIER AANESQDKVW RMPLDEAYQD ALESPLADMI NAGFDRSAGS ITAACFLSRF TEKYRWAHLD IAGTAWISGK KRNATGRPVP LLIQLLRHVA NSR //