ID AMPA_BURM9 Reviewed; 503 AA. AC A2SAC2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 1. DT 02-SEP-2026, entry version 90. 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}; GN OrderedLocusNames=BMA10229_A2947; OS Burkholderia mallei (strain NCTC 10229). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=412022; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 10229; RX PubMed=20333227; DOI=10.1093/gbe/evq003; RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S., RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J., RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P., RA Nierman W.C.; RT "Continuing evolution of Burkholderia mallei through genome reduction and RT large-scale rearrangements."; RL Genome Biol. Evol. 2:102-116(2010). 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; Evidence={ECO:0000255|HAMAP- CC 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; CP000546; ABN01268.1; -; Genomic_DNA. DR RefSeq; WP_004191270.1; NC_008836.1. DR AlphaFoldDB; A2SAC2; -. DR SMR; A2SAC2; -. DR MEROPS; M17.003; -. DR GeneID; 92978435; -. DR KEGG; bml:BMA10229_A2947; -. DR HOGENOM; CLU_013734_2_2_4; -. 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:InterPro. 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 NCBIfam; NF002083; PRK00913.3-5; 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. FT CHAIN 1..503 FT /note="Probable cytosol aminopeptidase" FT /id="PRO_1000019893" FT ACT_SITE 286 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT ACT_SITE 360 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 274 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 279 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 279 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 297 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 356 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 358 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 358 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" SQ SEQUENCE 503 AA; 52681 MW; 71EEB720D60B5ACE CRC64; MDFSIKGCDW SKGTANGFLT GKSDCIVLGV FEAQTLSGAA LDIDEATKGL VSRVIKAGDI DGKLGKTLFL HEVSGIGASR VLLVGLGRQD AFSQKAYGDA AKVAWRALLG TKVVQVTFTL AQLPVPERAS DWGVRAAILA LRNETYKFTQ MKSKPDAGAP ALKRVVFSVD PADDKAAKVA AKQAVALANG MDLTRDLGNL PGNVCTPTYL ANTAKKIAKD WGLKVDVLGL KQIQALKMGS FLSVAKGSVE PPQFIVLQYR GAAAKAAPVV LVGKGITFDS GGISLKPGEG MDEMKYDMCG AGSVLGTMRA VAEMGLKVNV VAIVPTCENM PAGNANKPGD IVTSMKGLTI EVLNTDAEGR LILCDALTYA ERFKPAAVID VATLTGACII ALGHHNTGLF SKDDALAGEL LDASREAGDP AWRLPLDDEY QDQLKSNFAD LANIGGRPAG SVTAACFLSR FAENYPWAHL DIAGTAWKSG AAKGATGRPV PLLAQFLIDR AGA //