ID A0A0H3N0Q1_MYCLB Unreviewed; 443 AA. AC A0A0H3N0Q1; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 22-FEB-2023, entry version 27. DE RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467}; DE EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467}; GN Name=pepC {ECO:0000313|EMBL:CAR72310.1}; GN Synonyms=apeB {ECO:0000256|HAMAP-Rule:MF_00467}; GN OrderedLocusNames=MLBr02213 {ECO:0000313|EMBL:CAR72310.1}; OS Mycobacterium leprae (strain Br4923). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=561304 {ECO:0000313|EMBL:CAR72310.1, ECO:0000313|Proteomes:UP000006900}; RN [1] {ECO:0000313|EMBL:CAR72310.1, ECO:0000313|Proteomes:UP000006900} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Br4923 {ECO:0000313|Proteomes:UP000006900}; RX PubMed=19881526; DOI=10.1038/ng.477; RA Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A., RA Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C., RA Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H., RA Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R., RA Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A., RA Rougemont J., Brennan P.J., Cole S.T.; RT "Comparative genomic and phylogeographic analysis of Mycobacterium RT leprae."; RL Nat. Genet. 41:1282-1289(2009). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947, CC ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004387}; CC -!- SIMILARITY: Belongs to the peptidase M18 family. CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|HAMAP-Rule:MF_00467, CC ECO:0000256|RuleBase:RU004386}. 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; FM211192; CAR72310.1; -; Genomic_DNA. DR RefSeq; WP_010908772.1; NC_011896.1. DR AlphaFoldDB; A0A0H3N0Q1; -. DR SMR; A0A0H3N0Q1; -. DR EnsemblBacteria; CAR72310; CAR72310; MLBr02213. DR KEGG; mlb:MLBr02213; -. DR HOGENOM; CLU_019532_2_0_11; -. DR OMA; GPILKVN; -. DR Proteomes; UP000006900; Chromosome. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule. DR CDD; cd05658; M18_DAP; 1. DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR HAMAP; MF_00467; Aminopeptidase_M18_2; 1. DR InterPro; IPR022984; M18_aminopeptidase_2. DR InterPro; IPR001948; Peptidase_M18. DR InterPro; IPR023358; Peptidase_M18_dom2. DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1. DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1. DR Pfam; PF02127; Peptidase_M18; 1. DR PRINTS; PR00932; AMINO1PTASE. DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. PE 3: Inferred from homology; KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP- KW Rule:MF_00467}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00467}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00467}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP- KW Rule:MF_00467}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00467}; KW Signal {ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00467}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..443 FT /note="Probable M18 family aminopeptidase 2" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002616066" FT BINDING 96 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467" FT BINDING 173 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467" FT BINDING 416 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00467" SQ SEQUENCE 443 AA; 47273 MW; D559DDAFFAD87AD3 CRC64; MPTLASTTSS PTAMMLGMPA SAADLCEFIN ASPSPFHVCA TVAGRLLDAG YAELSEVERW PDHPGRYFIV RAGSLVAWSA GQGVKAHAPF RIVGAHTDSP NLRVKQHPDL LVAGWRVVAL QPYGGAWLNS WLDRDLGVSG RLSVRSAGKG SEITDRLVRI DDPILRVPQL AIHLAEDRKS LTLDPQRHVN AVWGVGDKAG SLLEYVAERT GVAVADVLAV DLMTHDLVPS MVIGADANLL SAPRLDNQVS CYAGMEALLA SVPHDCLPVL ALFDHEEVGS TSDRGARSNL LSTVLERIVL AAGGGRDDYL RRLPASLLVS ADMAHATHPN YPECHEPSHL IEVNAGPVLK VHPNLRYATD GRTAAAFEVA CQQAGVRLQR YEHRADRPCG STIGPLASAR TGIPTVDVGA AQLAMHSARE LMGAHDVAVY SAALQAFFSA DLF //