ID A0A1H5W336_9BACI Unreviewed; 372 AA. AC A0A1H5W336; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 03-MAY-2023, entry version 24. DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:SEF93954.1}; GN ORFNames=SAMN04487919_10465 {ECO:0000313|EMBL:SEF93954.1}; OS Bacillus sp. ok061. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1761766 {ECO:0000313|EMBL:SEF93954.1, ECO:0000313|Proteomes:UP000236757}; RN [1] {ECO:0000313|EMBL:SEF93954.1, ECO:0000313|Proteomes:UP000236757} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OK061 {ECO:0000313|EMBL:SEF93954.1, RC ECO:0000313|Proteomes:UP000236757}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2}; CC Note=Binds 2 divalent metal cations per subunit. CC {ECO:0000256|PIRSR:PIRSR001123-2}; CC -!- SIMILARITY: Belongs to the peptidase M42 family. CC {ECO:0000256|PIRNR:PIRNR001123}. 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; FNUW01000004; SEF93954.1; -; Genomic_DNA. DR RefSeq; WP_000609800.1; NZ_FNUW01000004.1. DR AlphaFoldDB; A0A1H5W336; -. DR EnsemblBacteria; SEF93954; SEF93954; SAMN04487919_10465. DR Proteomes; UP000236757; Unassembled WGS sequence. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR CDD; cd05683; M20_peptT_like; 1. DR Gene3D; 3.30.70.360; -; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR InterPro; IPR001261; ArgE/DapE_CS. DR InterPro; IPR036264; Bact_exopeptidase_dim_dom. DR InterPro; IPR010162; PepT-like. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR InterPro; IPR008007; Peptidase_M42. DR PANTHER; PTHR42994; PEPTIDASE T; 1. DR PANTHER; PTHR42994:SF2; T, PUTATIVE-RELATED; 1. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF001123; PepA_GA; 3. DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR TIGRFAMs; TIGR01883; PepT-like; 1. DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1. DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1. PE 3: Inferred from homology; KW Aminopeptidase {ECO:0000313|EMBL:SEF93954.1}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000313|EMBL:SEF93954.1}. FT DOMAIN 182..274 FT /note="Peptidase M20 dimerisation" FT /evidence="ECO:0000259|Pfam:PF07687" FT BINDING 345 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2" SQ SEQUENCE 372 AA; 39618 MW; 21C156E92B191AE1 CRC64; MINQERLVNE FMELVQVDSE TKFEAEICKV LTKKFTDLGV EIFEDDTMAV TGHGAGNLIC TLPATKDGVD TIYFTSHMDT VVPGNGIKPS IKDGYIVSDG TTILGADDKA GLASMFEAIR VLKEKNIPHG KIEFIITVGE ESGLVGAKAL DRERITAKYG YALDSDGKVG EIVVAAPTQA KVNAIIRGKT AHAGVAPEKG VSAITIAAKA IAKMPLGRID SETTANIGRF EGGTQTNIVC DHVQIFAEAR SLINEKMEAQ VAKMKEAFET TAKEMGGHAD VEVNVMYPGF KFADGDHVVE VAKRAAEKIG RTPSLHQSGG GSDANVIAGH GIPTVNLAVG YEEIHTTNEK IPVEELAKTA ELVVAIIEEV AK //