ID A0A075LK38_9BACI Unreviewed; 375 AA.
AC A0A075LK38;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=GZ22_08770 {ECO:0000313|EMBL:AIF66719.1};
OS Terribacillus goriensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Terribacillus.
OX NCBI_TaxID=386490 {ECO:0000313|EMBL:AIF66719.1, ECO:0000313|Proteomes:UP000027980};
RN [1] {ECO:0000313|EMBL:AIF66719.1, ECO:0000313|Proteomes:UP000027980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP602 {ECO:0000313|EMBL:AIF66719.1,
RC ECO:0000313|Proteomes:UP000027980};
RA Wang Y., Lu P., Zhang L.;
RT "Complete genome sequence of a moderately halophilic bacterium
RT Terribacillus aidingensis MP602, isolated from Cryptomeria fortunei in
RT Tianmu mountain in China.";
RL Submitted (JUL-2014) 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}.
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DR EMBL; CP008876; AIF66719.1; -; Genomic_DNA.
DR RefSeq; WP_038561091.1; NZ_CP008876.1.
DR AlphaFoldDB; A0A075LK38; -.
DR MEROPS; M20.018; -.
DR KEGG; tap:GZ22_08770; -.
DR HOGENOM; CLU_021802_6_0_9; -.
DR OrthoDB; 9776600at2; -.
DR Proteomes; UP000027980; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 NCBIfam; TIGR01883; PepT-like; 1.
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 PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000027980}.
FT DOMAIN 186..275
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 375 AA; 40025 MW; D77E2201294EB049 CRC64;
MIKVNENRLV EEFFELVKVD SETGNEKEIS EVLKRKFTEL GVKVQEDDSM GKTGHGANNL
ICTWEGEVET AETIYFTSHM DTVVPGQGIK PQIKDGYITS DGTTILGADD KAGLAAILET
IKVYNEQNLQ HGTVQFIITA GEESGLVGSR ALDPSLLTAS FGYAIDSDGP VGDIVVAAPT
QAKVLAKIYG KTAHAGVAPE KGISAITLAA RAISKMPLGR IDEETTANIG SFAGGKQTNI
VCDYVEILAE ARSLETGKME EQVEKMKRAF EQTAEDMGGR AEVEVKVMYP GYKQQAGDRV
VEVARAAAKT IGRDSNLTRS GGGSDANVIA GFGIPTVNLS VGYEEIHTTN ERIPVAELVK
TAELVAAIIR EVANS
//
