ID A0A0G0PQI4_9BACT Unreviewed; 350 AA.
AC A0A0G0PQI4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=UT61_C0012G0023 {ECO:0000313|EMBL:KKR30153.1};
OS Candidatus Woesebacteria bacterium GW2011_GWA1_39_8.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618552 {ECO:0000313|EMBL:KKR30153.1, ECO:0000313|Proteomes:UP000034793};
RN [1] {ECO:0000313|EMBL:KKR30153.1, ECO:0000313|Proteomes:UP000034793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKR30153.1}.
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DR EMBL; LBXL01000012; KKR30153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0PQI4; -.
DR Proteomes; UP000034793; 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 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; 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 PROSITE; PS00758; ARGE_DAPE_CPG2_1; 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}.
FT DOMAIN 163..255
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 350 AA; 38142 MW; A414FB5E25EE0D03 CRC64;
MEKVTRTFID LVKIDSPSGE EDGVRKYLIM KLSSLGIKSV TDKVGNLFVK VDGAGEPVLL
SAHMDTVEPG RGIIPKVVNG VVKSDGSTIL GADNKAAVAA ILTVLGNLPD SHRSLEIVFS
VCEETDGGIE SFDFNQLKSK IGIAPDRGSK IGNVVLAAPW IDNFEIEVHG RIVHSSVPEK
GINALTAASR AMVALEWGRP DKETTTNMGI IHGGSVMNSI PSKVDLTGEV RSFSEKSLEK
NIVKIRDTFE KEAKKIGAKI AFRRESYCKG YSYKKTDYSV VYFKKVCDRL KIPLSYEKSF
GGSDANSFIA HGISVLNIGE GSKYPHTLRE QVSEKDLFKL VELIATYITL
//
