ID A0A0J1DP86_9FIRM Unreviewed; 372 AA.
AC A0A0J1DP86;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Peptidase M20 {ECO:0000313|EMBL:KLU40758.1};
GN ORFNames=AA931_04280 {ECO:0000313|EMBL:KLU40758.1};
OS Peptococcaceae bacterium 1109.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1655638 {ECO:0000313|EMBL:KLU40758.1, ECO:0000313|Proteomes:UP000036486};
RN [1] {ECO:0000313|EMBL:KLU40758.1, ECO:0000313|Proteomes:UP000036486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1109 {ECO:0000313|EMBL:KLU40758.1};
RA Town J.R., Dumonceaux T.J.;
RL Submitted (MAY-2015) 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 -!- 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:KLU40758.1}.
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DR EMBL; LDJB01000001; KLU40758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1DP86; -.
DR STRING; 1655638.AA931_04280; -.
DR PATRIC; fig|1655638.3.peg.860; -.
DR Proteomes; UP000036486; 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 Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}.
FT DOMAIN 181..275
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; 38877 MW; AC0ECC6AFFF5D63B CRC64;
MTVNDSRLVA EFLELVQIDS APKDERKMAD ALLGKLQALG FDAQEDETGE KIGGNAGNVC
AFLDGDPNLP ALLFSAHMDR VSPGYGIKPI VEDGRIRSDG TTILAADDVA GICAILEGIR
IIQEQNIPHG RIEVVFTVAE EGGLFGAKNL DTTPFKAQAG FFLDSTGPVG TIIVQAPAQK
SLKVKIHGRS AHAGVAPEEG INAIVVAAKA ISSMKLGRID PETTANIGVI RGGAATNIVP
DLVELEGEAR SRNEASLEAQ TAHMVEALQA ACAEYGAEAE INVTHSYSAY HMKPEDYVVQ
LAVKASQGIG VEPIQQGTGG GSDANIINSR GIPSVVLGLG YENIHSTAES IPVSQLVKAA
ELVVSIIQAS GR
//
