ID A0A1G1CKS8_9BACT Unreviewed; 359 AA.
AC A0A1G1CKS8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=A2W24_07070 {ECO:0000313|EMBL:OGV95629.1};
OS Microgenomates group bacterium RBG_16_45_19.
OC Bacteria.
OX NCBI_TaxID=1817747 {ECO:0000313|EMBL:OGV95629.1, ECO:0000313|Proteomes:UP000178440};
RN [1] {ECO:0000313|EMBL:OGV95629.1, ECO:0000313|Proteomes:UP000178440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV95629.1}.
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DR EMBL; MHDC01000045; OGV95629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1CKS8; -.
DR STRING; 1817747.A2W24_07070; -.
DR Proteomes; UP000178440; 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; 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.
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 168..259
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 359 AA; 38569 MW; 299DC557F35319C7 CRC64;
MKEAIERTFR ELAAFNSPSK NEVRVASYLQ EQLTTMGLEV KVDDFGNVIG YLSGRGESIL
LNAHMDGVPP AKGHIPVKEG DVLRSDGSTN LRADDIAGIT IILEATITII EGKKKHPPLV
LAFTAQEEIG LWGAKALDVT EYDVNQGIVF DNAFGAGTVV SKGACYVAFD VEIKGKETHP
GKDLSQGVNA VKVLLDTGIQ VGEADKGQTR VNIGTVSAGK ARNVVPGNAT IQGEIRSFLT
GDKLSGRLSE VEMAFKNAAS RNGAQVEFTQ KQLAFAYKVD EDEPLVQKYK EVVGARGGEF
EMAETFVASD ANALREKGLK VFVISTGVES EHSVNETVKL SDMEQLTSDL VALLELLPQ
//