ID A0A1F6HR09_9BACT Unreviewed; 359 AA.
AC A0A1F6HR09;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=A2776_02830 {ECO:0000313|EMBL:OGH12771.1};
OS Candidatus Levybacteria bacterium RIFCSPHIGHO2_01_FULL_40_10.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1798593 {ECO:0000313|EMBL:OGH12771.1, ECO:0000313|Proteomes:UP000177290};
RN [1] {ECO:0000313|EMBL:OGH12771.1, ECO:0000313|Proteomes:UP000177290}
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:OGH12771.1}.
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DR EMBL; MFNQ01000021; OGH12771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6HR09; -.
DR STRING; 1798593.A2776_02830; -.
DR Proteomes; UP000177290; 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 166..264
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 66
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; 39501 MW; 28A86F4BF906980C CRC64;
MIKKARLIKT FIDLVKIDSP SEHEDEIAKN LLSRLKKLGA KTDTDSYGNV FGFFEGIGDP
FMLNSHMDTV EPGRGIKPQI KGDRIYSDGN TILGGDAKAG LTIILEALTS LVESGKKHIP
INVVFTRGEE SGLFGAINLN YGKLRAKQGI TFDGDDDVSN VDISSPGYDR VDVTITGRGA
HAGAEPERGI SAIKIASEII SKLKLGRIDF ETTANIGLIS GGSARNAVPE TVHFKGEVRS
RDRKKLEKHT RHFEDVINNT MNKYPDASVN LVLEREFNPY RFEEQHPVID KIKKAFSELK
IKPNLHETGG GSDVNIFHNH GLQSIVVGIG DYEAHTTREY VVISQMVQAA EFCEKIVLA
//