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Database: UniProt
Entry: A0A1F6HR09_9BACT
LinkDB: A0A1F6HR09_9BACT
Original site: A0A1F6HR09_9BACT 
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
//
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