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Database: UniProt
Entry: A0A368XEG3_9BACI
LinkDB: A0A368XEG3_9BACI
Original site: A0A368XEG3_9BACI 
ID   A0A368XEG3_9BACI        Unreviewed;       782 AA.
AC   A0A368XEG3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Endonuclease MutS2 {ECO:0000256|HAMAP-Rule:MF_00092};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00092};
GN   Name=mutS2 {ECO:0000256|HAMAP-Rule:MF_00092};
GN   ORFNames=DFR57_10969 {ECO:0000313|EMBL:RCW66352.1};
OS   Saliterribacillus persicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Saliterribacillus.
OX   NCBI_TaxID=930114 {ECO:0000313|EMBL:RCW66352.1, ECO:0000313|Proteomes:UP000252585};
RN   [1] {ECO:0000313|EMBL:RCW66352.1, ECO:0000313|Proteomes:UP000252585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27696 {ECO:0000313|EMBL:RCW66352.1,
RC   ECO:0000313|Proteomes:UP000252585};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endonuclease that is involved in the suppression of
CC       homologous recombination and may therefore have a key role in the
CC       control of bacterial genetic diversity. {ECO:0000256|HAMAP-
CC       Rule:MF_00092}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00092}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00092}.
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:RCW66352.1}.
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DR   EMBL; QPJJ01000009; RCW66352.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368XEG3; -.
DR   OrthoDB; 9808166at2; -.
DR   Proteomes; UP000252585; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IEA:InterPro.
DR   CDD; cd03280; ABC_MutS2; 1.
DR   Gene3D; 3.30.1370.110; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00092; MutS2; 1.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR046893; MSSS.
DR   InterPro; IPR005747; MutS2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002625; Smr_dom.
DR   InterPro; IPR036063; Smr_dom_sf.
DR   NCBIfam; TIGR01069; mutS2; 1.
DR   PANTHER; PTHR48378:SF1; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR48378; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF20297; MSSS; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   Pfam; PF01713; Smr; 1.
DR   PIRSF; PIRSF005814; MutS_YshD; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SMART; SM00463; SMR; 1.
DR   SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF160443; SMR domain-like; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR   PROSITE; PS50828; SMR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00092}; Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00092};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00092}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00092};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00092};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00092}; Reference proteome {ECO:0000313|Proteomes:UP000252585}.
FT   DOMAIN          707..782
FT                   /note="Smr"
FT                   /evidence="ECO:0000259|PROSITE:PS50828"
FT   COILED          226..261
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          533..600
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         331..338
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   782 AA;  87837 MW;  BE13F93239E1A434 CRC64;
     MNERIFKVLE FDKIIQRLNQ LTASSLGEEK TRRLKPLTDL NEVEKNHLET DEAVSVLRLK
     GHIPLGGIVD IKPMIKRAVI GGILNANECL DVAGTIYGGR QLKLFIEQME EPELPIIREM
     IDAIVTLPEL ERMIKNAIDD HGHVMDGASD QLRSLRSRIR SNQSRIRDRM DNITKSKSKM
     LSDTIVTIRN DRFVLPVKQE YRMAIGGIVH DQSASGQTLF MEPQAVVELN NELQSLRVKE
     KQEVEKILRD LTIAIAEQEE QLSSNVEILG SVDFIFARGK LSEQMKARKP KMNDQGIIKM
     MQARHPLLNE DEVVANDIEL GESYTSIVIT GPNTGGKTVT LKMVGLCTLM AQSGLQIPAQ
     DGCQLSLFNE VYADIGDEQS IEQSLSTFSS HMTNIVKILK EVDEKTLVLF DELGAGTDPQ
     EGAALAMSIL DYVVDKKARV IATTHYPELK AYGYNRENVV NASVEFDIQT LKPTYRLLIG
     VPGRSNAFEI SRRLGLDEAV IAQAKMQVGT DSKDVENMIA SLEASRRGAD NDYVEAHQIL
     EEAEYLRNEL KDQLDKLDQK KEMVLKKAEE KAEKALAKAK EEAEQIVNEL KSRKEDINFK
     DHEWIETKKL LEESQPKLTK KTPDKAETAP TPKTKELKVG DEVKLLSLDQ KATILEKTGK
     NEFQIQVGIM KMKAKRKDLL FLNRTQDKIE QPLTTMRGQA YHVKPELDLR GERYEDALQQ
     LEKYIDDAIL ANYTTVSIIH GKGTGALRQG VKTFARKHSR INAAKDGGMN EGGSGVTVLE
     LK
//
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