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MUTS2_ALKCK
ID   MUTS2_ALKCK             Reviewed;         787 AA.
AC   Q5WEK0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Endonuclease MutS2 {ECO:0000255|HAMAP-Rule:MF_00092};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00092};
GN   Name=mutS2 {ECO:0000255|HAMAP-Rule:MF_00092}; OrderedLocusNames=ABC2675;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) 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:0000255|HAMAP-
CC       Rule:MF_00092}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00092}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00092}.
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DR   EMBL; AP006627; BAD65210.1; -; Genomic_DNA.
DR   RefSeq; WP_011247518.1; NC_006582.1.
DR   AlphaFoldDB; Q5WEK0; -.
DR   SMR; Q5WEK0; -.
DR   STRING; 66692.ABC2675; -.
DR   EnsemblBacteria; BAD65210; BAD65210; ABC2675.
DR   KEGG; bcl:ABC2675; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor 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; -; 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; IPR005747; MutS2.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002625; Smr_dom.
DR   InterPro; IPR036063; Smr_dom_sf.
DR   PANTHER; PTHR11361; PTHR11361; 1.
DR   PANTHER; PTHR11361:SF14; PTHR11361:SF14; 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; SSF160443; SSF160443; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01069; mutS2; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR   PROSITE; PS50828; SMR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..787
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000075473"
FT   DOMAIN          712..787
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         335..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   787 AA;  87167 MW;  6D25A992D74AC1E8 CRC64;
     MERVQRVLEY NKMKQQLLEH VASSLGRQKV NELVPSTSLE EVRHLQDETA EAANVLRLKG
     HVPLGGISDV RPHIKRAAIG GVLSATELIE IASTLYGGKR VKQFIETIIE DGHIEVPILA
     GHVEQIEPLS PIEKAIKQCI DDNGYVLDSA STSLRTVRHQ IRSYESGIKS KLDQLTRSSN
     TRKMLSDAIV TIRSDRYVLP VKQEYRGTFG GIVHDQSSSG ATLFIEPAAI VTLNNQLTEA
     KAKEKREIER ILRELSAKVA EESEQLLLNV DKLAQLDFIC AKAYYAKAVK AVKPTLNDRG
     YLDLRQARHP LLPPDKVVPS DMAIGDQVRS LVITGPNTGG KTVTLKTIGL LTLMAQSGLF
     VPAAEETELA VFEHIFADIG DEQSIEQSLS TFSSHMKNIV SILNEMNENS LILFDELGAG
     TDPTEGAALA ISILDHVYKR GALAVATTHY SELKGYAYNR EGALNASVEF DVETLRPTYR
     LLVGVPGRSN AFAISRRLGL DERIIDQAKL QIDSDASQVE KMIASLEDSQ KSAQSEWSRA
     EAVRREAEAL KRDLEKRMAS FEEMKEAALQ KAEQKAEKVV AAAQENAELI ISELRDLQKQ
     GVAVKEHQLI EARKQLEEAA PKLVSKKRKQ VKKQAEKAKR LPEPGDEVKV LSFNQKGTVV
     KKIGDNEYQV QLGIMKMAVP IDDIQLLEQE RRQPEKAITT IRGNDAHVKA ELDLRGERYE
     DAMRRVEKYI DDALLAGYHQ VSIIHGKGTG ALRKGVKQFV ANHPRVKSAR DGGMNEGGLG
     NTVIELK
 
 
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