ID   MUTS2_BACSU             Reviewed;         785 AA.
AC   P94545;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Endonuclease MutS2 {ECO:0000255|HAMAP-Rule:MF_00092};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00092};
GN   Name=mutSB; Synonyms=mutS2, yshD; OrderedLocusNames=BSU28580;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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; Z75208; CAA99569.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14818.1; -; Genomic_DNA.
DR   PIR; D69985; D69985.
DR   RefSeq; NP_390736.1; NC_000964.3.
DR   RefSeq; WP_003229541.1; NZ_JNCM01000036.1.
DR   PDB; 7QV3; EM; 5.14 A; v/w=1-785.
DR   PDBsum; 7QV3; -.
DR   AlphaFoldDB; P94545; -.
DR   EMDB; EMD-14159; -.
DR   SMR; P94545; -.
DR   STRING; 224308.BSU28580; -.
DR   PaxDb; 224308-BSU28580; -.
DR   EnsemblBacteria; CAB14818; CAB14818; BSU_28580.
DR   GeneID; 937447; -.
DR   KEGG; bsu:BSU28580; -.
DR   PATRIC; fig|224308.179.peg.3105; -.
DR   eggNOG; COG1193; Bacteria.
DR   InParanoid; P94545; -.
DR   OrthoDB; 9808166at2; -.
DR   PhylomeDB; P94545; -.
DR   BioCyc; BSUB:BSU28580-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
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   CDD; cd06503; ATP-synt_Fo_b; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..785
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_0000115217"
FT   DOMAIN          710..785
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   785 AA;  87417 MW;  20D14CDB931167C2 CRC64;
     MQQKVLSALE FHKVKEQVIG HAASSLGKEM LLELKPSASI DEIKKQLDEV DEASDIIRLR
     GQAPFGGLVD IRGALRRAEI GSVLSPSEFT EISGLLYAVK QMKHFITQMA EDGVDIPLIH
     QHAEQLITLS DLERDINSCI DDHGEVLDHA SETLRGIRTQ LRTLESRVRD RLESMLRSSS
     ASKMLSDTIV TIRNDRFVIP VKQEYRSSYG GIVHDTSSSG ATLFIEPQAI VDMNNSLQQA
     KVKEKQEIER ILRVLTEKTA EYTEELFLDL QVLQTLDFIF AKARYAKAVK ATKPIMNDTG
     FIRLKKARHP LLPPDQVVAN DIELGRDFST IVITGPNTGG KTVTLKTLGL LTLMAQSGLH
     IPADEGSEAA VFEHVFADIG DEQSIEQSLS TFSSHMVNIV GILEQVNENS LVLFDELGAG
     TDPQEGAALA MSILDDVHRT NARVLATTHY PELKAYGYNR EGVMNASVEF DIETLSPTYK
     LLIGVPGRSN AFEISKRLGL PDHIIGQAKS EMTAEHNEVD TMIASLEQSK KRAEEELSET
     ESIRKEAEKL HKELQQQIIE LNSKKDKMLE EAEQQAAEKV KAAMKEAEDI IHELRTIKEE
     HKSFKDHELI NAKKRLEGAM PAFEKSKKPE KPKTQKRDFK PGDEVKVLTF GQKGTLLEKT
     GGNEWNVQIG ILKMKVKEKD LEFIKSAPEP KKEKMITAVK GKDYHVSLEL DLRGERYENA
     LSRVEKYLDD AVLAGYPRVS IIHGKGTGAL RKGVQDLLKN HRSVKSSRFG EAGEGGSGVT
     VVELK
//