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
//
