ID   MUTS_BACSU              Reviewed;         858 AA.
AC   P49849;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=DNA mismatch repair protein MutS;
GN   Name=mutS; OrderedLocusNames=BSU17040;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8760914; DOI=10.1099/13500872-142-8-2021;
RA   Ginetti F., Perego M., Albertini A.M., Galizzi A.;
RT   "Bacillus subtilis mutS mutL operon: identification, nucleotide sequence
RT   and mutagenesis.";
RL   Microbiology 142:2021-2029(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).
RN   [3]
RP   SEQUENCE REVISION TO 480-481.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=12483591; DOI=10.2323/jgam.46.183;
RA   Sasaki M., Yonemura Y., Kurusu Y.;
RT   "Genetic analysis of Bacillus subtilis mutator genes.";
RL   J. Gen. Appl. Microbiol. 46:183-187(2000).
RN   [5]
RP   POSSIBLE ROLE IN STATIONARY-PHASE-INDUCED MUTAGENESIS REPAIR.
RC   STRAIN=168 / YB955;
RX   PubMed=19011023; DOI=10.1128/jb.01210-08;
RA   Vidales L.E., Cardenas L.C., Robleto E., Yasbin R.E., Pedraza-Reyes M.;
RT   "Defects in the error prevention oxidized guanine system potentiate
RT   stationary-phase mutagenesis in Bacillus subtilis.";
RL   J. Bacteriol. 191:506-513(2009).
CC   -!- FUNCTION: This protein is involved in the repair of mismatches in DNA.
CC       It is possible that it carries out the mismatch recognition step. This
CC       protein has a weak ATPase activity (By similarity). Overexpression of
CC       mutSL partially suppresses the high spontaneous mutation frequency of a
CC       ytkD/mutM/mutY triple disruption which lacks the system required to
CC       prevent damage by oxidized guanine (8-oxo-dGTP). This suggests that
CC       MutSL also functions to repair mismatches due to oxidative stress in
CC       both growing and stationary phase cells. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene have a 225-fold increased
CC       spontaneous mutation frequency. Double or triple disruptions with
CC       mutL/nth do not change the frequency. {ECO:0000269|PubMed:12483591}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB19235.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U27343; AAB19235.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB13577.2; -; Genomic_DNA.
DR   PIR; C69663; C69663.
DR   RefSeq; NP_389586.2; NC_000964.3.
DR   RefSeq; WP_003244841.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P49849; -.
DR   SMR; P49849; -.
DR   STRING; 224308.BSU17040; -.
DR   PaxDb; P49849; -.
DR   PRIDE; P49849; -.
DR   EnsemblBacteria; CAB13577; CAB13577; BSU_17040.
DR   GeneID; 939501; -.
DR   KEGG; bsu:BSU17040; -.
DR   PATRIC; fig|224308.179.peg.1845; -.
DR   eggNOG; COG0249; Bacteria.
DR   InParanoid; P49849; -.
DR   OMA; TPMMAQY; -.
DR   PhylomeDB; P49849; -.
DR   BioCyc; BSUB:BSU17040-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0030983; F:mismatched DNA binding; IBA:GO_Central.
DR   GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR   Gene3D; 3.30.420.110; -; 1.
DR   Gene3D; 3.40.1170.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00096; MutS; 1.
DR   InterPro; IPR005748; DNA_mismatch_repair_MutS.
DR   InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR   InterPro; IPR017261; DNA_mismatch_repair_MutS/MSH.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR   InterPro; IPR036678; MutS_con_dom_sf.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11361; PTHR11361; 1.
DR   Pfam; PF01624; MutS_I; 1.
DR   Pfam; PF05188; MutS_II; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF05190; MutS_IV; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53150; SSF53150; 1.
DR   SUPFAM; SSF55271; SSF55271; 1.
DR   TIGRFAMs; TIGR01070; mutS1; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..858
FT                   /note="DNA mismatch repair protein MutS"
FT                   /id="PRO_0000115070"
FT   BINDING         602..609
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        480..481
FT                   /note="KQ -> NE (in Ref. 1; AAB19235)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   858 AA;  97604 MW;  B83E3288CED1F900 CRC64;
     MAGYTPMIQQ YLKIKAEHQD AFLFFRLGDF YEMFFEDAKK ASQELEITLT SRDGGAAEKI
     PMCGVPYHSA SAYIEQLIKK GYKVAICEQT EDPKAAKGVV KREVVQLITP GTVMDGKGIH
     ESENNFIASV SACSNGYGLA LSDLTTGENL AVLIERLEDV ISEIYSVGAR EIVVSGSLDA
     DTVAQLRERC GATISIEDGE TDEHVTIIEH LNNEDITKTF LRLYTYLKRT QKRSLDHLQP
     VQVYELEEAM KIDLYSKRNL ELTETIRSKN KKGSLLWLLD ETKTAMGGRL LKQWIDRPLI
     RVNQIEERQE MVETLMSHFF EREDLRERLK EVYDLERLAG RVAFGNVNAR DLIQLKESLK
     QVPGIKQLVA SLAHDKAKER AKRIDPCGDV LELLEEALYE NPPLSVKEGN LIKDGYNQKL
     DEYRDASRNG KDWIARLEQQ EREYTGIRSL KVGFNKVFGY YIEVTKANLH LLEEGRYERK
     QTLTNAERYI TPELKEKEAL ILEAENNICE LEYELFTELR EKVKQYIPRL QQLAKQMSEL
     DALQCFATIS ENRHYTKPEF SKDEVEVIEG RHPVVEKVMD SQEYVPNNCM MGDNRQMLLI
     TGPNMSGKST YMRQIALISI MAQIGCFVPA KKAVLPIFDQ IFTRIGAADD LISGQSTFMV
     EMLEAKNAIV NATKNSLILF DEIGRGTSTY DGMALAQAII EYVHDHIGAK TLFSTHYHEL
     TVLEDKLPQL KNVHVRAEEY NGTVVFLHQI KEGAADKSYG IHVAQLAELP GDLIARAQDI
     LKELEHSGNK PEVPVQKPQV KEEPAQLSFF DEAEKPAETP KLSKKEKQVI DAFKSLNILD
     MTPLEAMNEM YKLQKKLH