MUTS2_BACHK
ID MUTS2_BACHK Reviewed; 786 AA.
AC Q6HCX6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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};
GN OrderedLocusNames=BT9727_4285;
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; AE017355; AAT60888.1; -; Genomic_DNA.
DR RefSeq; WP_000893750.1; NC_005957.1.
DR RefSeq; YP_038600.1; NC_005957.1.
DR AlphaFoldDB; Q6HCX6; -.
DR SMR; Q6HCX6; -.
DR EnsemblBacteria; AAT60888; AAT60888; BT9727_4285.
DR KEGG; btk:BT9727_4285; -.
DR PATRIC; fig|281309.8.peg.4567; -.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR Proteomes; UP000001301; 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.
FT CHAIN 1..786
FT /note="Endonuclease MutS2"
FT /id="PRO_1000075471"
FT DOMAIN 711..786
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 786 AA; 88209 MW; 26765371D2AE9CE7 CRC64;
MLERTLRVLE YNKVKEQLLE HTASSLGRDK VKNLVPSTDF EEIVEMQDTT DEAAKVIRLK
GSAPLGGITD IRSNVKRAKI GSMLSPNELL DIANTMYGSR NMKRFIEDMV DNGVELPILE
THVAQIVSLY DLEKKITNCI GDGGEVVDSA SDKLRGIRTQ IRTAESRIRE KLENMTRSSN
SQKMLSDSIV TIRNERYVIP VKQEYRGVYG GIVHDQSASG QTLFIEPQVI VELNNALQEA
RVKEKQEIER ILLMLTEEVA VEADIVLSNV EVVANLDFIF AKAFYAKRIK ATKPIVNNER
YMDLRQARHP LIDPEVIVPN NIMLGKDFTT IVITGPNTGG KTVTLKTVGI CVLMAQSGLH
IPVMDESEIC VFKNIFADIG DEQSIEQSLS TFSSHMVNIV DILEKADFES LVLFDELGAG
TDPQEGAALA ISILDEVCNR GARVVATTHY PELKAYGYNR EQVINASVEF DVNTLSPTYK
LLIGVPGRSN AFEISKRLGL SDRVIDQARN HISTDTNKIE NMIAKLEESQ KNAERDWNEA
EALRKQSEKL HRELQRQIIE FNEERDERLL KAQKEGEEKV EAAKKEAEGI IQELRQLRKA
QLANVKDHEL IEAKSRLEGA APELVKKQKV NVKNTAPKQQ LRAGDEVKVL TFGQKGQLLE
KVSDTEWSVQ IGILKMKVKE SNMEYINTPK QTEKKAVATV KGRDYHVSLE LDLRGERFEN
AMARVEKYLD DAQLASYPRV SIIHGKGTGA LRQGVQDYLK KHRGVKTFRY GDMGEGGLGV
TVVELK