MUTS2_BACLD
ID MUTS2_BACLD Reviewed; 785 AA.
AC Q65GE2; Q62RU8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=BLi03005, BL00333;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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; CP000002; AAU24512.1; -; Genomic_DNA.
DR EMBL; AE017333; AAU41872.1; -; Genomic_DNA.
DR RefSeq; WP_011198179.1; NC_006322.1.
DR AlphaFoldDB; Q65GE2; -.
DR SMR; Q65GE2; -.
DR STRING; 279010.BL00333; -.
DR EnsemblBacteria; AAU24512; AAU24512; BL00333.
DR KEGG; bld:BLi03005; -.
DR KEGG; bli:BL00333; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR BioCyc; BLIC279010:BLI_RS14865-MON; -.
DR Proteomes; UP000000606; 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..785
FT /note="Endonuclease MutS2"
FT /id="PRO_1000075472"
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; 87398 MW; 044DFB5EC4D56F17 CRC64;
MQQKALSALE FHKVKEQLTE HAASSLGKEM LLELKPSRSL EEVKKLQEEV DEAGTVLRLK
GSAPFGGLTD IRKALRRAEI GSILSPAELT EISGLLYAAK QMKHFLEGLF EDGVEIPYLH
QYAEKLIPLS ELERDINSCI DDHGEVLDHA SETLRGIRTQ LRTLESRIRD RLESMLRSSS
AQKMLSDTII TIRNDRFVIP VKQEYRSSYG GIVHDQSSSG ATLFIEPQAI VDMNNALRQA
KVNEKQEIER ILRVLTEKTA EHTNELFHDV KVLQTLDFIF AKAKYAKATK AVKPAVNADG
YVRLIQARHP LLPLDEVVPN DIELGGEYTT IVITGPNTGG KTVTLKTLGL LTMMAQSGLH
VPAEEGSETA VFDQVFADIG DEQSIEQSLS TFSSHMVNIV DILKDMTENS LVLFDELGAG
TDPQEGAALA ISILDEVCQT GARVIATTHY PELKAYGYNR ENVINASVEF DIDTLSPTYK
LLIGVPGRSN AFEISKRLGL PDYLIGRAKA EMTAEHNEVD TMIASLEDSK KRAEAELKET
EAIRAEAEAL HRDLQQQISE WQEKKDKLYE EAEQKAAEKV KAAMKEADDI IQSLRMIKED
HKAFKDHELI EAKKRLEEAV PSFEKAKKPA QKKTDKRELK PGDEVKVLTF GQKGTLLEKT
GAAEWNVQIG ILKMKVKEKD LEFLKSAPEP EKQKTIAAVK GKDYHVSLEL DLRGERFENA
LHRVEKYLDD AVLAGYPRVS IIHGKGTGAL RKGVQDLLKS HRNVKNSRFG EAGEGGSGVT
IVELK
