ID   MUTS2_ALKMQ             Reviewed;         789 AA.
AC   A6TNX0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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}; OrderedLocusNames=Amet_1712;
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF;
RX   PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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; CP000724; ABR47888.1; -; Genomic_DNA.
DR   RefSeq; WP_012062926.1; NC_009633.1.
DR   AlphaFoldDB; A6TNX0; -.
DR   SMR; A6TNX0; -.
DR   STRING; 293826.Amet_1712; -.
DR   PRIDE; A6TNX0; -.
DR   EnsemblBacteria; ABR47888; ABR47888; Amet_1712.
DR   KEGG; amt:Amet_1712; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000001572; 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..789
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093338"
FT   DOMAIN          714..789
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   REGION          690..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         334..341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   789 AA;  88575 MW;  167F98D09F152E4A CRC64;
     MNEKSIRVLE YGKMIDRLEE RCLSAMAKEK ARELRPIQSF GEITQLQSET SEAQSILIQR
     GNIPLGGIHD IKQYLRKTEI GSYLDPKELL LVKDTLRTAR NLKSFFKEGD DQTKHPIVSG
     LIQGLQSFRA IEDRIEICIV SDTEISDHAS STLKNIRRQI SSKNDAVRNK LNGIINSSTT
     QKYLQDAIIT MRQDRYVVPV KQEHRGNVPG LIHDQSSSGA TLFVEPMAVV QLNNELRELK
     IKEHIEIERI LMEIAEMIAQ YATEMRNNQI ILTAIDFVFA KGKLSLEMKG VEPLLNVEGN
     VHIKNGRHPL LNADEVVPTN LWIGETFQTL VITGPNTGGK TVTLKTLGLL SMMAQSGLHV
     PADYGTRLAI FDQIFADIGD EQSIEQSLST FSSHMTNIVN IVEEVTSNSL VLFDELGAGT
     DPTEGAALGM AILNHLREMN VTTVATTHYS ELKQYALTNE GVENASVEFD VATLSPTYRL
     LIGVPGKSNA FEISKKLGLP DGLVQRAKRF LSQDTIHFED LLQNIEKNRR ESEIERQEAK
     RIRLEAEKFA EGYEDRKQRL EAQRDQILRD AKKEAYRLVK EAKMDSEHII KGLREMKFEL
     EAKEMNKKME DAKNQLTGKM NDLSDHHQQI LNKKNKKPPK NLKPGDAVRI LSLNQVGHVL
     NEVDPKGEVQ VQAGIMKVNM HISNLERVSP EKDIQQSGTG KIMKSKTGDT KSEVDVRGKN
     LEEAMLEIDK YLDDSYIVGL TQVTIIHGVG TGVLKAGIKQ MLKKNKHVRT HREGVYGEGG
     MGVTIVELK