ID   MUTS2_SYNY3             Reviewed;         822 AA.
AC   P73625;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 141.
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}; Synonyms=mutSB;
GN   OrderedLocusNames=sll1772;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA17670.1; -; Genomic_DNA.
DR   PIR; S77112; S77112.
DR   AlphaFoldDB; P73625; -.
DR   SMR; P73625; -.
DR   DIP; DIP-48807N; -.
DR   IntAct; P73625; 4.
DR   STRING; 1148.1652751; -.
DR   PaxDb; P73625; -.
DR   EnsemblBacteria; BAA17670; BAA17670; BAA17670.
DR   KEGG; syn:sll1772; -.
DR   eggNOG; COG1193; Bacteria.
DR   InParanoid; P73625; -.
DR   OMA; IHAIIND; -.
DR   PhylomeDB; P73625; -.
DR   Proteomes; UP000001425; 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: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   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; 2.
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..822
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_0000115237"
FT   DOMAIN          749..822
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   REGION          707..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..731
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         348..355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   822 AA;  90670 MW;  78AE7942F777F721 CRC64;
     MSDSTNLTIA EETLALLEWP RLCQHLSTFT QTPLGAIAAR YLLPPSQWEE SRELLAQTQA
     VESIENSPES NWHFKGIADI TEPLARVERG GLVTGLELLA IAGTLAGVRR LRRVIEERDD
     LEILQTLVAE VRTLPELEQA IHHCLGEDGK VAERASPKLG EIRQKLKAVR EQIQQKLQKI
     IQRQSNALQE AVITQRGDRF VLPIKAGYKE QMPGIVHDSS ASGNTLYVEP QAIVELGNKL
     RQARRQEQTE EERILRQLSD QVLEVLLDLE HLLAIATRLD LATARVRYSF WLGAHPPQWL
     TPGDEKPITL RQLRHPLLHW QAEKEGGPAV VPITLTIDSQ IRVIAITGPN TGGKTVTLKT
     LGLVALMAKV GLYIPAKETV EMPWFAQILA DIGDEQSLQQ NLSTFSGHIC RIIRILQALP
     SGVQDVLDPE IDSPNHPIFP SLVLLDEVGA GTDPTEGSAL AIALLRHLAD QPCLTVATTH
     YGELKALKYQ DARFENASVE FDDQSLSPTY RLLWGIPGRS NALAIAQRLG LPLAIVEQAK
     DKLGGFSEDI NQVIAGLESQ RREQEQKAAN AQKLLQETEI FYQQVSQKAA SLQARERELK
     SYQDQEVQQA IAAAKEEIAK VIRQLQRGKP SAQKAQQATE ILGQIQAEQK AKVAPKPIGY
     QPTVGERIRI PSFGQTAEVT QVNATAQTVN VTLGLMKMTV PMADIESLNG KKVEPPPKSE
     PVPKKVKAEP PATEAKSPPV LVRTEKNTLD CRGDRLERAE SRLEKALNQA LDAGVLWIIH
     GKGTGKLRQG VQEYLSHHPL VKSYALAPQN DGGAGVTIAY LR