ID   MUTS2_ALKOO             Reviewed;         790 AA.
AC   A8MHU4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Clos_1836;
OS   Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS   OhILAs)).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=350688;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OhILAs;
RA   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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA   Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT   "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000853; ABW19376.1; -; Genomic_DNA.
DR   RefSeq; WP_012159688.1; NC_009922.1.
DR   AlphaFoldDB; A8MHU4; -.
DR   SMR; A8MHU4; -.
DR   STRING; 350688.Clos_1836; -.
DR   EnsemblBacteria; ABW19376; ABW19376; Clos_1836.
DR   KEGG; aoe:Clos_1836; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000000269; 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..790
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093339"
FT   DOMAIN          715..790
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         334..341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   790 AA;  88889 MW;  F70D6F26618DC5B7 CRC64;
     MNERSLRVLE YNKIIHMLED KCTSSLGREK LKELKPISNF EQITTWQKET SEAQSILIHR
     GNIPLGGIHD VSQYLRRTEI GSYLDPGQLL QLKETLAAAR RMKTFLKDDK KESTYPIIQE
     LGNNISSLKH IEDKIELCII SETELSDNAS PELRNIRRQI SSKNDAIRNK LNSIITSASN
     QKYLQDPIIT MRQDRYVVPV KQEHRGNIPG LIHDQSSSGA TIFVEPMAVV ELNNQLKELR
     LKEQVEIERI LMEIAAMIAE RSDDIKSNQI ILKELDFIFA KGKLSVEMRA VEPVLNTNKK
     ISIKNGRHPL LPSNKVVPNT MWLGEDFHTL VITGPNTGGK TVTLKTLGLL TLMAQSGLHV
     PADYGTKLAI FDQVFADIGD EQSIEQSLST FSSHMTNIVN IMDNVTEQSL VLFDELGAGT
     DPTEGAALAM AILNSLREMG TVTVATTHYS ELKQYALSTE GVENASVEFD VNTLSPTYKL
     LIGVPGKSNA FEISRKLGLS DFLIQRSKEL LTREDIQFED LLQNIEKNRS TAEKEKDEAA
     RLRMETQKLR EEYYEKKQQL QTQKEKLISD AKREAYKIVK QAKLDADEIV ENLKTLRAEL
     EEKEMNKKIE EARKNLSDQM GKLAENMGEK LVLKTNKKPP KNLKIGESVN ILSLNQIGYV
     ILPEDANGEV QLQVGIMKVN MHVSNLERIK EEKDTKKTGV GKIVKSKAEN IKMEIDVRGQ
     NLEEAMLNVD KYLDDAYIAG LTHVTIIHGV GTGVLSAGLK QMLKKHKHTK SFREGEYGEG
     GMGVTIVHLK