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MUTS2_LATSS
ID   MUTS2_LATSS             Reviewed;         787 AA.
AC   Q38YN3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=LCA_0393;
OS   Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei
OS   subsp. sakei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Latilactobacillus.
OX   NCBI_TaxID=314315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=23K;
RX   PubMed=16273110; DOI=10.1038/nbt1160;
RA   Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M.,
RA   Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V.,
RA   Zagorec M.;
RT   "The complete genome sequence of the meat-borne lactic acid bacterium
RT   Lactobacillus sakei 23K.";
RL   Nat. Biotechnol. 23:1527-1533(2005).
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; CR936503; CAI54694.1; -; Genomic_DNA.
DR   RefSeq; WP_011374102.1; NC_007576.1.
DR   AlphaFoldDB; Q38YN3; -.
DR   SMR; Q38YN3; -.
DR   STRING; 314315.LCA_0393; -.
DR   EnsemblBacteria; CAI54694; CAI54694; LCA_0393.
DR   KEGG; lsa:LCA_0393; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
DR   Proteomes; UP000002707; 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   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..787
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093372"
FT   DOMAIN          712..787
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   787 AA;  87609 MW;  76FD33C659020D66 CRC64;
     MNHKILKTLE YDKIKQMLQG YAITAFGQEQ IATLEPINEA DLIQIRLNQT KDGVDIERLK
     GGIPLPQLEN IRPHLKRIEI GAMLNGSELA QIGRVLRATS AVVRFFDDLE KDELELKALP
     ELVAQFVTLP QLTERIRSSV ADDGAILDTA STKLRGLRTG LKQLEGQIRS RMASYTHGAK
     AKYLSDPIVT IRNDRYVIPV KQEYRGQFGG VVHDQSASGQ TLFMEPQAIM ELNNRLRQLQ
     IEEQQEIERI LAELSEAIMP ERHNILANAE LLGQLDFVNA KAQLAKALKA TEPLINAENH
     VDLKQARHPL IDATKVVAND IAIGADYQAI VVTGPNTGGK TITLKTLGLV QVMAQSGLFI
     TAREESQVGV FSDIFADIGD EQSIEQNLST FSAHMENIIQ ILKQIDDRSL VLLDELGAGT
     DPQEGAALAI AILDQIGIVG ANVVASTHYP ELKIYGYNRP QTINASMEFD VATLQPTYRL
     LIGVPGRSNA FDISTRLGLP NSIVDQAKQL MNDESQDLNN MITDLENQRK AAETEYQALR
     HELTEATDLH QQLSTAYQQF FEDRETEMTK AKEKANAIVE KAEVKADKVI TKLRDMQMNQ
     GAQIKENQLI DAKAELGQLH QETTLKKNKV LQRAKRRQTL KVGDDVLVTS YGQRGTLIRQ
     VDSKNWEVQM GIIKMKIAND DLEKQKVVED NRPQRHVTTV NSGGARHVKA QLDLRGKRYE
     EAMAEVDQYI DAALLANYQQ VTIVHGKGTG AIRQGVQEYL QANRQVKKYE YAPANAGGNG
     ATIVTFK
 
 
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