ID   MUTS2_LISMO             Reviewed;         785 AA.
AC   Q8Y7P1;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=lmo1232;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591978; CAC99310.1; -; Genomic_DNA.
DR   PIR; AH1228; AH1228.
DR   RefSeq; NP_464757.1; NC_003210.1.
DR   RefSeq; WP_010989713.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y7P1; -.
DR   SMR; Q8Y7P1; -.
DR   STRING; 169963.lmo1232; -.
DR   PaxDb; Q8Y7P1; -.
DR   PRIDE; Q8Y7P1; -.
DR   EnsemblBacteria; CAC99310; CAC99310; CAC99310.
DR   GeneID; 986039; -.
DR   KEGG; lmo:lmo1232; -.
DR   PATRIC; fig|169963.11.peg.1263; -.
DR   eggNOG; COG1193; Bacteria.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   PhylomeDB; Q8Y7P1; -.
DR   BioCyc; LMON169963:LMO1232-MON; -.
DR   Proteomes; UP000000817; 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   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_0000115226"
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;  86716 MW;  08FA4F563C77022A CRC64;
     MEKKVEAILE FDKIKKQLTE FASSSLGEQA ILELAPATDF QVVQKTQLET EEGAKIIRLR
     GSAPITGLTD VFAHLKRLEI GGDLNGLEIY QIGSNLRVSR QMKNFMNDLL EIGVELPILG
     ALSDELLVLK EVEEDIAISV DESGKVLDTA SEALSTIRRT LRRTEDRVRE KLESYLRDRN
     ASKMLSDAVI TIRNDRYVIP VKQEYKGHYG GIVHDQSASG QTLFIEPQSV VDLNNERKAL
     QAKEKQEIER ILAEISASLA AWINEIHHNT FILGRFDFIF AKARFGKAMK AVTPHLSDAG
     VVHLIAARHP LLDAAKVVAN DIYLGEDFTT IVITGPNTGG KTITLKTLGL LTLMAQSGLQ
     IPAQEDSTIA VFEHVFADIG DEQSIEQSLS TFSSHMTNIV SILEKVNQKS LILYDELGAG
     TDPQEGAALA IAILDASHEK GASVVATTHY PELKAYGYNR VHATNASVEF NVETLSPTYK
     LLIGVPGRSN AFDISRRLGL SENIITEARS LVDTESADLN DMISSLEEKR NLAETEYEEA
     RELARGADNL LKDLQKEITN YYQQKDKLIE QASEKAATIV EKAEAEAEEI IRELRTMQLN
     GAAGIKEHEL IDAKTRLGNA KPKTINKTIP QAPKQKPHVF QEGDNVRVLS LGQKGTLLNK
     ISDKEWNVQI GIIKMKIKTA DLEYIQPEKP KKQRIITSVH SSGSPAKSEL DLRGERYEDA
     LQKVDKYLDE ALLAGYPQVA IIHGKGTGAL RTGVTEYLKN HRMVKSIRFG AAAEGGNGVT
     IVEFK