ID   MUTS2_LISMC             Reviewed;         785 AA.
AC   C1L2D7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Lm4b_01237;
OS   Listeria monocytogenes serotype 4b (strain CLIP80459).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=568819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIP80459;
RX   PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA   Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA   Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA   Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA   Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT   "Comparative genomics and transcriptomics of lineages I, II, and III
RT   strains of Listeria monocytogenes.";
RL   BMC Genomics 13:144-144(2012).
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; FM242711; CAS05003.1; -; Genomic_DNA.
DR   RefSeq; WP_003726543.1; NC_012488.1.
DR   AlphaFoldDB; C1L2D7; -.
DR   SMR; C1L2D7; -.
DR   KEGG; lmc:Lm4b_01237; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   BioCyc; LMON568819:LM4B_RS06170-MON; -.
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.
FT   CHAIN           1..785
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000202683"
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;  86569 MW;  AEAE1C437A04E7E6 CRC64;
     MEKKVEAILE FDKIKKQLTE FASSSLGEQA ILELAPATDF QVVQKTQLET EEGAKIIRLR
     GSAPITGLTD VFAHLKRLEI GGDLNGLEIY QIGSNLRVSR QMKNFMNDLL EIGVELPLLG
     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 SILGNVNQKS LILYDELGAG
     TDPQEGAALA IAILDASHAK GASVVATTHY PELKAYGYNR VHATNASVEF NVETLSPTYK
     LLIGVPGRSN AFDISRRLGL SENIITEARS LVDTESADLN DMISSLEEKR NLAETEYEEA
     RELARGADNL LKDLQKEISN YYQQKDKLIE QASEKAATIV EKAEAEAEEI IHELRTMQLN
     GAAGIKEHEL IDAKTRLGNA KPKTINKTIP QAPKQKPHVF QEGDNVRVLS LGQKGTLLNK
     ISDKEWNVQI GIIKMKIKTT DLEYIQPEKP KKQRIITSVH SSGSPAKSEL DLRGERYEDA
     LQKVDKYLDE ALLAGYPQVA IIHGKGTGAL RTGVTEYLKN HRMVKSIRFG AAAEGGNGVT
     IVEFK