ID   MUTS2_HELPJ             Reviewed;         762 AA.
AC   Q9ZLL4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=jhp_0565;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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; AE001439; AAD06136.1; -; Genomic_DNA.
DR   PIR; H71916; H71916.
DR   AlphaFoldDB; Q9ZLL4; -.
DR   SMR; Q9ZLL4; -.
DR   STRING; 85963.jhp_0565; -.
DR   EnsemblBacteria; AAD06136; AAD06136; jhp_0565.
DR   KEGG; hpj:jhp_0565; -.
DR   eggNOG; COG1193; Bacteria.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000000804; 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; PS50828; SMR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleotide-binding.
FT   CHAIN           1..762
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_0000115223"
FT   DOMAIN          688..762
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   BINDING         333..340
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   762 AA;  86648 MW;  71F2433DB07E7AB5 CRC64;
     MSDASKRSLN PTLMMNNNNT LPKPLEESLD LKEFIALFKT FFAKERGSIA LENDLKQAFT
     YLNEVDAIGL PAPKSVKESD LIVVKLTKLG TLHLDEIYEI VKRLRYIVVL QNAFKPFTHL
     KFHERLNAII LPPFFNDLIL LLDDEGQIKQ GANATLDALN ESLNRLKKES TKIIHHYAHS
     KELAPYLVDT QSHLKHGYEC LLLKSGFSSA IKGVVLERSA NGYFYLLPES AQKIAQKIAQ
     IGNEIDCCIV EMCQTLSRSL QKHLLFLKFL FKEFDFLDSL QARLNFAKAY NLEFVMPSFT
     QKKMILENFS HPILKEPKPL NLKFEKSMLA VTGVNAGGKT MLLKSLLSAA FLSKHLIPMK
     INAHHSTIPY FREIHAIIND PQNSANNIST FAGRMKQFSA LLSKENMLLG VDEIELGTDA
     DEASSLYKTL LEKLLKQNNQ IVITTHHKRL SVLMAENKEV ELLAALYDEE KERPTYTFLK
     GVIGKSYAFE TALRYGVPPF LIEKAKAFYG EDKEKLNVLI ENSSTLEREL KQKNEHLENA
     LKEQEDLKNA WLLEMEKQKE IFHHKKLELE KSYQQALNIL KSEVASKDTS SMHKEIHKAS
     EILNKHKTDQ EIPQIITSFQ INEKARYKNE SVLVIQILDK GYYLVETELG MRLKAHGSWL
     KQIQKPPKNK FKPPKTIVPK PKEASLRLDL RGQRSEEALD LLDAFLNDAL LGGFEEVLIC
     HGKGSGILEK FVKEFLKNHP KVVSFSDAPI NLGGSGVKIV KL