MUTS2_HELPY
ID MUTS2_HELPY Reviewed; 762 AA.
AC O25338;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=HP_0621;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=JP26;
RX PubMed=15866941; DOI=10.1128/jb.187.10.3528-3537.2005;
RA Kang J., Huang S., Blaser M.J.;
RT "Structural and functional divergence of MutS2 from bacterial MutS1 and
RT eukaryotic MSH4-MSH5 homologs.";
RL J. Bacteriol. 187:3528-3537(2005).
RN [3]
RP FUNCTION, ATPASE ACTIVITY, DNA-BINDING, ACTIVITY REGULATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLY-338.
RX PubMed=15629722; DOI=10.1016/j.molcel.2004.11.035;
RA Pinto A.V., Mathieu A., Marsin S., Veaute X., Ielpi L., Labigne A.,
RA Radicella J.P.;
RT "Suppression of homologous and homeologous recombination by the bacterial
RT MutS2 protein.";
RL Mol. Cell 17:113-120(2005).
RN [4]
RP FUNCTION IN DNA DAMAGE REPAIR, DNA-BINDING, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700392 / 26695, and SS1;
RX PubMed=16164556; DOI=10.1111/j.1365-2958.2005.04833.x;
RA Wang G., Alamuri P., Humayun M.Z., Taylor D.E., Maier R.J.;
RT "The Helicobacter pylori MutS protein confers protection from oxidative DNA
RT damage.";
RL Mol. Microbiol. 58:166-176(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 (Probable). Also involved in
CC repairing oxidative DNA damage. Has ATPase activity. Binds DNA.
CC {ECO:0000255|HAMAP-Rule:MF_00092, ECO:0000269|PubMed:15629722,
CC ECO:0000269|PubMed:15866941, ECO:0000269|PubMed:16164556, ECO:0000305}.
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by DNA.
CC {ECO:0000269|PubMed:15629722}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00092}.
CC -!- DOMAIN: Contains an N-terminal DNA-binding domain, followed by a
CC dimerization domain and a C-terminal domain, called the small MutS-
CC related (Smr) domain, which is absent from MutS and contains the
CC endonuclease activity. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutants have a significantly increased frequency
CC of intergenomic recombination. They are more sensitive than wild-type
CC cells to oxidative stress induced by agents such as H(2)O(2), paraquat
CC or oxygen. They also have a reduced colonization capacity in a mouse
CC model of infection. {ECO:0000269|PubMed:15629722,
CC ECO:0000269|PubMed:15866941, ECO:0000269|PubMed:16164556}.
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; AE000511; AAD07685.1; -; Genomic_DNA.
DR PIR; E64597; E64597.
DR RefSeq; NP_207415.1; NC_000915.1.
DR RefSeq; WP_010875507.1; NC_018939.1.
DR AlphaFoldDB; O25338; -.
DR SMR; O25338; -.
DR DIP; DIP-3208N; -.
DR IntAct; O25338; 32.
DR MINT; O25338; -.
DR STRING; 85962.C694_03215; -.
DR PaxDb; O25338; -.
DR PRIDE; O25338; -.
DR EnsemblBacteria; AAD07685; AAD07685; HP_0621.
DR KEGG; hpy:HP_0621; -.
DR PATRIC; fig|85962.8.peg.651; -.
DR eggNOG; COG1193; Bacteria.
DR OMA; IHAIIND; -.
DR PhylomeDB; O25338; -.
DR Proteomes; UP000000429; 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; IMP:CACAO.
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 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..762
FT /note="Endonuclease MutS2"
FT /id="PRO_0000115222"
FT DOMAIN 688..762
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 333..340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT MUTAGEN 338
FT /note="G->R: Lack of ATPase activity."
FT /evidence="ECO:0000269|PubMed:15629722"
SQ SEQUENCE 762 AA; 86753 MW; 8EFCE02A77DE4761 CRC64;
MSDAPKRSLN PTLMMNNNNT PPKPLEESLD LKEFIALFKT FFAKERDTIA LENDLKQTFT
YLNEVDAIGL PTPKSVKESD LIIIKLTKLG TLHLDEIFEI VKRLHYIVVL QNAFKTFTHL
KFHERLNAIV LPPFFNDLIA LFDDEGKIKQ GANATLDALN ESLNRLKKES VKIIHHYARS
KELAPYLVDT QSHLKHGYEC LLLKSGFSGA IKGVVLERSA NGYFYLLPES AQKIAQKIAQ
IGNEIDCCIV EMCQTLSHSL QKHLLFLKFL FKEFDFLDSL QARLNFAKAY NLEFVMPSFT
QKKMILENFS HPILKEPKPL NLKFEKSMLA VTGVNAGGKT MLLKSLLSAA FLSKHLIPMK
INAHHSIIPY FKEIHAIIND PQNSANNIST FAGRMKQFSA LLSKENMLLG VDEIELGTDA
DEASSLYKTL LEKLLKQNNQ IIITTHHKRL SVLMAENKEV ELLAALYDEE KERPTYTFLK
GVIGKSYAFE TALRYGVPHF LIEKAKTFYG EDKEKLNVLI ENSSALEREL KQKNEHLENA
LKEQEYLKNA WLLEMEKQKE IFHNKKLELE KSYQQALNIL KSEVASKDTS SMHKEIHKAS
EILSKHKTNQ EIPQIITNFQ ANEKARYKNE SVLIVQILDK GYYWIETELG MRLKAHGSLL
KKIQKPPKNK FKPPKTTIPK PKEASLRLDL RGQRSEEALD LLDAFLNDAL LGGFEEVLIC
HGKGSGILEK FVKEFLKNHP KVVSFSDAPI NLGGSGVKIV KL
