MUTS2_STRT2
ID MUTS2_STRT2 Reviewed; 783 AA.
AC Q5M2P5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=stu1762;
OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=264199;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-250 / LMG 18311;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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; CP000023; AAV61361.1; -; Genomic_DNA.
DR RefSeq; WP_011226555.1; NC_006448.1.
DR AlphaFoldDB; Q5M2P5; -.
DR SMR; Q5M2P5; -.
DR STRING; 264199.stu1762; -.
DR EnsemblBacteria; AAV61361; AAV61361; stu1762.
DR GeneID; 66899497; -.
DR KEGG; stl:stu1762; -.
DR PATRIC; fig|264199.4.peg.1739; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR Proteomes; UP000001170; 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 CDD; cd03280; ABC_MutS2; 1.
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..783
FT /note="Endonuclease MutS2"
FT /id="PRO_1000093406"
FT DOMAIN 708..783
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 328..335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 783 AA; 88077 MW; 3964202E6A74A6EC CRC64;
MNTKILDQLE FNKVKDQFTE YLQTEQAQAE LRDLVPMTNP ERIQNQFTEI QEMSEIFVEH
HGFAIGSLRD ISEPLRRLEL DADLNIQELI AIKKVLQASA DLSRFYADLE NVELIALKRL
FEKIEAFPSL QGSLQSINDG GFIEHFASPE LQNIRRQLKA CDDAIRQTLQ DILKKSGHML
AENLIASRNG RSVLPVKNTY RNRIAGVVHD ISSSGNTVYI EPRAVIQLNE KITQLRADER
HEMARILHEL SDQLRPHTAA IANNAWILGH MDFIRGKYLY LHDKKAIIPE ISDNQTLQLL
NVRHPLLINP VANDLRFDED LTVIVITGPN TGGKTVMLKT LGLAQLMAQS GLPILADKGS
RVAIFQEIFA DIGDEQSIEQ SLSTFSSHMT HIVEILNTAD SNSLVLVDEL GAGTDPQEGA
SLAMAILEHL RLSQIKTMAT THYPELKAYG IETQHVENAS MEFDTATLRP TYRFMQGVPG
RSNAFEIARR LGLNEIIVKE AENLTDTDSD VNRIIEQLEA QTVETQKRLE HIKDVEQENL
KFNRAVKKLY NEFSHEYDKE LEKAQKEIQE MVDTALAESD SILKNLHDKS QLKPHEVIDA
KGKLKKLAAQ VDLSKNKVLR KAKKEKAARA PRVGDDIIVT AYGQRGTLTS QAKNGNWEAQ
VGLIKMSLKA DEFTLVRTQA EAQQPKKKQI NVVKKAKKTS SDGPRARLDL RGKRYEEAMQ
ELDAFIDQAL LNNMSQVEII HGIGTGVIRD AVTKYLRRHR HVKNFEYAPQ SAGGSGCTIA
TLG