ID   MUTS2_STRPI             Reviewed;         778 AA.
AC   B1I9K1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=SPH_0515;
OS   Streptococcus pneumoniae (strain Hungary19A-6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hungary19A-6;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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; CP000936; ACA35692.1; -; Genomic_DNA.
DR   RefSeq; WP_001035029.1; NC_010380.1.
DR   AlphaFoldDB; B1I9K1; -.
DR   SMR; B1I9K1; -.
DR   PRIDE; B1I9K1; -.
DR   EnsemblBacteria; ACA35692; ACA35692; SPH_0515.
DR   GeneID; 66805598; -.
DR   KEGG; spv:SPH_0515; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   Proteomes; UP000002163; 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; 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..778
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093397"
FT   DOMAIN          702..777
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   778 AA;  87620 MW;  52E5466AA2DDD275 CRC64;
     MNKKILETLE FDKVKALFEP HLLTEQGLEQ LRQLAPTAKA DKIKQAFAEM KEMQALFVEQ
     PHFTILSTKE IAGVCKRLEM GADLNIEEFL LLKRVLLTSR ELQSFYANLE NVSLEELAFW
     FEKLHDFPQL QGNLQAFNDA GFIENFASEE LARIRRKIHD SESQVRDVLQ DLLKQKAQML
     TEGIVASRNG RQVLPVKNTY RNKIAGVVHD ISASGNTVYI EPREVVKLSE EIASLRADER
     YEMLRILQEI SERVRPHAAE IANDAWIIGH LDLIRAKVRF IQERQAVVPQ LSENQEIQLL
     HVCHPLVKNA VANDVYFGQD LTAIVITGPN TGGKTIMLKT LGLTQVMAQS GLPILADKGS
     RVGIFEEIFA DIGDEQSIEQ SLSTFSSHMT NIVDILGKVN QHSLLLLDEL GAGTDPQEGA
     ALAMAILEDL RLRQIKTMAT THYPELKAYG IETAFVQNAS MEFDTATLRP TYRFMQGVPG
     RSNAFEIAKR LGLSEVIVGD ASQQIDQDND VNRIIEQLEE QTLESRKRLD NIREVEQENL
     KMNRALKKLY NELNREKETE LNKAREQAAE IVDMALSESD QILKNLHSKS QLKPHEIIEA
     KAKLKKLAPE KVDLSKNKVL QKAKKKRAPK VGDDIVVLSY GQRGTLTSQL KDGRWEAQVG
     LIKMTLEEKE FDLVQAQQEK AVKKKQVNVV KRTSGRGPQA RLDLRGKRYE EAMNELDTFI
     DQALLNNMAQ VDIIHGIGTG VIREGVTKYL QRNKHVKSFG YAPQNAGGSG ATIVTFKG