MUTS2_STRP2
ID MUTS2_STRP2 Reviewed; 778 AA.
AC Q04M67;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=SPD_0371;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
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; CP000410; ABJ55516.1; -; Genomic_DNA.
DR RefSeq; WP_001035008.1; NC_008533.2.
DR AlphaFoldDB; Q04M67; -.
DR SMR; Q04M67; -.
DR STRING; 373153.SPD_0371; -.
DR EnsemblBacteria; ABJ55516; ABJ55516; SPD_0371.
DR GeneID; 60233859; -.
DR KEGG; spd:SPD_0371; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR BioCyc; SPNE373153:G1G6V-408-MON; -.
DR Proteomes; UP000001452; 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_1000093393"
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; 87590 MW; 11322EA4001BA8C9 CRC64;
MNKKILETLE FDKVKALFEP HLLTEQGLEQ LRQLAPTAKA DKIKQAFAEM KEMQALFVEQ
PHFTILSTKE IAGVCKRLEM GADLNIEEFL LLKRVLLASR 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