MUTS2_STRA1
ID MUTS2_STRA1 Reviewed; 779 AA.
AC Q3JZH6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=SAK_1727;
OS Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS SS700).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=205921;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27591 / A909 / CDC SS700;
RX PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA Wessels M.R., Rappuoli R., Fraser C.M.;
RT "Genome analysis of multiple pathogenic isolates of Streptococcus
RT agalactiae: implications for the microbial 'pan-genome'.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(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. {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; CP000114; ABA44913.1; -; Genomic_DNA.
DR RefSeq; WP_001060323.1; NC_007432.1.
DR AlphaFoldDB; Q3JZH6; -.
DR SMR; Q3JZH6; -.
DR GeneID; 66886559; -.
DR KEGG; sak:SAK_1727; -.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
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.
FT CHAIN 1..779
FT /note="Endonuclease MutS2"
FT /id="PRO_1000093386"
FT DOMAIN 704..779
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 779 AA; 87741 MW; 28A940AFC7CC1F2A CRC64;
MNNKILEQLE FNKVKELILP YLKTEQSQEE LSELEPMTEA PKIEKSFNEI SDMEQIFVEH
HSFGIVSLSS ISESLKRLEL SADLNIQELL AIKKVLQSSS DMIHFYSDLD NVSFQSLDRL
FENLEQFPNL QGSFQAINDG GFLEHFASPE LERIRRQLTN SERRVRQILQ DMLKEKAELL
SENLIASRSG RSVLPVKNTY RNRISGVVHD ISSSGSTVYI EPRAVVTLNE EITQLRADER
HEESRILHAF SDLLRPHVAT IRNNAWILGH LDFVRAKYLF MSDNKATIPE ISNDSTLALI
NVRHPLLSNP VANDLHFDQD LTAIVITGPN TGGKTIMLKT LGLAQLMGQS GLPVLADKGS
KIAVFNNIFA DIGDEQSIEQ SLSTFSSHMT HIVSILNEAD HNSLVLFDEL GAGTDPQEGA
SLAMAILEHL RLSNIKTMAT THYPELKAYG IETNFVENAS MEFDAETLSP TYRFMQGVPG
RSNAFEIASR LGLAPFIVKQ AKQMTDSDSD VNRIIEQLEA QTLETRRRLD HIKEVEQENL
KFNRAVKKLY NEFSHERDKE LEKIYQEAQE IVDMALNESD TILKKLNDKS QLKPHEIIDA
KAQIKKLAPQ VDLSKNKVLN KAKKIKAARA PRIGDDIIVT SYGQRGTLTS QLKDGRWEAQ
VGIIKMTLTQ DEFTLVRVQE EQKVKSKQIN VVKKADSSGP RARLDLRGKR YEEAMQELDN
FIDQALLNNM GQVDIIHGIG TGVIREGVTK YLRRNKHVKH FAYAPQNAGG SGATIVTLG