MUTS2_STAAR
ID MUTS2_STAAR Reviewed; 782 AA.
AC Q6GHU1;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=SAR1117;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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; BX571856; CAG40120.1; -; Genomic_DNA.
DR RefSeq; WP_001249264.1; NC_002952.2.
DR AlphaFoldDB; Q6GHU1; -.
DR SMR; Q6GHU1; -.
DR KEGG; sar:SAR1117; -.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000000596; 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.
FT CHAIN 1..782
FT /note="Endonuclease MutS2"
FT /id="PRO_0000115230"
FT DOMAIN 707..782
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 336..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 782 AA; 88564 MW; 7D6CD279BB0EE4A1 CRC64;
MRQKTLDVLE FDKIKSLVAN ETISDLGLEK VNQMMPATNF ETVVFQMEET DEIAQIYNKH
RLPSLSGLSK VSAFIHRADI GGVLNVSELN LIKRLIQVQN QFKTFYNQLV EEDEGVKYPI
LDDKMNQLPV LTDLFQQINE TCDTYDLYDN ASYELQGIRS KISSTNQRIR QNLDRIVKSQ
ANQKKLSDAI VTVRNERNVI PVKAEYRQDF NGIVHDQSAS GQTLYIEPSS VVEMNNQISR
LRHDEAIEKE RILTQLTGYV AADKDALLVA EQVMGQLDFL IAKARCSRSI KGTKPIFKEE
RTVYLPKAYH PLLNRETVVA NTIEFMEDIE TVIITGPNTG GKTVTLKTLG LIIVMAQSGL
LIPTLDGSQL SVFKNVYCDI GDEQSIEQSL STFSSHMTNI VEILKNADKH SLVLFDELGA
GTDPSEGAAL AMSILDHVRK IGSLVMATTH YPELKAYSYN REGVMNASVE FDVDTLSPTY
KLLMGVPGRS NAFDISKKLG LSLNIINKAK TMIGTDEKEI NEMIESLERN YKRVETQRLE
LDRLVKEAEQ VHDDLSKQYQ QFQNYEKSLI EDAKEKANQK IKAATKEADD IIKDLRQLRE
QKGADVKEHE LIDKKKRLDD HYEAKSIKQN VQKQKYDKIV AGDEVKVLSY GQKGEVLEIV
NDEEAIVQMG IIKMKLPIED LEKKQKEKVK PTKMVTRQNR QTIKTELDLR GYRYEDALIE
LDQYLDQAVL SNYEQVYIIH GKGTGALQKG VQQHLKKHKS VSDFRGGMPS EGGFGVTVAT
LK