ID MUTS2_STAAT Reviewed; 782 AA.
AC A8Z1S5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
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};
GN OrderedLocusNames=USA300HOU_1079;
OS Staphylococcus aureus (strain USA300 / TCH1516).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=451516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USA300 / TCH1516;
RX PubMed=17986343; DOI=10.1186/1471-2180-7-99;
RA Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S.,
RA Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y., Igboeli O.,
RA Petrosino J., Tirumalai M., Uzman A., Fox G.E., Cardenas A.M., Muzny D.M.,
RA Hemphill L., Ding Y., Dugan S., Blyth P.R., Buhay C.J., Dinh H.H.,
RA Hawes A.C., Holder M., Kovar C.L., Lee S.L., Liu W., Nazareth L.V.,
RA Wang Q., Zhou J., Kaplan S.L., Weinstock G.M.;
RT "Subtle genetic changes enhance virulence of methicillin resistant and
RT sensitive Staphylococcus aureus.";
RL BMC Microbiol. 7:99-99(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; CP000730; ABX29098.1; -; Genomic_DNA.
DR RefSeq; WP_001249285.1; NC_010079.1.
DR AlphaFoldDB; A8Z1S5; -.
DR SMR; A8Z1S5; -.
DR KEGG; sax:USA300HOU_1079; -.
DR HOGENOM; CLU_011252_2_1_9; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis 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; P-loop containing nucleotide triphosphate hydrolases; 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; IPR046893; MSSS.
DR InterPro; IPR005747; MutS2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002625; Smr_dom.
DR InterPro; IPR036063; Smr_dom_sf.
DR NCBIfam; TIGR01069; mutS2; 1.
DR PANTHER; PTHR48378:SF1; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48378; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF20297; MSSS; 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; SSF48334; DNA repair protein MutS, domain III; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF160443; SMR domain-like; 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_1000093384"
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; 88661 MW; 1DFC2347703100EA CRC64;
MRQKTLDVLE FEKIKSLVAN 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 IAKARYSRSI KGTKPIFKED
RTVYLPKAYH PLLNRETVVA NTIEFMEDIE TVIITGPNTG GKTVTLKTLG LIIVMAQSGL
LIPTLDGSQL SVFKNVYCDI GDEQSIEQSL STFSSHMTNI VEILKHADKH SLVLFDELGA
GTDPSEGAAL AMSILDHVRK IGSLVMATTH YPELKAYSYN REGVMNASVE FDVDTLSPTY
KLLMGVPGRS NAFDISKKLG LSLNIINKAK TMIGTDEKEI NEMIESLERN YKRVETQRLE
LDRLVKEAEQ VHDDLSKQYQ QFQNYEKSLI EEAKEKANQK IKAATKEADD IIKDLRQLRE
QKGADVKEHE LIDKKKRLDD HYEAKSIKQN VQKQKYDKIV AGDEVKVLSY GQKGEVLEIV
NDEEAIVQMG IIKMKLPIED LEKKQKEKVK PTKMVTRQNR QTIKTELDLR GYRYEDALIE
LDQYLDQAVL SNYEQVYIIH GKGTGALQKG VQQHLKKHKS VSDFRGGMPS EGGFGVTVAT
LK
//
