MUTS2_STAAN
ID MUTS2_STAAN Reviewed; 782 AA.
AC P65496; Q99UW1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=SA0991;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB42240.1; -; Genomic_DNA.
DR PIR; D89885; D89885.
DR RefSeq; WP_001249275.1; NC_002745.2.
DR AlphaFoldDB; P65496; -.
DR SMR; P65496; -.
DR EnsemblBacteria; BAB42240; BAB42240; BAB42240.
DR KEGG; sau:SA0991; -.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR Proteomes; UP000000751; 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 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW Nucleotide-binding.
FT CHAIN 1..782
FT /note="Endonuclease MutS2"
FT /id="PRO_0000115229"
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; 88670 MW; CFE5B302C6CAEDAD CRC64;
MRQKTLDVLE FEKIKSLVAN ETISDLGLEK VNQMMPATNF ETVVFQMEET DEIAQIYNKH
RLPSLSGLSK VSAFIHRADI GGVLNVSELN LIKRLIQVQN QFKTFYNQLV EEDEGVKYPI
LDDKMNQLPV LTDLFHQINE TCDTYDLYDN ASYELQGIRS KISSTNQRIR QNLDRIVKSQ
ANQKKLSDAI VTVRNERNVI PVKAEYRQDF NGIVHDQSAS GQTLYIEPSS VVEMNNQISR
LRHDEAIEKE RVLTQLTGYV AADKDALLVA EQVMGQLDFL IAKARYSRSI KGTKPIFKEE
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