MUTS2_STAEQ
ID MUTS2_STAEQ Reviewed; 782 AA.
AC Q5HQ30;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=SERP0727;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(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; CP000029; AAW54100.1; -; Genomic_DNA.
DR RefSeq; WP_002446210.1; NC_002976.3.
DR AlphaFoldDB; Q5HQ30; -.
DR SMR; Q5HQ30; -.
DR STRING; 176279.SERP0727; -.
DR EnsemblBacteria; AAW54100; AAW54100; SERP0727.
DR KEGG; ser:SERP0727; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000000531; 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; Reference proteome.
FT CHAIN 1..782
FT /note="Endonuclease MutS2"
FT /id="PRO_0000115235"
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; 88719 MW; 2EF695D7C78E9B31 CRC64;
MRQKTLDVLE FEKIKSFVAD ETISDLGREK VQEMAPASNF DTVEFQMNET DEISQIYNKH
RLPSLSGLAK VSPLVHRASI GGVLNVAELN RIKRLVQVQN QFKTFYNQML EEDEEVKYPI
LHDKMNHLPI LTDLFKEINE TCDAHDLFDH ASYTLQSIRS KISRTNQRIR QNLDRIVKNQ
GNQKKLSDAI VTVRNDRNVI PVKAEYRQDF NGIVHDQSAS GQTLYIEPNS VVEMNNQISR
LRNDEAVERE RILTELTGFV SAEADALLIA ESVMGQIDFL IAKARYARTI KGTKPTFKED
RTIYLPNAFH PLLDKDTVVA NTIEFIDDVE TVIITGPNTG GKTVTLKTLG LIIVMAQSGL
LIPTLDGSQL SIFENVYCDI GDEQSIEQSL STFSSHMKNI VEILQDADQN SLILFDELGA
GTDPSEGAAL AMSILDYVRR LGSLVMATTH YPELKAYSYN REGVMNASVE FDVETLSPTY
KLLMGVPGRS NAFDISKKLG LSLNIINKAK TMIGTDEQEI NAMIESLEQN SKRVDQQRIE
LDRLVREAQQ THDALSKQYQ QYQNYETSLM DEAKEKANQR VKSATKEADE ILKELRNLRD
HKGAEVKEHE LIDKKKQLDD QYEVKSIKQH VQKKKYDTIH TGDEVKVLSY GQKGEVLELV
GDEEAVVQMG IIKMKLPIED LEKTKKKKEK PTKMVTRQNR QTIKTELDLR GYRYEEALNE
LDQYLDQAVL SNYEQVYIIH GKGTGALQKG VQQHLKKHKS VRQFRGGMPS EGGFGVTVAE
LK