MUTS2_ENTFA
ID MUTS2_ENTFA Reviewed; 788 AA.
AC Q835H3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=EF_1404;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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; AE016830; AAO81195.1; -; Genomic_DNA.
DR RefSeq; NP_815125.1; NC_004668.1.
DR RefSeq; WP_002382291.1; NZ_KE136528.1.
DR AlphaFoldDB; Q835H3; -.
DR SMR; Q835H3; -.
DR STRING; 226185.EF_1404; -.
DR DNASU; 1200304; -.
DR EnsemblBacteria; AAO81195; AAO81195; EF_1404.
DR KEGG; efa:EF1404; -.
DR PATRIC; fig|226185.45.peg.2097; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR Proteomes; UP000001415; 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..788
FT /note="Endonuclease MutS2"
FT /id="PRO_1000075475"
FT DOMAIN 713..788
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 334..341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 788 AA; 88311 MW; 5555AB7704C1FE32 CRC64;
MNQRILSTLG FDKVKQQLLQ FIVTAQGTNE VSELLPIADE NKIQSWLNET QDGLKVQRLR
GGIPIPKLEN IQPHMKRIEI GADLNGIELA QVGRVLSTTS ELTRFFDELS ENEVDFERLY
MWREQLEVLP ELNRQLKQAI DDDGYVTDEA SPALKAIRQN IRRSEQTIRE ELDSIIRGKN
ARYLSDALVT MRNERYVIPV KQEYKNIFGG VVHDQSASGQ TLFIEPKQIL EMNNRLRQQQ
IAERNEITRI LAELSAELVP YRREITHNAY VIGKLDFINA KARLGKELKA VVPEISQANH
VVFKQARHPL LNPEKAVAND IVIGEEYQAI VITGPNTGGK TITLKTLGLL QLMGQAGLPI
PVEEESKMGI FTEVFADIGD EQSIEQSLST FSSHMTNIVS VLKKVDHQSL VLFDELGAGT
DPQEGAALAI AILDSLGAKG AYVMATTHYP ELKVYGYNRA GTINASMEFD VDTLSPTYRL
LIGVPGRSNA FEISKRLGLD NSIIEAAKQI MDGESQDLNE MIEDLENRRK MAETEYLEAR
HYVDESAALH KELKEAYQVF FEEREKELQK ARKEANKIIA EAEENAETII SDIRKMQLES
GQQGGVKEHQ LIDAKTQLSQ LHHEETKLAK NKVLKKAKEQ KKLKAGDEVI VNTYGQRGTL
LKDNGKGQWQ VQLGILKMNV SEEDMTPVAP QKEAKPRVTT VRSAESSHVG TQLDLRGKRY
EEALAEVDQY IDAAILAGYP QVTIVHGKGT GALRTGITEF LKNHRSVKSY EFAPQNQGGN
GATVVKFQ