MUTS2_THET8
ID MUTS2_THET8 Reviewed; 744 AA.
AC Q5SHT5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=TTHA1645;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1-8, FUNCTION, ATPASE ACTIVITY, NUCLEASE ACTIVITY,
RP DNA-BINDING, ACTIVITY REGULATION, INTERACTION WITH MUTL, AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=15113836; DOI=10.1093/jb/mvh045;
RA Fukui K., Masui R., Kuramitsu S.;
RT "Thermus thermophilus MutS2, a MutS paralogue, possesses an endonuclease
RT activity promoted by MutL.";
RL J. Biochem. 135:375-384(2004).
RN [3]
RP FUNCTION, DNA-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, AND
RP MUTAGENESIS OF HIS-701.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=17215294; DOI=10.1093/nar/gkl735;
RA Fukui K., Kosaka H., Kuramitsu S., Masui R.;
RT "Nuclease activity of the MutS homologue MutS2 from Thermus thermophilus is
RT confined to the Smr domain.";
RL Nucleic Acids Res. 35:850-860(2007).
RN [4]
RP FUNCTION AS AN ENDONUCLEASE.
RX PubMed=17686785; DOI=10.1093/nar/gkm575;
RA Fukui K., Takahata Y., Nakagawa N., Kuramitsu S., Masui R.;
RT "Analysis of a nuclease activity of catalytic domain of Thermus
RT thermophilus MutS2 by high-accuracy mass spectrometry.";
RL Nucleic Acids Res. 35:E100-E100(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 663-744, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18838375; DOI=10.1074/jbc.m806755200;
RA Fukui K., Nakagawa N., Kitamura Y., Nishida Y., Masui R., Kuramitsu S.;
RT "Crystal structure of MutS2 endonuclease domain and the mechanism of
RT homologous recombination suppression.";
RL J. Biol. Chem. 283:33417-33427(2008).
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. Cleaves the phosphate backbone
CC of oligodeoxynucleotides non-sequence-specifically at the 3' side of
CC the phosphates. Preferably incises the branched DNA structures,
CC especially the D-loop structure over the Holliday junction. Has ATPase
CC activity. Binds to dsDNA but not to ssDNA. {ECO:0000255|HAMAP-
CC Rule:MF_00092, ECO:0000269|PubMed:15113836,
CC ECO:0000269|PubMed:17215294, ECO:0000269|PubMed:17686785,
CC ECO:0000269|PubMed:18838375}.
CC -!- ACTIVITY REGULATION: Nuclease activity is stimulated by interaction
CC with MutL. ATPase activity is stimulated by dsDNA.
CC {ECO:0000269|PubMed:15113836}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=48 uM for ATP {ECO:0000269|PubMed:17215294};
CC Note=kcat is 2.1 min(-1) for ATP.;
CC -!- SUBUNIT: Homodimer. Interacts with MutL. {ECO:0000255|HAMAP-
CC Rule:MF_00092, ECO:0000269|PubMed:15113836,
CC ECO:0000269|PubMed:17215294}.
CC -!- DOMAIN: Contains an N-terminal DNA-binding domain, followed by a
CC dimerization domain and a C-terminal domain, called the small MutS-
CC related (Smr) domain, which is absent from MutS and contains the
CC endonuclease activity. The Smr domain can also bind DNA.
CC {ECO:0000269|PubMed:17215294}.
CC -!- DISRUPTION PHENOTYPE: Disruption causes an increase in the frequency of
CC recombination between perfectly matched sequences.
CC {ECO:0000269|PubMed:18838375}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00092}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008226; BAD71468.1; -; Genomic_DNA.
DR RefSeq; WP_011228829.1; NC_006461.1.
DR RefSeq; YP_144911.1; NC_006461.1.
DR PDB; 2ZQE; X-ray; 1.70 A; A=663-744.
DR PDB; 7VUF; X-ray; 3.11 A; A/B/C/D=1-488.
DR PDB; 7VUK; X-ray; 3.38 A; A/B=1-488.
DR PDBsum; 2ZQE; -.
DR PDBsum; 7VUF; -.
DR PDBsum; 7VUK; -.
DR AlphaFoldDB; Q5SHT5; -.
DR SMR; Q5SHT5; -.
DR STRING; 300852.55773027; -.
DR EnsemblBacteria; BAD71468; BAD71468; BAD71468.
DR GeneID; 3169358; -.
DR KEGG; ttj:TTHA1645; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_0; -.
DR OMA; IHAIIND; -.
DR PhylomeDB; Q5SHT5; -.
DR EvolutionaryTrace; Q5SHT5; -.
DR Proteomes; UP000000532; 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 Gene3D; 3.30.1370.110; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00092; MutS2; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 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 3D-structure; ATP-binding; Direct protein sequencing; DNA-binding;
KW Endonuclease; Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..744
FT /note="Endonuclease MutS2"
FT /id="PRO_0000423737"
FT DOMAIN 668..743
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 315..322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT MUTAGEN 701
FT /note="H->A: 140-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:17215294"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:2ZQE"
FT HELIX 675..691
FT /evidence="ECO:0007829|PDB:2ZQE"
FT STRAND 695..700
FT /evidence="ECO:0007829|PDB:2ZQE"
FT HELIX 707..718
FT /evidence="ECO:0007829|PDB:2ZQE"
FT STRAND 722..727
FT /evidence="ECO:0007829|PDB:2ZQE"
FT TURN 730..733
FT /evidence="ECO:0007829|PDB:2ZQE"
FT HELIX 734..736
FT /evidence="ECO:0007829|PDB:2ZQE"
FT STRAND 737..742
FT /evidence="ECO:0007829|PDB:2ZQE"
SQ SEQUENCE 744 AA; 82517 MW; D28A24B86E20662F CRC64;
MRDVLEVLEF PRVRALLAER AKTPLGRELA LALAPLPREE AEKRHELTGE ALSYPYALPE
AGTLREAYGR ALAGARLSGP ELLKAAKALE EAMALKEELL PLKNALSQVA EGIGDHTPFL
ERVRKALDEE GAVKDEASPR LAQIRRELRP LRQQILDRLY ALMDRHREAF QDRFVTLRRE
RYCVPVRAGM AQKVPGILLD ESESGATLFI EPFSVVKLNN RLQALRLKEE EEVNRILRDL
SERLAKDEGV PKTLEALGLL DLVQAQAALA RDLGLSRPAF GERYELYRAF HPLIPDAVRN
SFALDEKNRI LLISGPNMGG KTALLKTLGL AVLMAQSGLF VAAEKALLAW PDRVYADIGD
EQSLQENLST FAGHLRRLRE MLEEATSHSL VLIDELGSGT DPEEGAALSQ AILEALLERG
VKGMVTTHLS PLKAFAQGRE GIQNASMRFD LEALRPTYEL VLGVPGRSYA LAIARRLALP
EEVLKRAEAL LPEGGRLEAL LERLEAERLA LEAERERLRR ELSQVERLRK ALAEREARFE
EERAERLKAL EEEVRAELLK VEAELKALKE KARTEGKRDA LRELMALRER YAKKAPPPPP
PPGLAPGVLV EVPSLGKRGR VVELRGEEVL VQVGPLKMSL KPQEVKPLPE AEPGKPLLAK
PRREVKEVDL RGLTVAEALL EVDQALEEAR ALGLSTLRLL HGKGTGALRQ AIREALRRDK
RVESFADAPP GEGGHGVTVV ALRP
