MUTS2_SYMTH
ID MUTS2_SYMTH Reviewed; 793 AA.
AC Q67QE3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=STH1115;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD40100.1; -; Genomic_DNA.
DR RefSeq; WP_011195247.1; NC_006177.1.
DR AlphaFoldDB; Q67QE3; -.
DR SMR; Q67QE3; -.
DR STRING; 292459.STH1115; -.
DR PRIDE; Q67QE3; -.
DR EnsemblBacteria; BAD40100; BAD40100; STH1115.
DR KEGG; sth:STH1115; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000000417; 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..793
FT /note="Endonuclease MutS2"
FT /id="PRO_1000093409"
FT DOMAIN 717..792
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT REGION 611..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 329..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 793 AA; 87439 MW; 457DB102EAAAFCC3 CRC64;
MDERTLRTLE FAKIKEMLAE RTATSLGREV VESLAPATDF LEVQHRQAET SEARRLYEGG
HAIPLGGLHD LRAHVQRAVR GGVLDPGDLL DVADTAASSR RLKRFLEEQE GLPILTALSR
MLGTFHHLEA EIRQAVDEHG EVRDDASPAL AEIRRSMRIL QNRMKERLDA FVRGSAAKYL
QDPIVTIREG RFVVPVKIEY RAQVPGIVHD QSASGSTLFI EPMAIVEMNN DLRELALKEH
EEVERILARL SSLVAGEADA LLDTLQAVAQ IDFASAKGKL SLDLDCTEPE LVREPILEIH
KGRHPLLKGR VVPIDVHIGI TFDTLVITGP NTGGKTVALK TMGLFVLMAQ AGLHLPAGHG
TRVGVFQQVF VDIGDEQSIE QSLSTFSGHM TNIIRILDAL EGPALVLLDE LGAGTDPTEG
AALAMSILEH LHKRGAKTVA TTHYSELKTY AYTRSRVENA SVEFDVETLR PTFRLLIGVP
GSSNAFEISR RLGLSPHIVD RARQFLTQEQ ERVEDLIQGI HATRAELEKE RAEAHRLRAE
AQRMREEYER RYGDAQRKAA ETVEKARAQA QQILATARRE AEAVIAELKQ ALREQREAER
MQAIQSARSR LARARQAVEP TEEEQRARRR GEVPRGLKPG DKVRVVSLDT TGYVLSEPDA
DGNVLVQAGI LKMTVSLTDL ERASEEQPAA GAGGPARMRT HGKGLAVSKA REMSPEVDLR
GLMVEEALER VDKFLDDAVL AGLPQVRIIH GKGTGALRKA VTEALRHDRR VESYRLGGVG
EGGDGVTVAK LRE