MUTS2_CLOB1
ID MUTS2_CLOB1 Reviewed; 788 AA.
AC A7FY72;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=CLB_3152;
OS Clostridium botulinum (strain ATCC 19397 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441770;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19397 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000726; ABS33974.1; -; Genomic_DNA.
DR RefSeq; WP_012099509.1; NC_009697.1.
DR AlphaFoldDB; A7FY72; -.
DR SMR; A7FY72; -.
DR KEGG; cba:CLB_3152; -.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
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.
FT CHAIN 1..788
FT /note="Endonuclease MutS2"
FT /id="PRO_1000093344"
FT DOMAIN 713..788
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 332..339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 788 AA; 88645 MW; 212AE0E6196CE09B CRC64;
MKDKSIKVLE FNKIQEILKN YTCTKAAKDI IEDLKPYDSM YEVREHLEET KEAFKLLITK
GAPPFEGVYD IRSGISLAEK GSALLPGQLL KIAAVLRCAR RFKEYINHKE EEESYRVLEN
ICEGIFSLPK IEEEIFNAIE GEDEIADRAS STLYNIRRSL KEKNYSVRDK INSLVRSYSS
YLQENIYTVR GDRYVLPVKA EHKGAVPGLV HDQSSTGATL FIEPMSLVNL NNEIKELMLK
EKAEIERILT VLSAKINANI TGVKTDANIV WELDFIFAKA KFASEYNCTC PTINDEGIVD
IIEGRHPLID RREVVPISVK LGEEFTSLMI TGPNTGGKTV TLKTVGLIHL MAMSGLMIPA
RENSVISYFN NVFADIGDEQ SIEQSLSTFS SHMKNIVEIM DKADENSLVL FDELGAGTDP
TEGAALAISI LENLRKRGTK IIATTHYSEL KAYALRKEGV ENASVEFDVE TLRPTYRLLI
GIPGKSNAFE ISKRLGLPDY IIDFARENIS NENIRFEELI QNLQEKSIKA QEDARLAENL
KLERDKEKKK YEEKLEGLQK VRDNALIDAR REAKNIIKEA KEEADKILKD IRQLERMGYS
SDARRKLEEE RKKLKDKLDS IEEKEIKTVH KGEALKNVKE GDEVLLASIN QKVIVLSKPD
NKGDVLVQAG IMKITANIKD LRAAKGSNSN NSSSKIKKSK KLNLNLRRVE SSVDLRGMDA
EEAIYTVDKY LDEAYLGGLG EVTIVHGKGT GVLRKTIMDM LKGHSHVKKY RLGEYGEGGT
GVTVVELK