MUTS2_CLOAB
ID MUTS2_CLOAB Reviewed; 788 AA.
AC Q97GM6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=CA_C2340;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80296.1; -; Genomic_DNA.
DR PIR; E97188; E97188.
DR RefSeq; NP_348956.1; NC_003030.1.
DR RefSeq; WP_010965637.1; NC_003030.1.
DR AlphaFoldDB; Q97GM6; -.
DR SMR; Q97GM6; -.
DR STRING; 272562.CA_C2340; -.
DR EnsemblBacteria; AAK80296; AAK80296; CA_C2340.
DR GeneID; 44998815; -.
DR KEGG; cac:CA_C2340; -.
DR PATRIC; fig|272562.8.peg.2536; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000000814; 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_0000115219"
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; 88271 MW; 3726BEFDAB395517 CRC64;
MNEKSLRVLE YFKIKDGIKK YISTSAAKKL IDELEPYGSL YEVKEHIEET KEAFELLMKK
GAPPFEGAYD VTEAVSMAEK GFSLAPGQLL KVGSMLRCAR KFKEYISHKE EEESYRIIED
ICSGIIPLKN IEDNIFNAII GEEEISDKAS TALYSIRRSL KDKNASIKDK VNAMMRSYSK
YLQENLYTIR GERYVIPVKA EYKAQVPGLV HDQSSTGATL FIEPMGLVNL NNEIKELMLK
EKAEIERILR ELSALIYKSI VAVKNNEKIV TELDFIFAKA KYASSINATA PHVNDKGVID
IVMGRHPLID PAKVVPLNIY MGREFTSLVI TGPNTGGKTV TLKTTGLLEV MAMSGLMIPA
RENSTISFFK EVYADIGDEQ SIEQSLSTFS SHMTNIVRII DDADEDSLVL FDELGAGTDP
TEGAALAISI LEALRKRGTK IVATTHYSEL KAYALKTENV ENASVEFDVE TLRPTYRLLI
GIPGKSNAFE ISKRLGLSDY IIEEARKGIS KDTLEFEDLI QNLQTRSVKA EENLRKAEFL
KEQAEKFKEK YEEKVSSITE TREKALHEGR REAKKIIEEA KSEADKILKD MREMERLGYS
SEARQRLQES RQKLKEKLNN AEESLNISER DQGEALKSVK EGEEVFIPSL NMKGIVISTQ
DSKGEVGIQA GIMKINVKLK DLRKTNNNPI SKKEKAVKKR EARLNLKSVA QSIDLRGLDS
EEAIYKTDIY LDEAYMAGLG SVTVIHGKGT GVLRNAINTM LKKNSHVKSY RLGNFGEGGT
GVTVVELK