MUTS2_LACP7
ID MUTS2_LACP7 Reviewed; 796 AA.
AC A9KR74;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Cphy_0153;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000885; ABX40542.1; -; Genomic_DNA.
DR RefSeq; WP_012198185.1; NC_010001.1.
DR AlphaFoldDB; A9KR74; -.
DR SMR; A9KR74; -.
DR STRING; 357809.Cphy_0153; -.
DR PRIDE; A9KR74; -.
DR EnsemblBacteria; ABX40542; ABX40542; Cphy_0153.
DR KEGG; cpy:Cphy_0153; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000000370; 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..796
FT /note="Endonuclease MutS2"
FT /id="PRO_1000093354"
FT DOMAIN 721..796
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT REGION 620..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 339..346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 796 AA; 88400 MW; 5D8B27914D3B1857 CRC64;
MNEKALRTLE YHKIIEKLSA LAGSSLGREK CHQLLPLVKL EDIVQMQQET TDALTRLYAK
GTLSFSGIPD IRDTLMRLEI GASLGAGELL KISSVLTATL RAKNYGYNQK NNEETEEAAQ
DTLTERFHLL EPLSPINNEI RRCIISEEEI ADDASPGLKS VRRQIKITND KIHESLGSIL
NSASTKGMLQ DAIITMRNGR YCLPIKQEYK NTFQGMMHDQ SSTGSTAFIE PMAIVKLNNE
LAELAVREQE EIEKILAELS NLVATEKYNL KYNQTTLAEL DFIFARAGLS KNMKASQPHF
NNRHYINIKK GRHPLIDPKK VVPIDIYFGD KFDLLVITGP NTGGKTVSLK TVGLFTLMGQ
AGLHIPAFDG SELSIFEEVY ADIGDEQSIE QSLSTFSSHM TNTVSILEHA NENSLVLFDE
LGAGTDPTEG AALAMAILSY LHQRKIRTMA TTHYSELKIF ALSTDGVSNA CCEFSVETLQ
PTYRLLIGIP GKSNAFAISS KLGLSNYIIE KAREFIGTKD ESFEDVISNL EASRIAMEKD
KAEAEQYKKE VEELKRKLAE KNSKIDDAKD RILREANEKA RTILQEAKDY ADETIRKYNK
WGAGGANNKE MENERAALRE KLGDTDSSLV SKAKKNRKQH KPSDFKVGDS VHVISLNLKG
SVSTLPNAKG DLYVQMGILR SLVNISDLEL IDEETIVAKA LTKTQSGKIR MSKSMSISPE
LNIIGKRVDE ALPLVDKYLD DAYLAHLPQV TIIHGRGTGA LKEAVHAHLK RTNYVKGYRV
GGFGEGDHGV TIVEFK