MUTS2_ALKCK
ID MUTS2_ALKCK Reviewed; 787 AA.
AC Q5WEK0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=ABC2675;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) 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}.
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; AP006627; BAD65210.1; -; Genomic_DNA.
DR RefSeq; WP_011247518.1; NC_006582.1.
DR AlphaFoldDB; Q5WEK0; -.
DR SMR; Q5WEK0; -.
DR STRING; 66692.ABC2675; -.
DR EnsemblBacteria; BAD65210; BAD65210; ABC2675.
DR KEGG; bcl:ABC2675; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000001168; 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..787
FT /note="Endonuclease MutS2"
FT /id="PRO_1000075473"
FT DOMAIN 712..787
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 335..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 787 AA; 87167 MW; 6D25A992D74AC1E8 CRC64;
MERVQRVLEY NKMKQQLLEH VASSLGRQKV NELVPSTSLE EVRHLQDETA EAANVLRLKG
HVPLGGISDV RPHIKRAAIG GVLSATELIE IASTLYGGKR VKQFIETIIE DGHIEVPILA
GHVEQIEPLS PIEKAIKQCI DDNGYVLDSA STSLRTVRHQ IRSYESGIKS KLDQLTRSSN
TRKMLSDAIV TIRSDRYVLP VKQEYRGTFG GIVHDQSSSG ATLFIEPAAI VTLNNQLTEA
KAKEKREIER ILRELSAKVA EESEQLLLNV DKLAQLDFIC AKAYYAKAVK AVKPTLNDRG
YLDLRQARHP LLPPDKVVPS DMAIGDQVRS LVITGPNTGG KTVTLKTIGL LTLMAQSGLF
VPAAEETELA VFEHIFADIG DEQSIEQSLS TFSSHMKNIV SILNEMNENS LILFDELGAG
TDPTEGAALA ISILDHVYKR GALAVATTHY SELKGYAYNR EGALNASVEF DVETLRPTYR
LLVGVPGRSN AFAISRRLGL DERIIDQAKL QIDSDASQVE KMIASLEDSQ KSAQSEWSRA
EAVRREAEAL KRDLEKRMAS FEEMKEAALQ KAEQKAEKVV AAAQENAELI ISELRDLQKQ
GVAVKEHQLI EARKQLEEAA PKLVSKKRKQ VKKQAEKAKR LPEPGDEVKV LSFNQKGTVV
KKIGDNEYQV QLGIMKMAVP IDDIQLLEQE RRQPEKAITT IRGNDAHVKA ELDLRGERYE
DAMRRVEKYI DDALLAGYHQ VSIIHGKGTG ALRKGVKQFV ANHPRVKSAR DGGMNEGGLG
NTVIELK