MUTS2_BACVZ
ID MUTS2_BACVZ Reviewed; 785 AA.
AC A7Z7E7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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};
GN OrderedLocusNames=RBAM_025650;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=326423;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant growth-
RT promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(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; CP000560; ABS74923.1; -; Genomic_DNA.
DR RefSeq; WP_012118134.1; NC_009725.2.
DR AlphaFoldDB; A7Z7E7; -.
DR SMR; A7Z7E7; -.
DR STRING; 326423.RBAM_025650; -.
DR PRIDE; A7Z7E7; -.
DR EnsemblBacteria; ABS74923; ABS74923; RBAM_025650.
DR KEGG; bay:RBAM_025650; -.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR Proteomes; UP000001120; 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.
FT CHAIN 1..785
FT /note="Endonuclease MutS2"
FT /id="PRO_1000075465"
FT DOMAIN 710..785
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 785 AA; 87234 MW; 6246DA645F60EFE2 CRC64;
MQQKVLSSLE FHKVKEQITA HAASSLGREK LLQLKPLTDL SDIQKQLDEV EEASAVMRLR
GHAPFGGLTD IRSALRRAEI GSVLTPAEFT ELSGLLYAVK QMKHFISQMT EDGVGIPLIQ
AHAEELITLG DLEREINSCI DDHGEVLDHA SPALRGIRTQ LRTLESRVRD RLESMLRSSS
ASKMLSDTIV TIRNDRFVIP VKQEYRSSYG GIVHDTSSSG ATLFIEPQAI VDMNNSLQQA
KVKEKQEIER ILRMLTEHTA EHTQEIAQDV EVLQTLDFIF AKARYAKAMK ATKPLMNGDG
FIRLKKARHP LLPQDQVVAN DIELGGDYST IVITGPNTGG KTVTLKTLGL LTIMAQAGLH
IPADEGSEAA VFDNVFADIG DEQSIEQSLS TFSSHMVNIV NILKDVSENS LVLFDELGAG
TDPQEGAALA MSILDEVHRT NARVLATTHY PELKAYGYNR QGVMNASVEF DIETLSPTYK
LLIGVPGRSN AFEISRRLGL PEHIIGQAKS EMTAEHNEVD LMIASLEKSK KRADEELSET
ESIRKEAEKL HKDLQQQIIE LNAQKDKMME EAEQKAAEKL EAAANEAEQI IRELRSIKQE
HRSFKEHELI DAKKRLGDAM PAFEKSKQPE RKTEKKRELK PGDEVKVLTF GQKGALLEKT
GEKEWNVQIG ILKMKVKEKD LEFLKSAPEP KKEKAITAVK GKDYHVSLEL DLRGERYENA
LSRVEKYLDD AVLAGHPRVS IIHGKGTGAL RKGVQDLLKN HRSVKSSRFG EAGEGGSGVT
IVELK