MUTS2_BORBU
ID MUTS2_BORBU Reviewed; 780 AA.
AC O51125;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
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}; Synonyms=mutSB;
GN OrderedLocusNames=BB_0098;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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; AE000783; AAC66481.1; -; Genomic_DNA.
DR PIR; B70112; B70112.
DR RefSeq; NP_212232.1; NC_001318.1.
DR RefSeq; WP_010889681.1; NC_001318.1.
DR AlphaFoldDB; O51125; -.
DR SMR; O51125; -.
DR STRING; 224326.BB_0098; -.
DR PRIDE; O51125; -.
DR EnsemblBacteria; AAC66481; AAC66481; BB_0098.
DR KEGG; bbu:BB_0098; -.
DR PATRIC; fig|224326.49.peg.496; -.
DR HOGENOM; CLU_011252_2_1_12; -.
DR OMA; IHAIIND; -.
DR Proteomes; UP000001807; 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..780
FT /note="Endonuclease MutS2"
FT /id="PRO_0000115218"
FT DOMAIN 706..780
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 334..341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 780 AA; 89052 MW; 903A3285893692DD CRC64;
MQDEQDKYLK NIDFYEILSL VSKYVSNPDT VNLLSNQKIL KTKESLEKIF SFVSLIRMLF
ESCKGYPNSF INSLKYPISL LLKENSRVSI ENLRDIIVFL DEVLRINLFL HKNSDIKHLN
VQILSDLLFL NPELKNLLNE LKEHIDVDAL ELKSGVVKEY DSIEFEIKNL NRRVENQIKK
IISLNAEYLT SNFVCYKSNK YTLALKSNFK GKIKGNIISI SSSGETFYIE PNDIVNANNR
LNYLSLEKER IILKILRNLS AKVHSNIVLL DNLYNNFLYY DSLKARAIYG IKTKGVFPEI
SNVLNIFDAH HPLLKDSKAI TFTPAENRVV IITGPNAGGK TVTLKTIGLL SAMFQFGIPI
VVGESSTFKI FDNIFIDIGD EQSISNSLST FSSHMSNISY ILKHTTKDSL VIFDEFCSGT
DIDQGQALAI SILEYLININ SYVLISTHYN ALKYFAYTHE GVVNASMRMD LETMQPNYNL
IFSIPGESYA FNVASKALID RSIVIRANEI YSSQKTEINE ILEKLIEKEK DLLLIKESMD
KKLIQIELQE KELENFYQDL LLREKNIETK LLNEQNEFLK NSRKVLENLV REIKEGNINV
AKNKAFISDL EKNVDLKTNK VNSLNNKRNV VADFKIGDKV RIVNSNAKGK IVGISKKKIT
VNVGAFNVSV SSSEISLENF KEKKENGKNF NFSIDYNKEN LLSFTIDIRG MRSVDALDFL
NKKIDNIILN GINKFEIIHG KGEGHLMREV HNLLKELKFI RKYYFAHPSD GGSGKTIVEI