MUTS_BORBU
ID MUTS_BORBU Reviewed; 862 AA.
AC O51737;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=DNA mismatch repair protein MutS;
GN Name=mutS; OrderedLocusNames=BB_0797;
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: This protein is involved in the repair of mismatches in DNA.
CC It is possible that it carries out the mismatch recognition step. This
CC protein has a weak ATPase activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000305}.
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DR EMBL; AE000783; AAC67157.1; -; Genomic_DNA.
DR PIR; D70199; D70199.
DR RefSeq; NP_212931.1; NC_001318.1.
DR RefSeq; WP_002657221.1; NC_001318.1.
DR AlphaFoldDB; O51737; -.
DR SMR; O51737; -.
DR STRING; 224326.BB_0797; -.
DR PRIDE; O51737; -.
DR EnsemblBacteria; AAC67157; AAC67157; BB_0797.
DR GeneID; 56567376; -.
DR KEGG; bbu:BB_0797; -.
DR PATRIC; fig|224326.49.peg.1189; -.
DR HOGENOM; CLU_002472_3_1_12; -.
DR OMA; TPMMAQY; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0006298; P:mismatch repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.420.110; -; 1.
DR Gene3D; 3.40.1170.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00096; MutS; 1.
DR InterPro; IPR005748; DNA_mismatch_repair_MutS.
DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR InterPro; IPR017261; DNA_mismatch_repair_MutS/MSH.
DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR InterPro; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361; PTHR11361; 1.
DR Pfam; PF01624; MutS_I; 1.
DR Pfam; PF05188; MutS_II; 1.
DR Pfam; PF05192; MutS_III; 1.
DR Pfam; PF05190; MutS_IV; 1.
DR Pfam; PF00488; MutS_V; 1.
DR PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF48334; SSF48334; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53150; SSF53150; 1.
DR SUPFAM; SSF55271; SSF55271; 1.
DR TIGRFAMs; TIGR01070; mutS1; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..862
FT /note="DNA mismatch repair protein MutS"
FT /id="PRO_0000115073"
FT BINDING 608..615
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 862 AA; 99749 MW; 513B2FD6A831BFE9 CRC64;
MEKNVTPMIR QYLDIKKKYK DAVLFFRVGS FYEMFFDDAI EVSKLLNLTL TKRENVPMCG
VPYHTSKEYI RKLILFDKKV AICEQASNST SGGPLEREVV EVITPGVIID EDFLNDDINN
YLVAISDYKD YYSFSYIDLS TSSLGIMFYE NGFFEKLKRD LEKYSPKEII VSENFYYEYS
EKLNLSRFLI NRVPTWHLDK DIAIKTIKEH FNILGLSSLG FDEEKPYYIS IFLIINHIKN
NLKNLLSNID KIDINNDSSY MFLDDVTQVN LELVKNNNDF SSQYSLYSVL NDCKTAMGKR
LLREFILNPI LNISEINTRL DHVEFFCKNI SLTVTLRETF INIWDIERII SRIQMKRYIK
KDFLFIEKAL SVFFTVKKLF DKHNFDYWNF DKFEEDSISK VYFLINSAIS SAPDELIKRG
YDLKLDNLKD LKINANKYID QYLESERLLS KINNLKIRKT NNRGLFFEVT KSNYAQVPPH
FMESQALNSS KRYKTEKLIS LEVDINNAED NVVAFEQEIF DEIASNVVMH NKVLKKVAEF
FAYIDLVVNF GYLAKKNEYK RPVLTSGKEI LLEKSRHPVV EHYTKNTEIF TENFVRINKE
KYFCLITGPN MAGKSTYLRQ VALITLMAHI GSFVPASKAL IGITDKIFCR IGASDNIAKG
ESTFLVEMNE TANILRNATE KSLIIMDEVG RGTSTNDGLA IAYSIIEYIL EYIKARSLFA
THFHELSSIN HQAFINLSMK IEKQGNDLVF LREVEEKPSL NSYGIYVARI AGLPLRVIDR
ANVILESLVG REGNSCLEFL PHVSSDGNDK EILKNDTDIH IKLNEYLELK NFISNIDINN
ITPFQSIELL NQIVLKVISQ SS