RECG_BORBU
ID RECG_BORBU Reviewed; 686 AA.
AC O51528;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ATP-dependent DNA helicase RecG;
DE EC=3.6.4.12;
GN Name=recG; OrderedLocusNames=BB_0581;
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: Critical role in recombination and DNA repair. Helps process
CC Holliday junction intermediates to mature products by catalyzing branch
CC migration. Has a DNA unwinding activity characteristic of a DNA
CC helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-
CC DNA) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000783; AAC66942.1; -; Genomic_DNA.
DR PIR; D70172; D70172.
DR RefSeq; NP_212715.1; NC_001318.1.
DR RefSeq; WP_002656646.1; NC_001318.1.
DR AlphaFoldDB; O51528; -.
DR SMR; O51528; -.
DR STRING; 224326.BB_0581; -.
DR PRIDE; O51528; -.
DR EnsemblBacteria; AAC66942; AAC66942; BB_0581.
DR GeneID; 56568014; -.
DR KEGG; bbu:BB_0581; -.
DR PATRIC; fig|224326.49.peg.972; -.
DR HOGENOM; CLU_005122_7_1_12; -.
DR OMA; DNGFQAC; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR004609; ATP-dep_DNA_helicase_RecG.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR045562; RecG_dom3_C.
DR InterPro; IPR033454; RecG_wedge.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF19833; RecG_C; 1.
DR Pfam; PF17191; RecG_wedge; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00643; recG; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..686
FT /note="ATP-dependent DNA helicase RecG"
FT /id="PRO_0000102139"
FT DOMAIN 277..438
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 457..617
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 391..394
FT /note="DEQH box"
FT BINDING 290..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 686 AA; 79044 MW; 5D4B20F38E6BA50B CRC64;
MFLHEFEYEL KGIGGLGEKG VERLNNLQIF NVKDLIEFFP VKYEDRQNIQ TFPDFSKVKS
CDMMTVFTVL GHKKFGDSSK KNLKLTVKSI NEEPFEILLF NRAFLENVFK IDKKFYIYSK
FTYNDYSGLW SCSNFDSEVY SDKPERFKKI LPVYSLTEGL TSKKISLYVK EALEYFFKFG
QTDIPRFLIE KYSLLSLSDA LKEIHFPSSL EMLEKAKKTL IYREIFLLQF FSRYRSSKIL
FREKKDLSKD LLEKVVSSLP FELTEDQKIS IDEIFFDLNS SKPMNRLLQG DVGSGKTLVA
LLSGLPLIEA GYQVAFMAPT DLLARQHYDN LSNILAPFNI SMTLLTGSLR KKDKEQALES
IRNGTSGLIV GTHAIFYEST EFKRLAYVII DEQHKFGVVQ REELKNKGEG VDMLLMSATP
IPRSFALTLF GDLEVSFIKT LPKGRLPITT YLARHGNEDK VYEFLRKELL KGHQVYFVYP
LISSSEKFEL KDVNNMCLKL KEVFGEYVVD MLHSKLPSDL KEEIMKNFYS KKVDILVATS
VIEVGIDCPN ATCMVVEHAE RFGLSTLHQI RGRVGRSNLQ SFFFLLYKEP LTSAGKFRLK
TIKENLDGFK IAEEDLRLRG PGNLFGLEQA GYLKLKIANF VDDREIIVLV REELDLFFYD
NSAYDKLDID LLDNLFCSYL NAGRSI