RECG_ECO27
ID RECG_ECO27 Reviewed; 693 AA.
AC B7UM74;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=ATP-dependent DNA helicase RecG {ECO:0000303|PubMed:18952797};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P24230};
GN Name=recG {ECO:0000303|PubMed:18952797};
GN OrderedLocusNames=E2348C_3916 {ECO:0000312|EMBL:CAS11464.1};
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1] {ECO:0000312|EMBL:CAS11464.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/JB.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=32023456; DOI=10.1016/j.celrep.2020.01.014;
RA Lawaree E., Jankevicius G., Cooper C., Ahel I., Uphoff S., Tang C.M.;
RT "DNA ADP-Ribosylation Stalls Replication and Is Reversed by RecF-Mediated
RT Homologous Recombination and Nucleotide Excision Repair.";
RL Cell Rep. 30:1373-1384(2020).
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). {ECO:0000250|UniProtKB:P24230}.
CC -!- FUNCTION: Plays a role in recovery after DNA ADP-ribosylation.
CC {ECO:0000269|PubMed:32023456}.
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 Evidence={ECO:0000250|UniProtKB:P24230};
CC -!- DISRUPTION PHENOTYPE: Significantly reduced survival of cells
CC expressing DNA ADP-ribosyl transferase (darT) mutant G49D.
CC {ECO:0000269|PubMed:32023456}.
CC -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC {ECO:0000305}.
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DR EMBL; FM180568; CAS11464.1; -; Genomic_DNA.
DR RefSeq; WP_000678455.1; NC_011601.1.
DR EnsemblBacteria; CAS11464; CAS11464; E2348C_3916.
DR KEGG; ecg:E2348C_3916; -.
DR HOGENOM; CLU_005122_7_1_6; -.
DR OMA; RETNDGF; -.
DR Proteomes; UP000008205; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.140; -; 1.
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.
FT CHAIN 1..693
FT /note="ATP-dependent DNA helicase RecG"
FT /id="PRO_0000456042"
FT DOMAIN 283..448
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 482..628
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 397..400
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 296..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 693 AA; 76553 MW; 891FD4D50B3C3F13 CRC64;
MKGRLLDAVP LSSLTGVGAA LSNKLAKINL HTVQDLLLHL PLRYEDRTHL YPIGELLPGV
YATVEGEVLN CNISFGSRRM MTCQISDGSG ILTMRFFNFN AAMKNSLATG RRVLAYGEAK
RGKYGAEMIH PEYRVQGDLS TPELQETLTP VYPTTEGVKQ ATLRKLTDQA LDLLDTCAIE
ELLPPELSQG MMTLPEALRT LHRPPPTLQL SDLETGQHPA QRRLILEELL AHNLSMLALR
AGAQRFHAQP LSANDALKNK LLAALPFKPT GAQARVVAEI ERDMALDVPM MRLVQGDVGS
GKTLVAALAA LRAVAHGKQV ALMAPTELLA EQHANNFRNW FAPLGIEVGW LAGKQKGKAR
LAQQEAIASG QVQMIVGTHA IFQEQVQFNG LALVIIDEQH RFGVHQRLAL WEKGQQQGFH
PHQLIMTATP IPRTLAMTAY ADLDTSVIDE LPPGRTPVTT VAIPDTRRID IIDRVRHACM
TEGRQAYWVC TLIEESELLE AQAAEATWEE LKLALPELNV GLVHGRMKPA EKQAVMTSFK
QGELHLLVAT TVIEVGVDVP NASLMIIENP ERLGLAQLHQ LRGRVGRGAV ASHCVLLYKT
PLSKTAQIRL QVLRDSNDGF VIAQKDLEIR GPGELLGTRQ TGNAEFKVAD LLRDQAMIPE
VQRLARHIHE RYPQQAKALI ERWMPETERY SNA
