RECG_ECOLI
ID RECG_ECOLI Reviewed; 693 AA.
AC P24230; P76721; Q2M7W5;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=ATP-dependent DNA helicase RecG {ECO:0000303|PubMed:7957087};
DE EC=3.6.4.12 {ECO:0000269|PubMed:7957087};
GN Name=recG; Synonyms=radC {ECO:0000303|PubMed:11053371};
GN OrderedLocusNames=b3652, JW3627;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1938888; DOI=10.1128/jb.173.21.6837-6843.1991;
RA Lloyd R.G., Sharples G.J.;
RT "Molecular organization and nucleotide sequence of the recG locus of
RT Escherichia coli K-12.";
RL J. Bacteriol. 173:6837-6843(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1544582; DOI=10.1016/0378-1119(92)90449-y;
RA Kalman M., Murphy H., Cashel M.;
RT "The nucleotide sequence of recG, the distal spo operon gene in Escherichia
RT coli K-12.";
RL Gene 110:95-99(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION.
RX PubMed=7957087; DOI=10.1002/j.1460-2075.1994.tb06853.x;
RA Whitby M.C., Vincent S.D., Lloyd R.G.;
RT "Branch migration of Holliday junctions: identification of RecG protein as
RT a junction specific DNA helicase.";
RL EMBO J. 13:5220-5228(1994).
RN [7]
RP FUNCTION.
RX PubMed=7774596; DOI=10.1002/j.1460-2075.1995.tb07233.x;
RA Hong X., Cadwell G.W., Kogoma T.;
RT "Escherichia coli RecG and RecA proteins in R-loop formation.";
RL EMBO J. 14:2385-2392(1995).
RN [8]
RP MUTAGENESIS OF 411-TRP--ALA-693.
RX PubMed=11053371; DOI=10.1128/jb.182.22.6287-6291.2000;
RA Lombardo M.J., Rosenberg S.M.;
RT "radC102 of Escherichia coli is an allele of recG.";
RL J. Bacteriol. 182:6287-6291(2000).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / AB1157;
RX PubMed=12446634; DOI=10.1128/jb.184.24.6836-6844.2002;
RA Beam C.E., Saveson C.J., Lovett S.T.;
RT "Role for radA/sms in recombination intermediate processing in Escherichia
RT coli.";
RL J. Bacteriol. 184:6836-6844(2002).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / AB1157;
RX PubMed=25484163; DOI=10.1111/mmi.12899;
RA Cooper D.L., Boyle D.C., Lovett S.T.;
RT "Genetic analysis of Escherichia coli RadA: functional motifs and genetic
RT interactions.";
RL Mol. Microbiol. 95:769-779(2015).
CC -!- FUNCTION: Plays a critical role in recombination and DNA repair. Helps
CC process Holliday junction intermediates to mature products by
CC catalyzing branch migration. Has a DNA unwinding activity
CC characteristic of a DNA helicase with 3'- to 5'- polarity. Unwinds
CC branched duplex DNA (Y-DNA). Has a role in constitutive stable DNA
CC replication (cSDR) and R-loop formation. Is genetically synergistic to
CC RadA and RuvABC (PubMed:12446634, PubMed:25484163).
CC {ECO:0000269|PubMed:12446634, ECO:0000269|PubMed:25484163,
CC ECO:0000269|PubMed:7774596, ECO:0000269|PubMed:7957087}.
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 -!- INTERACTION:
CC P24230; P06959: aceF; NbExp=2; IntAct=EBI-556882, EBI-542707;
CC -!- DISRUPTION PHENOTYPE: Very slight sensitivity to ciprofloxacin (CFX),
CC UV and azidothymidine (AZT) in single deletion mutants, but a radA-recG
CC deletion is extremely sensitive to CFX and AZT, less so to UV
CC (PubMed:12446634, PubMed:25484163). The SOS response is induced in this
CC double mutant, indicating spontaneous DNA damage. AZT sensitivity is
CC suppressed by further recA or recF deletions, suggesting AZT-induced
CC DNA gaps are processed into lethal intermediates in a RecA-dependent
CC fashion mediated by RecF (PubMed:25484163).
CC {ECO:0000269|PubMed:12446634, ECO:0000269|PubMed:25484163}.
CC -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC {ECO:0000305}.
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DR EMBL; X59550; CAA42123.1; -; Genomic_DNA.
DR EMBL; M64367; AAA24513.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62005.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76676.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77641.1; -; Genomic_DNA.
DR PIR; JH0265; JH0265.
DR RefSeq; NP_418109.1; NC_000913.3.
DR RefSeq; WP_000678419.1; NZ_LN832404.1.
DR AlphaFoldDB; P24230; -.
DR SMR; P24230; -.
DR BioGRID; 4262929; 148.
DR DIP; DIP-10653N; -.
DR IntAct; P24230; 30.
DR STRING; 511145.b3652; -.
DR jPOST; P24230; -.
DR PaxDb; P24230; -.
DR PRIDE; P24230; -.
DR EnsemblBacteria; AAC76676; AAC76676; b3652.
DR EnsemblBacteria; BAE77641; BAE77641; BAE77641.
DR GeneID; 948162; -.
DR KEGG; ecj:JW3627; -.
DR KEGG; eco:b3652; -.
DR PATRIC; fig|511145.12.peg.3772; -.
DR EchoBASE; EB0822; -.
DR eggNOG; COG1200; Bacteria.
DR HOGENOM; CLU_005122_7_1_6; -.
DR InParanoid; P24230; -.
DR OMA; DNGFQAC; -.
DR PhylomeDB; P24230; -.
DR BioCyc; EcoCyc:EG10829-MON; -.
DR PRO; PR:P24230; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009379; C:Holliday junction helicase complex; IDA:EcoCyc.
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; IDA:EcoCyc.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:EcoCyc.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
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 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..693
FT /note="ATP-dependent DNA helicase RecG"
FT /id="PRO_0000102140"
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="DEQH box"
FT BINDING 296..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 411..693
FT /note="Missing: In radC102; causes mild UV and X-ray
FT sensitivity."
FT /evidence="ECO:0000269|PubMed:11053371"
SQ SEQUENCE 693 AA; 76430 MW; 7826143A8F4292A2 CRC64;
MKGRLLDAVP LSSLTGVGAA LSNKLAKINL HTVQDLLLHL PLRYEDRTHL YPIGELLPGV
YATVEGEVLN CNISFGGRRM MTCQISDGSG ILTMRFFNFS AAMKNSLAAG RRVLAYGEAK
RGKYGAEMIH PEYRVQGDLS TPELQETLTP VYPTTEGVKQ ATLRKLTDQA LDLLDTCAIE
ELLPPELSQG MMTLPEALRT LHRPPPTLQL SDLETGQHPA QRRLILEELL AHNLSMLALR
AGAQRFHAQP LSANDTLKNK LLAALPFKPT GAQARVVAEI ERDMALDVPM MRLVQGDVGS
GKTLVAALAA LRAIAHGKQV ALMAPTELLA EQHANNFRNW FAPLGIEVGW LAGKQKGKAR
LAQQEAIASG QVQMIVGTHA IFQEQVQFNG LALVIIDEQH RFGVHQRLAL WEKGQQQGFH
PHQLIMTATP IPRTLAMTAY ADLDTSVIDE LPPGRTPVTT VAIPDTRRTD IIDRVHHACI
TEGRQAYWVC TLIEESELLE AQAAEATWEE LKLALPELNV GLVHGRMKPA EKQAVMASFK
QGELHLLVAT TVIEVGVDVP NASLMIIENP ERLGLAQLHQ LRGRVGRGAV ASHCVLLYKT
PLSKTAQIRL QVLRDSNDGF VIAQKDLEIR GPGELLGTRQ TGNAEFKVAD LLRDQAMIPE
VQRLARHIHE RYPQQAKALI ERWMPETERY SNA
