RECG_ECO57
ID RECG_ECO57 Reviewed; 693 AA.
AC Q8XD86;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=ATP-dependent DNA helicase RecG;
DE EC=3.6.4.12;
GN Name=recG; OrderedLocusNames=Z5078, ECs4527;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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). Has a role in constitutive stable DNA replication (CsdR) and R-
CC loop formation (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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG58796.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG58796.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB37950.1; -; Genomic_DNA.
DR PIR; G91194; G91194.
DR PIR; H86041; H86041.
DR RefSeq; NP_312554.1; NC_002695.1.
DR RefSeq; WP_000147776.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XD86; -.
DR SMR; Q8XD86; -.
DR STRING; 155864.EDL933_4915; -.
DR EnsemblBacteria; AAG58796; AAG58796; Z5078.
DR EnsemblBacteria; BAB37950; BAB37950; ECs_4527.
DR GeneID; 915516; -.
DR KEGG; ece:Z5078; -.
DR KEGG; ecs:ECs_4527; -.
DR PATRIC; fig|386585.9.peg.4745; -.
DR eggNOG; COG1200; Bacteria.
DR HOGENOM; CLU_005122_7_1_6; -.
DR OMA; DNGFQAC; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; 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; Reference proteome.
FT CHAIN 1..693
FT /note="ATP-dependent DNA helicase RecG"
FT /id="PRO_0000102141"
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"
SQ SEQUENCE 693 AA; 76496 MW; 0BC60DAE761C3172 CRC64;
MTGRLLDAVP LSSLTGVGAA LSNKLAKINL HTVQDLLLHL PLRYEDRTHL YPIGELLPGV
YATVEGEVLN CNISFGGRRM MTCQISDGSG ILTMRFFNFS AAMKNSLATG RRVLAYGEAK
RGKYGAEMIH PEYRVQGDLS TPELQETLTP VYPTTEGVKQ ATLRKLTDQA LDLLDTCAIE
ELLPPELSQG MMTLPEALRT LHRPPPTLQL SDLETGQHPA QRRLILEELL AHNLSMLALR
AGAQRFHAQP LSANDALKNK LLAALPFKPT GAQARVVAEI ERDMALDVPM MRLVQGDVGS
GKTLVAALAA LRAIAHGKQV ALMAPTELLA EQHANNFRNW FEPLGIEVGW LAGKQKGKAR
LSQQEAIASG QVQMIVGTHA IFQEQVQFNG LALVIIDEQH RFGVHQRLAL WEKGQQQGFH
PHQLIMTATP IPRTLAMTAY ADLDTSVIDE LPPGRTPVTT VAIPDTRRTD IIDRVRHACI
TEGRQAYWVC TLIEESELLE AQAAEATWEE LKLALPELNV GLVHGRMKPA EKQAVMASFK
QGELHLLVAT TVIEVGVDVP NASLMIIENP ERLGLAQLHQ LRGRVGRGAV ASHCVLLYKT
PLSKTAQIRL QVLRDSNDGF VIAQKDLEIR GPGELLGTRQ TGNAEFKVAD LLRDQAMIPE
VQRLARHIHE RYPQQAKALI ERWMPETERY SNA
