ID D3UYK4_XENBS Unreviewed; 693 AA.
AC D3UYK4;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=ATP-dependent DNA helicase RecG {ECO:0000256|ARBA:ARBA00017846, ECO:0000256|RuleBase:RU363016};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU363016};
GN Name=recG {ECO:0000256|RuleBase:RU363016,
GN ECO:0000313|EMBL:CBJ79382.1};
GN OrderedLocusNames=XBJ1_0231 {ECO:0000313|EMBL:CBJ79382.1};
OS Xenorhabdus bovienii (strain SS-2004).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79382.1, ECO:0000313|Proteomes:UP000002045};
RN [1] {ECO:0000313|EMBL:CBJ79382.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79382.1};
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:E27909-E27909(2011).
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:0000256|RuleBase:RU363016}.
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:0000256|RuleBase:RU363016};
CC -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC {ECO:0000256|ARBA:ARBA00007504, ECO:0000256|RuleBase:RU363016}.
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DR EMBL; FN667741; CBJ79382.1; -; Genomic_DNA.
DR RefSeq; WP_012986845.1; NC_013892.1.
DR AlphaFoldDB; D3UYK4; -.
DR STRING; 406818.XBJ1_0231; -.
DR KEGG; xbo:XBJ1_0231; -.
DR PATRIC; fig|406818.4.peg.212; -.
DR eggNOG; COG1200; Bacteria.
DR HOGENOM; CLU_005122_7_1_6; -.
DR Proteomes; UP000002045; 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:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd17992; DEXHc_RecG; 1.
DR CDD; cd04488; RecG_wedge_OBF; 1.
DR CDD; cd18811; SF2_C_RecG; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047112; RecG/Mfd.
DR InterPro; IPR045562; RecG_dom3_C.
DR InterPro; IPR033454; RecG_wedge.
DR NCBIfam; TIGR00643; recG; 1.
DR PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF19833; RecG_dom3_C; 1.
DR Pfam; PF17191; RecG_wedge; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363016};
KW DNA damage {ECO:0000256|RuleBase:RU363016};
KW DNA recombination {ECO:0000256|RuleBase:RU363016};
KW DNA repair {ECO:0000256|RuleBase:RU363016};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU363016};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363016};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363016}.
FT DOMAIN 283..448
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 482..628
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 693 AA; 77283 MW; 9EAD585F88E2130F CRC64;
MKGRLLDAIP LTTLRGVGAS QVTKLAKLGL VNLQDLLLHL PLRYEDQTRL YSINDLLPGV
YATVTGEVLR THVTFGRRRI MTCQISDGTG VLTLRFFNFT AAMKNNLAEG KHVIAYGEIR
RGNQGPEIIH PEYKTQQHAE RIQLQDTLTP IYPTTEGVRQ TTLRKLIEQA LELLDTCVIN
ELLPEEFSRK LISLPNALHT LHRPPPDVSL TDLDNRRHPA QRRLILEELL AHHLSMLAVR
AGAQRFHAQQ LTADNSLKQQ LISQLPFVPT GAQVRVVAEI EQDLEKNVPM MRLIQGDVGS
GKTLVAALAA LRALVHGKQV ALMAPTELLA EQHANTFRQW FEPLGIQVGW LAGKQKGKAR
QAQQEAIANG QVSMVVGTHA MFQEQVRFSG LALVIIDEQH RFGVHQRLAL WEKGCEQGFH
PHQLIMTATP IPRTLAMTAY ADLDTSIIDE LPPGRTPVTT VAIPDTRRNE IIQRIKSACL
DEGRQAYWVC TLIEDSEVLE AQAAQATSEE LALILPDLKI GLVHGRMKPA EKQTIMDAFK
RGELQLLVAT TVIEVGVDVP NASLMIIDNP ERLGLAQLHQ LRGRVGRGAV ASHCVLLYKT
PLTNTAKIRL QVLRDSNDGF VIAQKDLEIR GPGELLGTRQ TGNAEFRIAD LLRDQGMLSE
VQRISSYIHQ HYPEHAKALI ERWLPDRSQY SHA
//
