ID Q65JR1_BACLD Unreviewed; 682 AA.
AC Q65JR1; Q62V66;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 129.
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:AAU23343.1};
GN OrderedLocusNames=BL02311 {ECO:0000313|EMBL:AAU23343.1};
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU23343.1, ECO:0000313|Proteomes:UP000000606};
RN [1] {ECO:0000313|EMBL:AAU23343.1, ECO:0000313|Proteomes:UP000000606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC {ECO:0000313|Proteomes:UP000000606};
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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|ARBA:ARBA00024832, 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; CP000002; AAU23343.1; -; Genomic_DNA.
DR RefSeq; WP_009328528.1; NC_006322.1.
DR AlphaFoldDB; Q65JR1; -.
DR STRING; 279010.BL02311; -.
DR GeneID; 66216181; -.
DR KEGG; bli:BL02311; -.
DR PATRIC; fig|279010.13.peg.1807; -.
DR eggNOG; COG1200; Bacteria.
DR HOGENOM; CLU_005122_7_1_9; -.
DR Proteomes; UP000000606; 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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000606}.
FT DOMAIN 271..432
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 451..611
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 682 AA; 77627 MW; 67DF0CE6C2C2879C CRC64;
MEHNLQLSIS VIKGVGTETE KTLNELGIYT VLDLLNYFPY RYDDYELRDL EDVAHDERVT
VEGKVHSEPS LAYYGKKRSR LTFRLLVGNY LITAVCFNRP YLKKKLAIGS IVTVTGKWDK
HRQSVMVQEL KNGPHQGDQS IEPVYSVKEN ITVKTMRKLI QEAVRSHLPF AEDPLPEKLR
TAYKLLSYQE AVKAMHKPES REALKHARRR FVYEEFLLFQ LKMQALRKFE REASDGISHT
FRLEDVNSFV KSLPFPLTNA QAKALDDILR DMASGYKMNR LLQGDVGSGK TAVAAIALYA
SLLSGFQGAM MVPTEILAEQ HADSLVSLFE QHDVNVALLT SSVKGKRRRE LLERLKEGEI
DILVGTHALI QDDVHFKQLG LVITDEQHRF GVEQRKKLRS KGKDPDVLFM TATPIPRTLA
ITVFGEMDVS VIDEMPAGRK RIETYWVKHD MLERILAFID KELKKGRQAY VICPLIEESD
KLDVQNAIDV HSMLTHAFRG RWQIGLMHGK LSNDEKEQVM RQFSKNECQI LVSTTVVEVG
VNVPNATVML IYDADRFGLS QLHQLRGRVG RGDHQSYCIL MADPKSETGK ERMSIMSETT
DGFELSEKDL ELRGPGDFFG KKQSGMPEFK VADMVHDYRA LETARRDAAE LVSSKAFWTD
AEYKSLREHL QNSGVMDGEK LS
//
