RECG_BACSU
ID RECG_BACSU Reviewed; 682 AA.
AC O34942;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=ATP-dependent DNA helicase RecG;
DE EC=3.6.4.12;
GN Name=recG; Synonyms=ylpB; OrderedLocusNames=BSU15870;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9534248; DOI=10.1099/00221287-144-3-801;
RA Foulger D., Errington J.;
RT "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT genome.";
RL Microbiology 144:801-805(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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) (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}.
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DR EMBL; Y13937; CAA74246.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13460.1; -; Genomic_DNA.
DR PIR; H69879; H69879.
DR RefSeq; NP_389469.1; NC_000964.3.
DR RefSeq; WP_003244692.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34942; -.
DR SMR; O34942; -.
DR STRING; 224308.BSU15870; -.
DR PaxDb; O34942; -.
DR PRIDE; O34942; -.
DR EnsemblBacteria; CAB13460; CAB13460; BSU_15870.
DR GeneID; 936730; -.
DR KEGG; bsu:BSU15870; -.
DR PATRIC; fig|224308.179.peg.1727; -.
DR eggNOG; COG1200; Bacteria.
DR InParanoid; O34942; -.
DR OMA; DNGFQAC; -.
DR PhylomeDB; O34942; -.
DR BioCyc; BSUB:BSU15870-MON; -.
DR Proteomes; UP000001570; 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; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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..682
FT /note="ATP-dependent DNA helicase RecG"
FT /id="PRO_0000102138"
FT DOMAIN 271..432
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 451..611
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 385..388
FT /note="DEQH box"
FT BINDING 284..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 682 AA; 78141 MW; 5E479058D782295C CRC64;
MKQHQQTSIA NIKGIGPETE KTLNELGIYD ISDLLNYFPY RYDDYELRDL EEVKHDERVT
VEGKVHSEPS LTYYGKKRNR LTFRLLVGHY LITAVCFNRP YLKKKLSLGS VVTVSGKWDK
HRQTISVQEL KNGPHQEDKS IEPVYSVKEN VTVKMMRRFI QQALTQYADS LPDPLPEKLR
KSYKLPDYYQ ALKAMHQPET REALKLARRR FVYEEFLLFQ LKMQAFRKAE REQTQGIRQR
FSNEELMRFI KSLPFPLTNA QSRVLREITA DMSSPYRMNR LLQGDVGSGK TAVAAIALYA
AILSGYQGAL MVPTEILAEQ HADSLVSLFE KWDVSVALLT SSVKGKRRKE LLERLAAGEI
DILVGTHALI QDEVEFKALS LVITDEQHRF GVEQRKKLRN KGQDPDVLFM TATPIPRTLA
ITVFGEMDVS VIDEMPAGRK RIETYWVKHD MLDRILAFVE KELKQGRQAY IICPLIEESD
KLDVQNAIDV YNMLSDIFRG KWNVGLMHGK LHSDEKDQVM REFSANHCQI LVSTTVVEVG
VNVPNATIMV IYDADRFGLS QLHQLRGRVG RGEHQSFCIL MADPKSETGK ERMRIMSETN
DGFELSEKDL ELRGPGDFFG KKQSGMPEFK VADMVHDYRA LETARQDAAN LVASDAFWKE
PEYAVLRDEL LKSGVMDGEK LS