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Database: UniProt
Entry: O34942
LinkDB: O34942
Original site: O34942 
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   16-OCT-2019, entry version 122.
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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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
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 a 3'- to 5'- polarity.
CC       Unwinds branched duplex DNA (Y-DNA) (By similarity).
CC       {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}.
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   SMR; O34942; -.
DR   STRING; 224308.BSU15870; -.
DR   PaxDb; O34942; -.
DR   PRIDE; O34942; -.
DR   EnsemblBacteria; CAB13460; CAB13460; BSU15870.
DR   GeneID; 936730; -.
DR   KEGG; bsu:BSU15870; -.
DR   PATRIC; fig|224308.179.peg.1727; -.
DR   eggNOG; ENOG4105CB5; Bacteria.
DR   eggNOG; COG1200; LUCA.
DR   HOGENOM; HOG000036619; -.
DR   InParanoid; O34942; -.
DR   KO; K03655; -.
DR   OMA; DNGFQAC; -.
DR   PhylomeDB; O34942; -.
DR   BioCyc; BSUB:BSU15870-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   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; IPR033454; RecG_wedge.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_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; Complete proteome; DNA damage; DNA recombination;
KW   DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    682       ATP-dependent DNA helicase RecG.
FT                                /FTId=PRO_0000102138.
FT   DOMAIN      271    432       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      451    611       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     284    291       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       385    388       DEQH box.
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
//
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