ID   RECG_STAAR              Reviewed;         686 AA.
AC   Q6GHK8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=ATP-dependent DNA helicase RecG;
DE            EC=3.6.4.12;
GN   Name=recG; OrderedLocusNames=SAR1203;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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) (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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX571856; CAG40205.1; -; Genomic_DNA.
DR   RefSeq; WP_001151515.1; NC_002952.2.
DR   AlphaFoldDB; Q6GHK8; -.
DR   SMR; Q6GHK8; -.
DR   KEGG; sar:SAR1203; -.
DR   HOGENOM; CLU_005122_7_1_9; -.
DR   OMA; DNGFQAC; -.
DR   OrthoDB; 234717at2; -.
DR   Proteomes; UP000000596; 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.
FT   CHAIN           1..686
FT                   /note="ATP-dependent DNA helicase RecG"
FT                   /id="PRO_0000102153"
FT   DOMAIN          279..439
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          462..618
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           392..395
FT                   /note="DEQH box"
FT   BINDING         292..299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   686 AA;  78391 MW;  0CF268315CB3939D CRC64;
     MAKVNLIESP YSLLQLKGIG PKKIEVLQQL NIHTVEDLVL YLPTRYEDNT VIDLNQAEDQ
     SNVTIEGQVY TAPVVAFFGR NKSKLTVHLM VNNIAVKCIF FNQPYLKKKI ELNQTITVKG
     KWNRVKQEIT GNRVFLNSQG TQTQENADVQ LEPVYRIKEG IKQKQIRDQI RQALNDVTIH
     EWLTDELREK YKLETLDFTL NTLHHPKSKE DLLRARRTYA FTELFLFELR MQWLNRLEKS
     SDEAIEIDYD LDQVKSFIDR LPFELTEAQK SSVNEIFRDL KAPIRMHRLL QGDVGSGKTV
     VAAICMYALK TAGYQSALMV PTEILAEQHA ESLIALFGDS MNVALLTGSV KGKKRKILLE
     QLENRTIDCL IGTHALIQDD VIFHNVGLVI TDEQHRFGVN QRQLLREKGA MTNVLFMTAT
     PIPRTLAISV FGEMDVSSIK QLPKGRKPII TTWAKHEQYD KVLMQMTSEL KKGRQAYVIC
     PLIESSEHLE DVQNVVALYE SLQQYYGVSR VGLLHGKLSA DEKDEVMQKF SNHEIDVLVS
     TTVVEVGVNV PNATFMMIYD ADRFGLSTLH QLRGRVGRSD QQSYCVLIAS PKTETGIERM
     TIMTQTTDGF ELSERDLEMR GPGDFFGVKQ SGLPDFLVAN LVEDYRMLEV ARDEAAELIQ
     SGVFFENTYQ HLRHFVEENL LHRSFD