ID   RECG_STAAW              Reviewed;         686 AA.
AC   Q8NX11;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=ATP-dependent DNA helicase RecG;
DE            EC=3.6.4.12;
GN   Name=recG; OrderedLocusNames=MW1110;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB94975.1; -; Genomic_DNA.
DR   RefSeq; WP_001151517.1; NC_003923.1.
DR   AlphaFoldDB; Q8NX11; -.
DR   SMR; Q8NX11; -.
DR   EnsemblBacteria; BAB94975; BAB94975; BAB94975.
DR   KEGG; sam:MW1110; -.
DR   HOGENOM; CLU_005122_7_1_9; -.
DR   OMA; DNGFQAC; -.
DR   Proteomes; UP000000418; 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_0000102155"
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;  78272 MW;  558E3BDFFC35BD1D CRC64;
     MAKVNLIESP YSLLQLKGIG PKKIEVLQQL NIHTVEDLVL YLPTRYEDNT VIDLNQAEDQ
     SNVTIEGQVY TAPVVAFFGR NNSKLTVHLM VNNIAVKCIF FNQPYLKKKI ELNQTITVKG
     KWNRVKQEIT GNRVFFNSQG TQTQENADVQ LEPVYRIKEG IKQKQIRDQI RQALNDVTIH
     EWLTDELREK YKLETLDFTL NTLHHPKSKE DLLRARRTYA FTELFLFELR MQWLNRLEKS
     SDEAIEIDYG LDQVKSFIDR LPFELTEAQK SSVNEIFRDL KAPIRMHRLL QGDVGSGKTV
     VAAICMYALK TAGYQSALMV PTEILAEQHA ESLMALFGDS MNVALLTGSV KGKKRKILLE
     QLENGTIDCL 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