ID   RECG_STAES              Reviewed;         682 AA.
AC   Q8CSV3;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=ATP-dependent DNA helicase RecG;
DE            EC=3.6.4.12;
GN   Name=recG; OrderedLocusNames=SE_0902;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04499.1; -; Genomic_DNA.
DR   RefSeq; NP_764457.1; NC_004461.1.
DR   RefSeq; WP_001830069.1; NZ_WBME01000001.1.
DR   AlphaFoldDB; Q8CSV3; -.
DR   SMR; Q8CSV3; -.
DR   STRING; 176280.SE_0902; -.
DR   EnsemblBacteria; AAO04499; AAO04499; SE_0902.
DR   GeneID; 50018960; -.
DR   KEGG; sep:SE_0902; -.
DR   PATRIC; fig|176280.10.peg.875; -.
DR   eggNOG; COG1200; Bacteria.
DR   HOGENOM; CLU_005122_7_1_9; -.
DR   OMA; DNGFQAC; -.
DR   Proteomes; UP000001411; 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..682
FT                   /note="ATP-dependent DNA helicase RecG"
FT                   /id="PRO_0000102156"
FT   DOMAIN          275..435
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          454..614
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           388..391
FT                   /note="DEQH box"
FT   BINDING         288..295
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   682 AA;  78086 MW;  9E0438156FA4D7C8 CRC64;
     MSKVHLIESP YALDKIKGIG PKRLALLEEL NIKSVEDLVL YLPTRYEDNT VIDLNQADDQ
     ATVTVQGEVY SSPTVAFFGR NKSKLTVHLM INHIAVKCVF FNQPYLKKKL ELNSIVTIKG
     KWNRNKQEIN GNRIFFKDQK NQEDTHLEPI YRIKEGIKQK QLRDNIRQAL SDVTIHEWLT
     DDLREKYKLE TLAYTIQTLH HPINKQNLLR ARRTYAFTEL FMFELRMQWL NRLEKTSDEA
     IEINYDINKV KQFIDSLPFE LTDAQKVSVN EIFRDLKAPI RMHRLLQGDV GSGKTVVAAI
     CMYALKTAGY QSALMVPTEI LAEQHAESLI QLFGNTMNVA LLTGSVKGKK RRLLLEQLEN
     GTIDCLIGTH ALIQDDVVFN NVGLVITDEQ HRFGVNQRQI LREKGAMTNV LFMTATPIPR
     TLAISVFGEM DVSSIKQLPK GRKPIKTSWA KHEQYDQVLA QMSNELKKGR QAYVICPLIE
     SSEHLEDVQN VVALYESLQS DYGNEKVGLL HGKMSAEDKD QVMQKFSKHE IDILVSTTVV
     EVGVNVPNAT FMMIYDADRF GLSTLHQLRG RVGRSEHQSY CVLIASPKTE TGIERMTIMT
     QTTDGFELSE RDLEMRGPGD FFGVKQSGLP DFLVANVVED YRMLEVARDE AAELIQSGQF
     FEQQYSHLRE FIKQNLRHIR FD