ID   RECG_STAEQ              Reviewed;         682 AA.
AC   Q5HPW4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=ATP-dependent DNA helicase RecG;
DE            EC=3.6.4.12;
GN   Name=recG; OrderedLocusNames=SERP0793;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW54116.1; -; Genomic_DNA.
DR   RefSeq; WP_002486268.1; NC_002976.3.
DR   AlphaFoldDB; Q5HPW4; -.
DR   SMR; Q5HPW4; -.
DR   STRING; 176279.SERP0793; -.
DR   EnsemblBacteria; AAW54116; AAW54116; SERP0793.
DR   KEGG; ser:SERP0793; -.
DR   eggNOG; COG1200; Bacteria.
DR   HOGENOM; CLU_005122_7_1_9; -.
DR   OMA; DNGFQAC; -.
DR   OrthoDB; 234717at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome.
FT   CHAIN           1..682
FT                   /note="ATP-dependent DNA helicase RecG"
FT                   /id="PRO_0000102157"
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;  78120 MW;  E918AC66082EB470 CRC64;
     MSKVHLIESP YALDKIKGIG PKRLALLEEL NIKSVEDLVL YLPTRYEDNT VIDLNQADDQ
     ATVTVQGEVY SSPTVAFFGR NKSKLTVHLM INHIAVKCVF FNQPYLKKKL ELNSIVTIKG
     KWNRNKQEIN GNRIFFNDQK NQEDAHLEPV YRVKEGIKQK QLRDNIRQAL SDVTIHEWLT
     DDLREKYKLE TLAYTIQTLH HPIDKQNLLR ARRTYAFTEL FMFELRMQWL NRLEKTSDEA
     IEINYDINKV KQFIDSLPFE LTDAQKVSVN EIFRDLKAPI RMHRLLQGDV GSGKTIVAAI
     CMYALKTAGY QSALMVPTEI LAEQHAESLM QLFGNTMNVA LLTGSVKGKK RRLLLEQLEN
     GTIDCLIGTH ALIQDDVVFN NVGLVITDEQ HRFGVNQRQI LREKGAMTNV LFMTATPIPR
     TLAISVFGEM DVSSIKQLPK GRKPIKTSWA KHEQYDQVLA QMSNELKKGR QAYVICPLIE
     SSEHLEDVQN VVELYESLQS DYGNEKVGLL HGKMTAEDKD QVMQKFSEHE IDILVSTTVV
     EVGVNVPNAT FMMIYDADRF GLSTLHQLRG RVGRSEHQSY CVLIASPKTE TGIERMTIMT
     QTTDGFELSE RDLEMRGPGD FFGVKQSGLP DFLVANVVED YRMLEVARDE AAELIQSGQF
     FEQQYSHLRE FIKQNLRHIR FD