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 27-MAR-2024, entry version 122.
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; Bacillota; 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 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 OrthoDB; 9804325at2; -.
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:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd17992; DEXHc_RecG; 1.
DR CDD; cd04488; RecG_wedge_OBF; 1.
DR CDD; cd18811; SF2_C_RecG; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047112; RecG/Mfd.
DR InterPro; IPR045562; RecG_dom3_C.
DR InterPro; IPR033454; RecG_wedge.
DR NCBIfam; TIGR00643; recG; 1.
DR PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF19833; RecG_dom3_C; 1.
DR Pfam; PF17191; RecG_wedge; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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
//
