RECG_STAA8
ID RECG_STAA8 Reviewed; 686 AA.
AC O50581; Q2FZ57;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=ATP-dependent DNA helicase RecG;
DE EC=3.6.4.12;
GN Name=recG; OrderedLocusNames=SAOUHSC_01194;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9257758; DOI=10.1128/aac.41.8.1770;
RA Niga T., Yoshida H., Hattori H., Nakamura S.;
RT "Cloning and sequencing of a novel gene (recG) that affects the quinolone
RT susceptibility of Staphylococcus aureus.";
RL Antimicrob. Agents Chemother. 41:1770-1774(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; AB000439; BAA24572.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30301.1; -; Genomic_DNA.
DR RefSeq; WP_001151499.1; NZ_LS483365.1.
DR RefSeq; YP_499733.1; NC_007795.1.
DR AlphaFoldDB; O50581; -.
DR SMR; O50581; -.
DR STRING; 1280.SAXN108_1227; -.
DR EnsemblBacteria; ABD30301; ABD30301; SAOUHSC_01194.
DR GeneID; 3919327; -.
DR KEGG; sao:SAOUHSC_01194; -.
DR PATRIC; fig|93061.5.peg.1097; -.
DR eggNOG; COG1200; Bacteria.
DR HOGENOM; CLU_005122_7_1_9; -.
DR OMA; DNGFQAC; -.
DR PRO; PR:O50581; -.
DR Proteomes; UP000008816; 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; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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..686
FT /note="ATP-dependent DNA helicase RecG"
FT /id="PRO_0000102152"
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; 78343 MW; D3405F218D45432B CRC64;
MAKVNLIESP YSLLQLKGIG PKKIEVLQQL NIHTVEDLVL YLPTRYEDNT VIDLNQAEDQ
SNVTIEGQVY TAPVVAFFGR NKSKLTVHLM VNNIAVKCIF FNQPYLKKKI ELNQTITVKG
KWNRVKQEIT GNRVFFNSQG TQTQENADVQ LEPVYRIKEG IKQKQIRDQI RQALNDVTIH
EWLTDELREK YKLETLDFTL NTLHHPKSKE DLLRARRTYA FTELFLFELR MQWLNRLEKS
SDEAIEIDYD IDQVKSFIDR 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 SNHEINVLVS
TTVVEVGVNV PNATFMMIYD ADRFGLSTLH QLRGRVGRSD QQSYCVLIAS PKTETGIERM
TIMTQTTDGF ELSERDLEMR GPGDFFGVKQ SGLPDFLVAN LVEDYRMLEV ARDEAAELIQ
SGVFFENTYQ HLRHFVEENL LHRSFD