RECG_STAAM
ID RECG_STAAM Reviewed; 686 AA.
AC P64324; Q99UP1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ATP-dependent DNA helicase RecG;
DE EC=3.6.4.12;
GN Name=recG; OrderedLocusNames=SAV1227;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB57389.1; -; Genomic_DNA.
DR RefSeq; WP_001151509.1; NC_002758.2.
DR AlphaFoldDB; P64324; -.
DR SMR; P64324; -.
DR World-2DPAGE; 0002:P64324; -.
DR PaxDb; P64324; -.
DR EnsemblBacteria; BAB57389; BAB57389; SAV1227.
DR KEGG; sav:SAV1227; -.
DR HOGENOM; CLU_005122_7_1_9; -.
DR OMA; DNGFQAC; -.
DR PhylomeDB; P64324; -.
DR BioCyc; SAUR158878:SAV_RS06610-MON; -.
DR Proteomes; UP000002481; 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_0000102150"
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; 78344 MW; 1690A6502F53CCC6 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 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