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Database: UniProt
Entry: Q329K4_SHIDS
LinkDB: Q329K4_SHIDS
Original site: Q329K4_SHIDS 
ID   Q329K4_SHIDS            Unreviewed;       693 AA.
AC   Q329K4;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=ATP-dependent DNA helicase RecG {ECO:0000256|ARBA:ARBA00017846, ECO:0000256|RuleBase:RU363016};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU363016};
GN   Name=recG {ECO:0000256|RuleBase:RU363016,
GN   ECO:0000313|EMBL:ABB64001.1};
GN   OrderedLocusNames=SDY_4084 {ECO:0000313|EMBL:ABB64001.1};
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267 {ECO:0000313|EMBL:ABB64001.1, ECO:0000313|Proteomes:UP000002716};
RN   [1] {ECO:0000313|EMBL:ABB64001.1, ECO:0000313|Proteomes:UP000002716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197 {ECO:0000313|EMBL:ABB64001.1,
RC   ECO:0000313|Proteomes:UP000002716};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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). {ECO:0000256|RuleBase:RU363016}.
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         Evidence={ECO:0000256|RuleBase:RU363016};
CC   -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC       {ECO:0000256|ARBA:ARBA00007504, ECO:0000256|RuleBase:RU363016}.
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DR   EMBL; CP000034; ABB64001.1; -; Genomic_DNA.
DR   RefSeq; WP_000678413.1; NC_007606.1.
DR   RefSeq; YP_405492.1; NC_007606.1.
DR   AlphaFoldDB; Q329K4; -.
DR   STRING; 300267.SDY_4084; -.
DR   EnsemblBacteria; ABB64001; ABB64001; SDY_4084.
DR   KEGG; sdy:SDY_4084; -.
DR   PATRIC; fig|300267.13.peg.4805; -.
DR   HOGENOM; CLU_005122_7_1_6; -.
DR   Proteomes; UP000002716; 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-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363016};
KW   DNA damage {ECO:0000256|RuleBase:RU363016};
KW   DNA recombination {ECO:0000256|RuleBase:RU363016};
KW   DNA repair {ECO:0000256|RuleBase:RU363016};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU363016};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363016};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363016};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002716}.
FT   DOMAIN          283..448
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          482..628
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   693 AA;  76530 MW;  98E985958FE6AED7 CRC64;
     MKGRLLDAVP LSSLTGVGAA LSNKLAKINL HTVQDLLLHL PLRYEDRTHL YPIGELLPGV
     YATVEGEVLN CNISFGGRRM MTCQISDGSG ILTMRFFNFN AAMKNSLATG RRVLAYGEAK
     RGKYGAEMIH PEYRVQGDLS TPELQETLTP VYPTTEGVKQ ATLRKLTDQA LDLLDTCAIE
     ELLPPELSQG MMTLPEALRT LHRPRPTLQL SDLETGQHPA QRRLILEELL AHNLSMLALR
     AGAQRFHAQP LSANDTLKNK LLAALPFKPT GAQARVVAEI ECDMALNVPM MRLVQGDVGS
     GKTLVAALAA LRAIAHGKQV ALMAPTELLA EQHANNFRNW FAPLGIEVGW LAGKQKGKAR
     LAQQEAIASG QVQMIVGTHA IFQEQVQFNG LALVIIDEQH RFGVHQRLAL WEKGQQQGFH
     PHQLIMTATP IPRTLAMTAY ADLDTSVIDE LPPGRTPVTT VAIPDTRRTD IIDRVRHACM
     TEGRQAYWVC TLIEESELLE AQAAEATWEE LKLALPELNV GLVHGRMKPA EKQAVMASFK
     QGELHLLVAT TVIEVGVDVP NASLMIIENP ERLGLAQLHQ LRGRVGRGAV ASHCVLLYKT
     PLSKTAQIRL QVLRDSNDGF VIAQKDLEIR GPGELLGTRQ TGNAEFKVAD LLRDQAMIPE
     VQRLARHIHE RYPQQAKALI ERWMPETERY SNA
//
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