ID A0A2Z6IBW5_9BURK Unreviewed; 734 AA.
AC A0A2Z6IBW5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:BBF24009.1};
GN ORFNames=SUTMEG_19000 {ECO:0000313|EMBL:BBF24009.1};
OS Sutterella megalosphaeroides.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=2494234 {ECO:0000313|EMBL:BBF24009.1, ECO:0000313|Proteomes:UP000271003};
RN [1] {ECO:0000313|EMBL:BBF24009.1, ECO:0000313|Proteomes:UP000271003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6FBBBH3 {ECO:0000313|EMBL:BBF24009.1,
RC ECO:0000313|Proteomes:UP000271003};
RX PubMed=30394865; DOI=10.1099/ijsem.0.003096;
RA Sakamoto M., Ikeyama N., Kunihiro T., Iino T., Yuki M., Ohkuma M.;
RT "Mesosutterella multiformis gen. nov., sp. nov., a member of the family
RT Sutterellaceae and Sutterella megalosphaeroides sp. nov., isolated from
RT human faeces.";
RL Int. J. Syst. Evol. Microbiol. 68:3942-3950(2018).
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; AP018786; BBF24009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6IBW5; -.
DR KEGG; sutt:SUTMEG_19000; -.
DR OrthoDB; 9804325at2; -.
DR Proteomes; UP000271003; 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 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:UP000271003}.
FT DOMAIN 311..490
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 512..669
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 80900 MW; 1A13D30D541FA86D CRC64;
MANTHTSTSR YAQEFGAASS ETSAARPRKG AAGRTAGVIR QEKLAPLSER LRKLGLVSDW
DFVLHLPLRY EDETRITPIG RLNPGEVQQA QGTVERSGFV ATPRGQQFSA ILSDGTGRLQ
LRFIHYYPSI QSQLQPGKTV RVFGEPREAF GGGLEIVHPR IKPPVSRTDN LPQALTPIYP
LGENIQQKWL RKRIDRAMLD LQVEDLVPVA VTERLGLPRL RESLEYLHNP PADASADALR
DRTDPHWERL KFDELLAQQI SLGETRRLAR KAVALVLAPR ADANLIVRFR EHLPFALTGA
QERVWKEIAS DLARPEPMHR LVQGDVGSGK TVVAALAALR AVEAGYQAAL MAPTEILAEQ
HFKKLVDWLT PLGIRTAWLT GRLKAAEKRR ALEEIASGEA RIVVGTHALI QDGVRFENLG
LAIVDEQHRF GVAQRLALRT NGAAGVESES GETVEADANA AKPHLLMLSA TPIPRTLAMS
YLADLDVSVI NELPPGRTPV TTKTIRIERK NEVVALVRAV VAEGRQAYWV CPLIEESEAL
DLTPAVQAAE ELQRALPDLK VALLHGAMSA PEKEAVMTAF ASGETDLLVA TTVIEVGVDV
PNATLMVIEH AERFGLAQLH QLRGRVGRGA ARSACLLLYG GELSELGRER LKIIRETTDG
FEIARRDLQL RGPGEFLGER QSGMPLLRFA NLETDGALLE AARREAERWL REDRDRALAH
ARRWFSAKAE FLAA
//
