ID A4G1Z1_HERAR Unreviewed; 711 AA.
AC A4G1Z1;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 2.
DT 24-JAN-2024, entry version 97.
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:CAL60528.2};
GN OrderedLocusNames=HEAR0301 {ECO:0000313|EMBL:CAL60528.2};
OS Herminiimonas arsenicoxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL60528.2, ECO:0000313|Proteomes:UP000006697};
RN [1] {ECO:0000313|EMBL:CAL60528.2, ECO:0000313|Proteomes:UP000006697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
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; CU207211; CAL60528.2; -; Genomic_DNA.
DR AlphaFoldDB; A4G1Z1; -.
DR STRING; 204773.HEAR0301; -.
DR KEGG; har:HEAR0301; -.
DR eggNOG; COG1200; Bacteria.
DR HOGENOM; CLU_005122_7_1_4; -.
DR Proteomes; UP000006697; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; 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|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU363016};
KW DNA recombination {ECO:0000256|RuleBase:RU363016};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU363016};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|RuleBase:RU363016, ECO:0000313|EMBL:CAL60528.2};
KW Hydrolase {ECO:0000256|RuleBase:RU363016, ECO:0000313|EMBL:CAL60528.2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363016};
KW Reference proteome {ECO:0000313|Proteomes:UP000006697}.
FT DOMAIN 296..467
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 490..646
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 78327 MW; CD364DE53EC80606 CRC64;
MKKKPVASAK TATQTAAKST AKAAAPAAAT RAAKIDDKLI KLGLRSDMDK VLHLPLRYED
ETEIRSISEA GFIFGRSVQV EGVVTACEVA FRPRRQLVVT ISDDSGQLVM RFLNFYGSQV
KQMAEGNRVR ARGEVRHGFF GAEMVHPSYK MVTEGAPLPS ALTPVYPAGE GLSQTLLRKT
IIDAMARIEW RDTLSEQLRS SLDLMSFEPA VRLLHNPPPD IDESVLADRS HAAWVRMKFD
ELLAQQLSMK RAQIARREKG AAVLPTIGKL SKAFLKQLPF SLTAAQQRVL EEVRADLKQS
FPMQRLLQGD VGSGKTVVAA IAAAQAIDSG FQAVLMAPTE ILADQHFRKI AGWMEPLGVN
VAWLTGSLKK KEKLEAKARI ESGVAQLIIG THALIQEDVQ FSKLGLVIVD EQHRFGVGQR
LVLRNKGLDA SAAAAQQKIP HQLMMSATPI PRTLAMTYYA DLEVSVIDEL PPGRTPIVTR
VIDQNRRDEV IERVHAAALE GRQVYWVCPL IEESEALQLQ TATDTHQTLV AALPDLQVGL
VHGRMKPADK QQVMDAFTRG DIHVLVATTV IEVGVDVPNA SLMVIEHAER FGLSQLHQLR
GRVGRGSTAS VCLLLYQGPL GMVAKQRLRI MRESTDGFEI ARKDLEIRGP GEFLGARQSG
QAMLRFADLE TDQWLVDRAR DLAQTLLRDD PATVGAHLAR WLGAREDYLK V
//