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Database: UniProt
Entry: A0A0R1HJG7_9LACO
LinkDB: A0A0R1HJG7_9LACO
Original site: A0A0R1HJG7_9LACO 
ID   A0A0R1HJG7_9LACO        Unreviewed;       677 AA.
AC   A0A0R1HJG7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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   ORFNames=FC66_GL000135 {ECO:0000313|EMBL:KRK46512.1};
OS   Dellaglioa algida DSM 15638.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Dellaglioa.
OX   NCBI_TaxID=1423719 {ECO:0000313|EMBL:KRK46512.1, ECO:0000313|Proteomes:UP000051450};
RN   [1] {ECO:0000313|EMBL:KRK46512.1, ECO:0000313|Proteomes:UP000051450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15638 {ECO:0000313|EMBL:KRK46512.1,
RC   ECO:0000313|Proteomes:UP000051450};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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|ARBA:ARBA00024832, 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRK46512.1}.
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DR   EMBL; AZDI01000001; KRK46512.1; -; Genomic_DNA.
DR   RefSeq; WP_057973457.1; NZ_AZDI01000001.1.
DR   AlphaFoldDB; A0A0R1HJG7; -.
DR   STRING; 1423719.FC66_GL000135; -.
DR   PATRIC; fig|1423719.4.peg.137; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000051450; Unassembled WGS sequence.
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:UP000051450}.
FT   DOMAIN          267..428
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          447..607
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   677 AA;  76139 MW;  615C001D3A179F1A CRC64;
     MASLDDSVGV LTGVGPKKLT ALNQLGINTI EDLLTFYPYR YDDLKAKKLS EITDQEKVTL
     KGTVSSEPVL VRFGQKRNLL NVRLLVDDGN ITVSFFNQPF LQKQFEIGKE VAVYGKWDDK
     RKSLSGMKLL TKQTDDGLAA IYRSSKDIHQ TAIRQLITQA FEQYADEVGS LLPTELIQKY
     RLVNRKMMLH DIHFPKDEKN FHEAKRTAIF EEFFLFQLKL QYVKKTDTKN YGIKINYQNN
     ELKKFIQTLP FELTAAQKKV VNEICADMKQ AIHMNRLLQG DVGSGKTIVA AIVMYAAITA
     GYQAVLMAPT EILAEQHANN MATLFADFPV NVALLTGSMK VKARRELLAH LESGEVNLIV
     GTHAIIQPDV SFKRVGLVIT DEQHRFGVNQ RRILREKGAE PDVLAMTATP IPRTLAITAY
     GEMDVSTINE LPAGRQPITT SWLKSSQVGK GIDLIKEQLA QGSQAYIITP LIDESETLDL
     KNALALYENM KEIFEPKYKV GLLHGKMKND EKDQMMADFK ANKYQALVST TVIEVGVDVP
     NATVMMIYNA ERFGLAQLHQ LRGRVGRGKK ASYCVLIADP KNEFGIQRMQ IMTETTDGFV
     ISQKDLELRG AGDVLGRKQS GIPEFKIGDP IGDINALQVA QQEAHEIVFR DDFENNPEFK
     PLNDYLKEHQ NTDLKFD
//
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