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Database: UniProt
Entry: A0A0R1VX76_9LACO
LinkDB: A0A0R1VX76_9LACO
Original site: A0A0R1VX76_9LACO 
ID   A0A0R1VX76_9LACO        Unreviewed;       680 AA.
AC   A0A0R1VX76;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=FC89_GL000080 {ECO:0000313|EMBL:KRM07641.1};
OS   Liquorilactobacillus ghanensis DSM 18630.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423750 {ECO:0000313|EMBL:KRM07641.1, ECO:0000313|Proteomes:UP000051451};
RN   [1] {ECO:0000313|EMBL:KRM07641.1, ECO:0000313|Proteomes:UP000051451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18630 {ECO:0000313|EMBL:KRM07641.1,
RC   ECO:0000313|Proteomes:UP000051451};
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:KRM07641.1}.
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DR   EMBL; AZGB01000005; KRM07641.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1VX76; -.
DR   STRING; 1423750.FC89_GL000080; -.
DR   PATRIC; fig|1423750.3.peg.81; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000051451; 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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 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:UP000051451}.
FT   DOMAIN          271..434
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          453..613
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   680 AA;  76272 MW;  C55F4AB7BD7CD5BC CRC64;
     MSSLETILEQ SLASLKGVGP KTLQALQHLG ITTIEDLLTA FPFRYDDYRP KKIAELIDQE
     KVTLRGVVAT APVLVHFGRK KNRLNFNLQI DDQVVLVTFF NQGYLVDKVT QGAELTVFGK
     WESARQQLLG MKLLSLNKKE RLAGVYRSSK EIHATQLQRL VKQAFERYHL QISDLLPQNL
     QKKYHLLSRQ QMIHDMHFPA DQAAAQAAKR TAVYEEFFLF EARLQYLKQL DQQQSGLQIN
     YDNQQLKKFI SQLPFELTAA QKRSVNEICH DMHRPIHMNR LLQGDVGSGK TIVAAIAIYA
     AVTAGYQAAL MAPTEILARQ HADKLFRLFE PLGVNVSLLT GATTSGSRQR RELLQQLQKG
     AINVLVGTHA LIQNGVEFKN LGLVITDEQH RFGVNQRQAL RLKGVQPDVL ALTATPIPRT
     LALTVYGEMD VSIINELPQG RKPVKTFWLK KTQLQQAFNF IKEQLKQGQQ AYLVTPLVSE
     SEVLDLQNAE QLSEDATKFF APEYQVGLIH GKMKSDEKEQ IMTAFTGGKI AVLVATTVIE
     VGVDVPKASV ILILDADRFG LAQLHQLRGR VGRSSKQSYC LLVADPKTDY GRERLQTMTE
     TTDGFVIAQR DLELRGQGDV LGNKQAGLPE FKVADPVKDL RILQTAQIDA SQIVKQPDFG
     KTAATKPLLH YLQRQPLGFD
//
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