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Database: UniProt
Entry: A0A0R1RFY4_9LACO
LinkDB: A0A0R1RFY4_9LACO
Original site: A0A0R1RFY4_9LACO 
ID   A0A0R1RFY4_9LACO        Unreviewed;       679 AA.
AC   A0A0R1RFY4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=FD01_GL001286 {ECO:0000313|EMBL:KRL53186.1};
OS   Lacticaseibacillus manihotivorans DSM 13343 = JCM 12514.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1423769 {ECO:0000313|EMBL:KRL53186.1, ECO:0000313|Proteomes:UP000051790};
RN   [1] {ECO:0000313|EMBL:KRL53186.1, ECO:0000313|Proteomes:UP000051790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13343 {ECO:0000313|EMBL:KRL53186.1,
RC   ECO:0000313|Proteomes:UP000051790};
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:KRL53186.1}.
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DR   EMBL; AZEU01000018; KRL53186.1; -; Genomic_DNA.
DR   RefSeq; WP_056962296.1; NZ_AZEU01000018.1.
DR   AlphaFoldDB; A0A0R1RFY4; -.
DR   PATRIC; fig|1423769.4.peg.1386; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000051790; 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   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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000051790}.
FT   DOMAIN          269..430
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          449..614
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   COILED          447..495
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   679 AA;  74755 MW;  E7206D21C34DCE1D CRC64;
     MGLTDPASTL PGVGPKRAEA LASLDIHTVG DVLFYFPFRY DDLQVKSLDE AADQEKITIK
     GIVVADPVVS RFGPRKNRLN VRVQVDRAVV MVTFFNQPWL KDKFTQGMEA AIYGKWDAKR
     HSMTGMKVLA TQTEDAPSMA AIYPANKNIR QSTLAELAKA AFAKEQGHIP DIIPQVIREK
     LRLHSDEQLI QGMHWPKTPA EAKAARRTAI FREFFLFECQ IQSLREDSQL AANGLAIPFD
     NQQVRGLIKT LPFALTTAQK RVVNEICADM RSPKHMNRLL QGDVGSGKTI VAAIALYAAV
     TARFQAALMV PTEVLAEQHF AKLTKLFADF PVKLALLTGT TKGKQRKATL EGLASGDIDI
     VIGTHALIQK AVDYANLGLA IIDEQHRFGV KQRQILQDKG LKPDLLAMTA TPIPRTLAIT
     TYGEMDVSTI DELPAGRQPI TTTWVRHNQM REALQRMQQE LNAHHQIFAI TPLIAESEKI
     DLQNAEQLYA DMQKVFGKAA KVALLHGQMK ADEKDAIMRA FSDGEIDLLV STTVVEVGVD
     VPNATVMLIM DADRFGLAQL HQLRGRVGRG KSAAYCILVA DPKNDMGVER MQTMVTTTDG
     FKLAEKDLEL RGSGDIFGDK QSGLPEFRVA DPVADFATLS AAQQVAASLF KTDPSLSAPE
     FAPLRAYLAR QQQLVGTLD
//
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