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Database: UniProt
Entry: U6F209_LACHE
LinkDB: U6F209_LACHE
Original site: U6F209_LACHE 
ID   U6F209_LACHE            Unreviewed;       676 AA.
AC   U6F209;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=LHCIRMBIA951_00071 {ECO:0000313|EMBL:CDI58132.1};
OS   Lactobacillus helveticus CIRM-BIA 951.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1226334 {ECO:0000313|EMBL:CDI58132.1, ECO:0000313|Proteomes:UP000017248};
RN   [1] {ECO:0000313|EMBL:CDI58132.1, ECO:0000313|Proteomes:UP000017248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRM-BIA 951 {ECO:0000313|EMBL:CDI58132.1,
RC   ECO:0000313|Proteomes:UP000017248};
RA   Valence F., Chuat V., Ma L., Creno S., Falentin H., Lortal S., Bizet C.,
RA   Clermont D., Loux V., Bouchier C., Cousin S.;
RT   "Draft Genome Sequence of five Lactobacillus helveticus strains CIRM-BIA
RT   101T, 103, 104, 951 and 953 isolated from milk product.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:CDI58132.1}.
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DR   EMBL; CBUK010000051; CDI58132.1; -; Genomic_DNA.
DR   RefSeq; WP_023190680.1; NZ_HG530809.1.
DR   AlphaFoldDB; U6F209; -.
DR   STRING; 1587.ALV80_04285; -.
DR   HOGENOM; CLU_005122_7_1_9; -.
DR   Proteomes; UP000017248; 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   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:UP000017248}.
FT   DOMAIN          270..431
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          464..609
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   676 AA;  76110 MW;  2543D314CF211528 CRC64;
     MIENALFAPV TDLKGVGTKT AADLGSLGIY SIYYLLFYFP FRYDELQTLP LDQIMDGQKV
     VLKGFVATEP FVSRFGYKKS RLSFKMRIDH DVIMVNFFNQ PWLKSKIEIG EEVAIYGKYN
     VARQSLSAFK FIAAKENDSG MAPIYPVNRH VKQKKLVSLI NLAIDVFLDQ VRDIVPENIR
     EKYRLLTDQE IIQKMHHPKN STEANLAKRS AIFREFFIFE LQLALLANHD GKQAGYPKNY
     DLKEIAQLTS SLPFELSDDQ KEVVNEIFAD MHSSGQMRRL LQGDVGSGKT VVAVYAIFAA
     ITAGYQVALM VPTEILATQH FKKIDELLRP LGVRVALLTG NTKTLERREI YRELMDGTIN
     VMIGTHALIQ ENVIFKKLGL VIIDEQHRFG VGQRQALINK GDQPDILAMT ATPIPRTLAL
     TVYGDMTVSE IHHMPAGRKP IISSWKTSTQ MKDVYQKMQD QLDQGFQIYA VTPLITESET
     LDLKNAEELH AKLSHDFPDQ KVVLLHGQMP GPKKDEIMIA FASGEINILV TTSVIEVGVD
     VANANMMVIY NADRFGLSQL HQLRGRIGRG KTQSYCVFVA DPKTDSGKAR MKIIAATNDG
     FKLAEEDLKM RGEGDLFGKA QSGLPEFRVG DVVNNYNTLV VAQKVARDLV QQDPKLADYP
     TLKQVLEYKQ LEQNRI
//
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