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Database: UniProt
Entry: P96130
LinkDB: P96130
Original site: P96130 
ID   RECG_TREPA              Reviewed;         686 AA.
AC   P96130;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=ATP-dependent DNA helicase RecG;
DE            EC=3.6.4.12;
GN   Name=recG; OrderedLocusNames=TP_0687;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Nichols;
RA   Stamm L.V., Barnes N.Y.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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) (By similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U70661; AAB38707.1; -; Genomic_DNA.
DR   EMBL; AE000520; AAC65656.1; -; Genomic_DNA.
DR   PIR; D71292; D71292.
DR   RefSeq; WP_010882132.1; NC_021490.2.
DR   AlphaFoldDB; P96130; -.
DR   SMR; P96130; -.
DR   IntAct; P96130; 5.
DR   STRING; 243276.TP_0687; -.
DR   EnsemblBacteria; AAC65656; AAC65656; TP_0687.
DR   GeneID; 57879212; -.
DR   KEGG; tpa:TP_0687; -.
DR   eggNOG; COG1200; Bacteria.
DR   HOGENOM; CLU_005122_7_1_12; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000000811; Chromosome.
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-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd17992; DEXHc_RecG; 1.
DR   CDD; cd18811; SF2_C_RecG; 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; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..686
FT                   /note="ATP-dependent DNA helicase RecG"
FT                   /id="PRO_0000102161"
FT   DOMAIN          285..453
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          472..632
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           399..402
FT                   /note="DEQH box"
FT   BINDING         298..305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   686 AA;  77197 MW;  B05AFCDC6FA046B0 CRC64;
     MLIGEIKEPV SVLKGTGKVV LAQLERLNIS TIGDILSYWP RLWEDRTQEQ MFSQWTLAHR
     LQVRVSVTAH CWFGFGKSKT LKLVVQDGQG CVAELLCFRR NFLHFMFPVG SEAVVYGSFY
     EKDGLLESSS FDIEKIDCIE KKILPVYPLT KGLKQMKLRM LICAAMDQWI GTVDSELPKP
     ILEKYHLLTK RDVLLSMHTP RTLDDVAKGK HSLIFEEFFS LQMTIGMRSL QKRGRLPLTQ
     GESDQQSAIP SVVSELSLLQ KKLHRCLPFE LTVDQKRVIT EITQDLEREE PMARLIQGDV
     GSGKTLVAFF SCLKIIEQGG QVALLAPTEL LARQHADTAA RLLAPIGIRL AFLTGNVKSE
     GRAYLLEALV AGEINLVVGT HALFSKSVRY HDLRLVIIDE QHRFGVLQRS ALIQKGREGN
     PQGKTPHIIM MSATPIPRTL ALSVFGDLDI SIIKSMPGGR KPVITYIARK TKAEKVYEFV
     GNEIEKGRQA YFIYPRIHDI GLTDLKSVQC MYMYLKNYFA RYAVAMIHSK MTEEEQQRIM
     KYFSEGTVHI LVATSVVEVG VDVPNANCIV IEHAERFGLS ALHQLRGRVG RGDVQSYCFL
     MHGDEMTECA KRRLKIMGST ADGFVIAEED LKLRGPGDVG DTKNFEQSGY SGFRVADPVR
     DYPILQVARE AAFELLRKEK GSSEAR
//
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