RECG_STRPN
ID RECG_STRPN Reviewed; 671 AA.
AC Q54900;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ATP-dependent DNA helicase RecG;
DE EC=3.6.4.12;
GN Name=recG; Synonyms=mmsA; OrderedLocusNames=SP_1697;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8830261; DOI=10.1046/j.1365-2958.1996.445975.x;
RA Martin B., Sharples G.J., Humbert O., Lloyd R.G., Claverys J.-P.;
RT "The mmsA locus of Streptococcus pneumoniae encodes a RecG-like protein
RT involved in DNA repair and in three-strand recombination.";
RL Mol. Microbiol. 19:1035-1045(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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; Z49988; CAA90280.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK75775.1; -; Genomic_DNA.
DR PIR; B98064; B98064.
DR PIR; F95197; F95197.
DR PIR; S71016; S71016.
DR RefSeq; WP_001048775.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q54900; -.
DR SMR; Q54900; -.
DR STRING; 170187.SP_1697; -.
DR EnsemblBacteria; AAK75775; AAK75775; SP_1697.
DR KEGG; spn:SP_1697; -.
DR eggNOG; COG1200; Bacteria.
DR OMA; DNGFQAC; -.
DR PhylomeDB; Q54900; -.
DR BioCyc; SPNE170187:G1FZB-1720-MON; -.
DR Proteomes; UP000000585; 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:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR045562; RecG_dom3_C.
DR InterPro; IPR033454; RecG_wedge.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF19833; RecG_C; 1.
DR Pfam; PF17191; RecG_wedge; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00643; recG; 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.
FT CHAIN 1..671
FT /note="ATP-dependent DNA helicase RecG"
FT /id="PRO_0000102158"
FT DOMAIN 267..426
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 445..610
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 379..382
FT /note="DEQH box"
FT BINDING 280..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 196
FT /note="Y -> D (in Ref. 1; CAA90280)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="E -> A (in Ref. 1; CAA90280)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="M -> T (in Ref. 1; CAA90280)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="V -> A (in Ref. 1; CAA90280)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="V -> A (in Ref. 1; CAA90280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 671 AA; 75381 MW; 4DEC64E0E9DFF247 CRC64;
MNLHQPLHVL PGVGPKSAEK YAKLGIENLQ DLLLYFPFRY EDFKTKQVLE LEDGEKAVLS
GQVVTPASVQ YYGFKRNRLR FSLKQGEVVF AVNFFNQPYL ADKIELGATL AVFGKWDRAK
ASLTGMKVLA QVEDDLQPVY RLAQGISQAS LVKVIKTAFD QGLDLLIEEN LPQSLLDKYK
LMSRCQAVRA MHFPKYLAEY KQALRRIKFE ELFYFQMQLQ MLKSENRVQG SGLVLNWSQE
KVTAVKVSLP FALTQAQEKS LQEILTDMKS DHHMNRLLQG DVGSGKTVVA GLAMFAAVTA
GYQAALMVPT EILAEQHFES LQNLFPNLKL ALLTGSLKAA EKREVLETIA KGEADLIIGT
HALIQDGVEY ARLGLIIIDE QHRFGVGQRR ILREKGDNPD VLMMTATPIP RTLAITAFGD
MDVSIIDQMP AGRKPIVTRW IKHEQLPQVL TWLEGEIQKG SQVYVISPLI EESEALDLKN
AIALSEELTT HFAGKAEVAL LHGRMKSDEK DQIMQDFKER KTDILVSTTV IEVGVNVPNA
TVMIIMDADR FGLSQLHQLR GRVGRGDKQS YAVLVANPKT DSGKDRMRIM TETTNGFVLA
EEDLKMRGSG EIFGTRQSGL PEFQVADIIE DFPILEEARK VASYISSIEA WQEDPEWRMI
ALHLEKKEHL D
