RUVA_MYCLE
ID RUVA_MYCLE Reviewed; 203 AA.
AC P40832;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Holliday junction ATP-dependent DNA helicase RuvA {ECO:0000255|HAMAP-Rule:MF_00031};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00031};
GN Name=ruvA {ECO:0000255|HAMAP-Rule:MF_00031}; OrderedLocusNames=ML0482;
GN ORFNames=B1177_C2_188;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=9774974; DOI=10.1016/s1097-2765(00)80280-4;
RA Roe S.M., Barlow T., Brown T., Oram M., Keeley A., Tsaneva I.R.,
RA Pearl L.H.;
RT "Crystal structure of an octameric RuvA-Holliday junction complex.";
RL Mol. Cell 2:361-372(1998).
CC -!- FUNCTION: The RuvA-RuvB complex in the presence of ATP renatures
CC cruciform structure in supercoiled DNA with palindromic sequence,
CC indicating that it may promote strand exchange reactions in homologous
CC recombination. RuvAB is a helicase that mediates the Holliday junction
CC migration by localized denaturation and reannealing. RuvA stimulates,
CC in the presence of DNA, the weak ATPase activity of RuvB.
CC {ECO:0000255|HAMAP-Rule:MF_00031}.
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:0000255|HAMAP-Rule:MF_00031};
CC -!- SUBUNIT: Forms a complex with RuvB. {ECO:0000255|HAMAP-Rule:MF_00031}.
CC -!- SIMILARITY: Belongs to the RuvA family. {ECO:0000255|HAMAP-
CC Rule:MF_00031}.
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DR EMBL; U00011; AAA17095.1; -; Genomic_DNA.
DR EMBL; AL583918; CAC29990.1; -; Genomic_DNA.
DR PIR; S72731; S72731.
DR RefSeq; NP_301422.1; NC_002677.1.
DR RefSeq; WP_010907746.1; NC_002677.1.
DR PDB; 7OA5; X-ray; 2.38 A; A/B/C/D/E/F/G/H=1-203.
DR PDBsum; 7OA5; -.
DR AlphaFoldDB; P40832; -.
DR SMR; P40832; -.
DR STRING; 272631.ML0482; -.
DR EnsemblBacteria; CAC29990; CAC29990; CAC29990.
DR KEGG; mle:ML0482; -.
DR PATRIC; fig|272631.5.peg.845; -.
DR Leproma; ML0482; -.
DR eggNOG; COG0632; Bacteria.
DR HOGENOM; CLU_087936_2_1_11; -.
DR OMA; VGMAVQC; -.
DR EvolutionaryTrace; P40832; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0009379; C:Holliday junction helicase complex; IEA:InterPro.
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:0009378; F:four-way junction helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd14332; UBA_RuvA_C; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00031; DNA_helic_RuvA; 1.
DR InterPro; IPR013849; DNA_helicase_Holl-junc_RuvA_I.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000085; RuvA.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR011114; RuvA_C.
DR InterPro; IPR036267; RuvA_C_sf.
DR Pfam; PF07499; RuvA_C; 1.
DR Pfam; PF01330; RuvA_N; 1.
DR SMART; SM00278; HhH1; 2.
DR SUPFAM; SSF46929; SSF46929; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00084; ruvA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW SOS response.
FT CHAIN 1..203
FT /note="Holliday junction ATP-dependent DNA helicase RuvA"
FT /id="PRO_0000094649"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:7OA5"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:7OA5"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:7OA5"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:7OA5"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:7OA5"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:7OA5"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:7OA5"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:7OA5"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:7OA5"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:7OA5"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:7OA5"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:7OA5"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:7OA5"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:7OA5"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:7OA5"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:7OA5"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:7OA5"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:7OA5"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:7OA5"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:7OA5"
SQ SEQUENCE 203 AA; 20751 MW; 2C76B0144DB95006 CRC64;
MIFSVRGEVL EVALDHAVIE AAGIGYRVNA TPSALATLRQ GSQARLVTAM VVREDSMTLY
GFSDAENRDL FLALLSVSGV GPRLAMATLA VHDAAALRQA LADSDVASLT RVPGIGKRGA
ERIVLELRDK VGPVGASGLT VGTAADGNAV RGSVVEALVG LGFAAKQAEE ATDQVLDGEL
GKDGAVATSS ALRAALSLLG KTR
