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RUVB_PSEAE
ID   RUVB_PSEAE              Reviewed;         352 AA.
AC   Q51426; Q9I4Z6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Holliday junction ATP-dependent DNA helicase RuvB {ECO:0000255|HAMAP-Rule:MF_00016};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00016};
GN   Name=ruvB {ECO:0000255|HAMAP-Rule:MF_00016}; OrderedLocusNames=PA0967;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=8982068; DOI=10.1016/s0378-1119(96)00474-x;
RA   Hishida T., Iwasaki H., Ishioka K., Shinagawa H.;
RT   "Molecular analysis of the Pseudomonas aeruginosa genes, ruvA, ruvB and
RT   ruvC, involved in processing of homologous recombination intermediates.";
RL   Gene 182:63-70(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00016}.
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_00016};
CC   -!- SUBUNIT: Forms a complex with RuvA. {ECO:0000255|HAMAP-Rule:MF_00016}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00016}.
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DR   EMBL; D83138; BAA11819.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG04356.1; -; Genomic_DNA.
DR   PIR; A83525; A83525.
DR   RefSeq; NP_249658.1; NC_002516.2.
DR   RefSeq; WP_003086123.1; NZ_QZGE01000007.1.
DR   PDB; 6BLB; X-ray; 1.88 A; A=1-352.
DR   PDBsum; 6BLB; -.
DR   AlphaFoldDB; Q51426; -.
DR   SMR; Q51426; -.
DR   STRING; 287.DR97_970; -.
DR   PaxDb; Q51426; -.
DR   PRIDE; Q51426; -.
DR   EnsemblBacteria; AAG04356; AAG04356; PA0967.
DR   GeneID; 882028; -.
DR   KEGG; pae:PA0967; -.
DR   PATRIC; fig|208964.12.peg.1005; -.
DR   PseudoCAP; PA0967; -.
DR   HOGENOM; CLU_055599_1_0_6; -.
DR   InParanoid; Q51426; -.
DR   OMA; IHRMSRP; -.
DR   PhylomeDB; Q51426; -.
DR   BioCyc; PAER208964:G1FZ6-988-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009378; F:four-way junction helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071247; P:cellular response to chromate; IMP:PseudoCAP.
DR   GO; GO:0072715; P:cellular response to selenite ion; IMP:PseudoCAP.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IMP:PseudoCAP.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00016; DNA_helic_RuvB; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041445; AAA_lid_4.
DR   InterPro; IPR004605; DNA_helicase_Holl-junc_RuvB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008824; RuvB-like_N.
DR   InterPro; IPR008823; RuvB_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR42848; PTHR42848; 1.
DR   Pfam; PF17864; AAA_lid_4; 1.
DR   Pfam; PF05491; RuvB_C; 1.
DR   Pfam; PF05496; RuvB_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00635; ruvB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; DNA damage; DNA recombination; DNA repair;
KW   Helicase; Hydrolase; Nucleotide-binding; Reference proteome; SOS response.
FT   CHAIN           1..352
FT                   /note="Holliday junction ATP-dependent DNA helicase RuvB"
FT                   /id="PRO_0000165578"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00016"
FT   CONFLICT        146
FT                   /note="A -> G (in Ref. 1; BAA11819)"
FT                   /evidence="ECO:0000305"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           36..51
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           69..80
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           95..102
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           121..133
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   STRAND          157..163
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           165..167
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           170..174
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   STRAND          177..181
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           187..200
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           207..215
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           221..238
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   STRAND          239..243
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           245..254
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           264..277
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           284..291
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           295..300
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           303..308
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   STRAND          311..315
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   STRAND          318..321
FT                   /evidence="ECO:0007829|PDB:6BLB"
FT   HELIX           323..328
FT                   /evidence="ECO:0007829|PDB:6BLB"
SQ   SEQUENCE   352 AA;  38933 MW;  F24EE2804F12D7F1 CRC64;
     MIEPDRLISA VSGRERDEQL DRAIRPLKLA DYIGQPSVRE QMELFIHAAR GRQEALDHTL
     IFGPPGLGKT TLANIIAQEM GVSIKSTSGP VLERPGDLAA LLTNLEAGDV LFVDEIHRLS
     PIVEEVLYPA MEDFQLDIMI GEGPAARSIK LDLPPFTLVG ATTRAGMLTN PLRDRFGIVQ
     RLEFYNVEDL ATIVSRSAGI LGLEIEPQGA AEIAKRARGT PRIANRLLRR VRDFAEVRGQ
     GDITRVIADK ALNLLDVDER GFDHLDRRLL LTMIDKFDGG PVGIDNLAAA LSEERHTIED
     VLEPYLIQQG YIMRTPRGRV VTRHAYLHFG LNIPKRLGPG VTTDLFTSED GN
 
 
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