A dimeric two-component receiver domain inhibits the sigma54-dependent ATPase in DctD.
Meyer
M G
MG
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Park
S
S
Zeringue
L
L
Staley
M
M
McKinstry
M
M
Kaufman
R I
RI
Zhang
H
H
Yan
D
D
Yennawar
N
N
Yennawar
H
H
Farber
G K
GK
Nixon
B T
BT
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D019281:Dimerization; D010766:Phosphorylation; D017434:Protein Structure, Tertiary; D051877:RNA Polymerase Sigma 54; D012808:Sigma Factor / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D012808:Sigma Factor; D014157:Transcription Factors; C073788:dctD protein, Rhizobium meliloti; D012321:DNA-Directed RNA Polymerases; D051877:RNA Polymerase Sigma 54; D000251:Adenosine Triphosphatases