The crystal structure of the yeast histidine phosphotransferase protein Ypd1. The four helices shown in yellow comprise the conserved four-helix bundle typical of monomeric HPt domains; the helices shown in red are insertions specific to Ypd1. The histidine phosphorylation site is shown in green. From PDB: 1C02.[1]
Identifiers
Symbol
Hpt
Pfam
PF01627
InterPro
IPR008207
SMART
HPT
PROSITE
PS50894
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Histidine phosphotransferase
The crystal structure of the Caulobacter crescentus histidine phosphotransferase protein ChpT in dimeric form. The four helices shown in yellow comprise the conserved four-helix bundle, with the histidine phosphorylation sites highlighted in green. The domains shown in red and tan are pseudo-CA domains that resemble the ATP-binding domains of histidine kinases, but do not bind or hydrolyze ATP. From PDB: 4FMT.[2]
Identifiers
Symbol
HPTransfase
Pfam
PF10090
InterPro
IPR018762
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Histidine phosphotransfer domains and histidine phosphotransferases (both often abbreviated HPt) are protein domains involved in the "phosphorelay" form of two-component regulatory systems. These proteins possess a phosphorylatable histidine residue and are responsible for transferring a phosphoryl group from an aspartate residue on an intermediate "receiver" domain, typically part of a hybrid histidine kinase, to an aspartate on a final response regulator.
^Song HK, Lee JY, Lee MG, Moon J, Min K, Yang JK, Suh SW (November 1999). "Insights into eukaryotic multistep phosphorelay signal transduction revealed by the crystal structure of Ypd1p from Saccharomyces cerevisiae". Journal of Molecular Biology. 293 (4): 753–61. doi:10.1006/jmbi.1999.3215. PMID 10543964.
^Cite error: The named reference blair was invoked but never defined (see the help page).
and 10 Related for: Histidine phosphotransfer domain information
Histidinephosphotransferdomains and histidine phosphotransferases (both often abbreviated HPt) are protein domains involved in the "phosphorelay" form...
N-terminal dimerization and histidinephosphotransfer (DHp) domain. In HK853-CD, crystallized from Thermotoga maritima, this domain is a helical-hairpin and...
phosphate from its kinase domain to its receiver domain. The phosphate is then transferred to a histidinephosphotransfer protein which then phosphorylates...
the Histidine Kinase residue. These sporulation inhibitors are anti-kinases that bind to the histidine kinase KinA phosphotransfer protein domain and...
own receiver domain, and a histidinephosphotransfer protein performs the final transfer to a response regulator. In many cases, histidine kinases are...
has been observed in many metal-binding phosphotransfer proteins. The central domain and the N-terminal domain form a shallow cleft, which makes up the...
phytohormone cytokinin. Cytokinin activates histidine kinases which then phosphorylate histidinephosphotransfer proteins. Subsequently, the phosphate groups...
retinal, which leads to phototransductory signalling via a two-component phosphotransfer relay system. Halobacterium salinarum has two SRs, SRI and SRII, which...
retinal, which leads to phototransductory signalling via a two-component phosphotransfer relay system. Halobacterium salinarum has two SRs, SRI and SRII, which...
of the Kai proteins possess DNA-binding domains. Instead, a two-component system consisting of SasA, a histidine kinase, and RpaA, a transcription factor...
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