Summary: YycH protein
YycH protein Provide feedback
This domain is exclusively found in YycI proteins in the low GC content Gram positive species. These two domains share the same structural fold with domains two and three of YycH  PF07435. Both, YycH and YycI are always found in pair on the chromosome, downstream of the essential histidine kinase YycG. Additionally, both proteins share a function in regulating the YycG kinase with which they appear to form a ternary complex. Lastly, the two proteins always contain an N-terminal transmembrane helix and are localized to the periplasmic space as shown by PhoA fusion studies.
Szurmant H, Mohan MA, Imus PM, Hoch JA; , J Bacteriol. 2007;189:3280-3289.: YycH and YycI interact to regulate the essential YycFG two-component system in Bacillus subtilis. PUBMED:17307850 EPMC:17307850
Santelli E, Liddington RC, Mohan MA, Hoch JA, Szurmant H; , J Bacteriol. 2007;189:3290-3295.: The crystal structure of Bacillus subtilis YycI reveals a common fold for two members of an unusual class of sensor histidine kinase regulatory proteins. PUBMED:17307848 EPMC:17307848
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR018604
The YycFG two-component system is the only signal transduction system in Bacillus subtilis known to be essential for cell viability. This system is highly conserved in low-G+C Gram-positive bacteria, regulating important processes such as cell wall homeostasis, cell membrane integrity, and cell division. Four other genes, yycHIJK, are organised within the same operon with yycF and yycG in B. subtilis.
YycI and YycH proteins interact to control the activity of the YycG kinase. Both YycI and YycH proteins are localized outside the cytoplasm and attached to the membrane by an N-terminal transmembrane sequence. Bacterial two-hybrid data showed that the YycH, YycI, and the kinase YycG form a ternary complex. The data suggest that YycH and YycI control the activity of YycG in the periplasm and that this control is crucial in regulating important cellular processes [PUBMED:17307850, PUBMED:17307848].
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Curation and family details
|Seed source:||Pfam-B_6483 (Release 21.0)|
|Author:||Bateman A, Szurmant H|
|Number in seed:||33|
|Number in full:||732|
|Average length of the domain:||224.20 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||82.91 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the YycI domain has been found. There are 12 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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