Summary: YycH protein
YycH protein Provide feedback
This family contains the bacterial protein YycH which is approximately 450 residues long. YycH plays a role in signal transduction and is found immediately downstream of the essential histidine kinase YycG. YycG forms a two component system together with its cognate response regulator YycF. PhoA fusion studies have shown that YycH is transported across the cytoplasmic protein. It is postulated that YycH functions as an antagonist to YycG . The molecule is made up of three domains, and has a novel three-dimensional structure. The N-terminal domain features a calcium binding site and the central domain contains two conserved loop regions .
Fabret C, Hoch JA; , J Bacteriol 1998;180:6375-6383.: A two-component signal transduction system essential for growth of Bacillus subtilis: implications for anti-infective therapy. PUBMED:9829949 EPMC:9829949
Szurmant H, Nelson K, Kim EJ, Perego M, Hoch JA; , J Bacteriol 2005;187:5419-5426.: YycH regulates the activity of the essential YycFG two-component system in Bacillus subtilis. PUBMED:16030236 EPMC:16030236
Szurmant H, Zhao H, Mohan MA, Hoch JA, Varughese KI; , Protein Sci. 2006;15:929-934.: The crystal structure of YycH involved in the regulation of the essential YycFG two-component system in Bacillus subtilis reveals a novel tertiary structure. PUBMED:16600972 EPMC:16600972
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR009996
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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Both, YycH and YycI are always found in a 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. Structural studies show that these two protein families share two related domains.
The clan contains the following 2 members:YycH YycI
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Curation and family details
|Seed source:||Pfam-B_21457 (release 10.0)|
|Author:||Vella Briffa B, Szurmant H, Mistry J|
|Number in seed:||6|
|Number in full:||596|
|Average length of the domain:||421.40 aa|
|Average identity of full alignment:||30 %|
|Average coverage of the sequence by the domain:||97.23 %|
|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:||6|
|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 YycH domain has been found. There are 1 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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