Summary: Sporulation inhibitor A
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Sda protein domain Edit Wikipedia article
structure of the sda antikinase
In molecular biology, the protein domain Sda is short for suppressor of dnaA or otherwise known as sporulation inhibitor A. It is found only in bacteria. This protein domain is highly important to cell survival. When starved of nutrients, the cell is under extreme stress so undergoes a series of reactions to increase the chances of survival. One method is to form endospores which can withstand a large amount of environmental pressure. Sda protein domain is a checkpoint which prevents the formation of spores. The Sda domain affects cell signalling. It prevents the cell communicating the stress that it is under, which is crucial if the cell is to survive.
All cells communicate through cell signalling. The Sda protein domain inhibits the Histidine kinase signal transduction. This signal transduction mechanism is switched on when the cell is under stress, such as nutrient deprivation. It works through the kinase first autophosphorylating the Histidine residue and this triggers sporulation. Sda prevents this pathway from occurring by inhibiting the histidine kinase. More specifically, Sda can be considered an antikinase and binds to KinA. The Sda-KinA complex now physically blocks any phosphorylation of the Histidine Kinase residue.
These sporulation inhibitors are anti-kinases that bind to the histidine kinase KinA phosphotransfer protein domain and act as a molecular barricade that inhibit productive interaction between the ATP binding site and the phosphorylatable KinA His residue. This results in the inhibition of sporulation through the prevention of phosphorylation of spo0A, a transcription factor.
Members of this protein group contain two antiparallel alpha helices that are linked by an inter-helix loop to form a helical hairpin. These monomers associate to form a simple trimeric arrangement.
- Burkholder WF, Kurtser I, Grossman AD (2001). "Replication initiation proteins regulate a developmental checkpoint in Bacillus subtilis.". Cell 104 (2): 269–79. doi:10.1016/s0092-8674(01)00211-2. PMID 11207367.
- Rowland SL, Burkholder WF, Cunningham KA, Maciejewski MW, Grossman AD, King GF (2004). "Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis.". Mol Cell 13 (5): 689–701. doi:10.1016/S1097-2765(04)00084-X. PMID 15023339.
- Jacques DA, Streamer M, Rowland SL, King GF, Guss JM, Trewhella J et al. (2009). "Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state.". Acta Crystallogr D Biol Crystallogr 65 (Pt 6): 574–81. doi:10.1107/S090744490901169X. PMC 2725781. PMID 19465772.
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Sporulation inhibitor A Provide feedback
Members of this protein family contain two antiparallel alpha helices that are linked by a highly structured inter-helix loop to form a helical hairpin; the structure is stabilised by numerous hydrophobic and electrostatic interactions. These sporulation inhibitors are antikinases that bind to the histidine kinase KinA phosphotransfer domain and act as a molecular barricade that inhibit productive interaction between the ATP binding site and the phosphorylatable KinA His residue. This results in the inhibition of sporulation (by preventing phosphorylation of spo0A) .
Rowland SL, Burkholder WF, Cunningham KA, Maciejewski MW, Grossman AD, King GF; , Mol Cell. 2004;13:689-701.: Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis. PUBMED:15023339 EPMC:15023339
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015064
Members of this protein group contain two antiparallel alpha helices that are linked by a highly structured inter-helix loop to form a helical hairpin; the structure is stabilised by numerous hydrophobic and electrostatic interactions. These sporulation inhibitors are antikinases that bind to the histidine kinase KinA phosphotransfer domain and act as a molecular barricade that inhibit productive interaction between the ATP binding site and the phosphorylatable KinA His residue. This results in the inhibition of sporulation (by preventing phosphorylation of spo0A) [PUBMED:15023339].
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a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
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Curation and family details
|Author:||Mistry J, Sammut SJ|
|Number in seed:||19|
|Number in full:||423|
|Average length of the domain:||44.70 aa|
|Average identity of full alignment:||57 %|
|Average coverage of the sequence by the domain:||90.34 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -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 Sda domain has been found. There are 4 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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