Protein Family Models

This domain is functionally uncharacterised. It is found as the periplasmic domain of the bacterial protein kinase PknH [1]. The domain is also found in isolation in numerous proteins, for example the lipoproteins lpqQ, lprH, lppH and lpqA from M. tuberculosis. This family of proteins is found in bacteria. Proteins in this family are typically between 214 and 268 amino acids in length. There are two completely conserved C residues that are likely to form a disulphide bond. A second pair of cysteines are less well conserved probably form a second disulphide bond. It seems likely that this domain functions to bind some as yet unknown ligand. [1]. 14690440. An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis. Molle V, Kremer L, Girard-Blanc C, Besra GS, Cozzone AJ, Prost JF;. Biochemistry. 2003;42:15300-15309. (from Pfam)

Date:

2024-10-16

These lipopolysaccharide kinases are related to protein kinases Pfam:PF00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica [1]. [1]. 11069912. Purification and characterization of WaaP from Escherichia coli, a lipopolysaccharide kinase essential for outer membrane stability. Yethon JA, Whitfield C;. J Biol Chem 2001;276:5498-5504. [2]. 12021457. Lipopolysaccharide phosphorylating enzymes encoded in the genomes of Gram-negative bacteria are related to the eukaryotic protein kinases. Krupa A, Srinivasan N;. Protein Sci 2002;11:1580-1584. [3]. 10531340. A Haemophilus influenzae gene that encodes a membrane bound 3-deoxy-D-manno-octulosonic acid (Kdo) kinase. Possible involvement of kdo phosphorylation in bacterial virulence. White KA, Lin S, Cotter RJ, Raetz CR;. J Biol Chem 1999;274:31391-31400. (from Pfam)

Date:

2024-10-16

Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [1]; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases. [1]. 3291115. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Hanks SK, Quinn AM, Hunter T;. Science. 1988;241:42-52. [2]. 1956325. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Hanks SK, Quinn AM;. Methods Enzymol 1991;200:38-62. [3]. 7768349. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. Hanks SK, Hunter T;. FASEB J 1995;9:576-596. [4]. 9020587. The protein kinases of budding yeast: six score and more. Hunter T, Plowman GD;. Trends Biochem Sci 1997;22:18-22. (from Pfam)

Date:

2024-10-16

Date:

2024-11-05

serine/threonine-protein kinase PknH/PknJ catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Date:

2023-05-26