Abstract：
:The histidine protein kinase SppK is a peptide pheromone-activated kinase that regulates the production of the bacteriocin sakacin P in Lactobacillus sakei. SppK belongs to subfamily 10 of histidine protein kinases (HPKs), which regulate important processes in Gram-positive bacteria, including virulence, competence and bacteriocin production. To obtain insight into the functional properties of this relatively unknown class of HPKs, we have subjected SppK to random mutagenesis by error-prone PCR, followed by selection for mutants displaying a constitutive phenotype. Most identified mutations were clustered in a predicted coiled coil-like region, which is an important part of the HPK dimer interface and which includes the autophosphorylated histidine. Other mutations were located in the junctions between the dimerization domain and the membrane receptor domain or the catalytic kinase domain. Interestingly, two previously identified constitutive variants of ComD, an SppK homologue involved in competence regulation in Streptococcus pneumoniae, contained single mutations in the same regions.
journal_name
Arch Microbioljournal_title
Archives of microbiologyauthors
Mathiesen G,Axelsen GW,Axelsson L,Eijsink VGdoi
10.1007/s00203-005-0049-5keywords:
subject
Has Abstractpub_date
2006-01-01 00:00:00pages
327-34issue
5eissn
0302-8933issn
1432-072Xjournal_volume
184pub_type
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