spr1630 is responsible for the lethality of clpX mutations in Streptococcus pneumoniae.
The Clp protease ATPase subunit and chaperone ClpX is dispensable in some bacteria, but it is thought to be essential in others, including streptococci and lactococci. We confirm that clpX is essential in the Rx strain of Streptococcus pneumoniae but show that the requirement for clpX can be relieved by point mutations, frame shifts, or deletion of the gene spr1630, which is found in many isolates of S. pneumoniae. Homologs occur frequently in Staphylococcus aureus as well as in a few strains of Listeria monocytogenes, Lactobacillus johnsonii, and Lactobacillus rhamnosus. In each case, the spr1630 homolog is accompanied by a putative transcriptional regulator with an HTH DNA binding motif. In S. pneumoniae, the spr1630-spr1629 gene pair, accompanied by a RUP element, occurs as an island inserted between the trpA and cclA genes in 15 of 22 sequenced genomes.
Piotrowski
Andrew
A
Department of Biological Sciences, University of Illinois at Chicago, Chicago, IL 60607, USA.
Burghout
Peter
P
Morrison
Donald A
DA
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000502:physiology*; D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology*; D008957:Models, Genetic; D009154:Mutation; D016133:Polymerase Chain Reaction; D013296:Streptococcus pneumoniae / Q000235:genetics* / Q000254:growth & development
D001426:Bacterial Proteins; D000251:Adenosine Triphosphatases