The Lactococcus lactis sex-factor aggregation gene cluA.
A gene, cluA, was cloned from the chromosomally located sex factor of Lactococcus lactis MG1363. Sequence analysis revealed significant homology with previously described aggregation proteins in Enterococcus and Streptococcus species. The possibility that cluA was an equivalent protein involved in cell aggregation between donor and recipient bacteria during lactococcal conjugation was confirmed by its expression under the control of a heterologous promoter in L. lactis. Analysis of the homology between the CluA protein and the related proteins of Enterococcus and Streptococcus allowed a common structure for these proteins to be postulated. This consisted of five domains. Functionally conserved domains I and V act respectively as a secretory leader and C-terminal membrane anchor. Domains II and IV are conserved at the amino acid level and probably have common structural roles whereas domain III is variable and may control binding specificity.
Godon
J J
JJ
AFRC Institute of Food Research, Norwich, UK.
Jury
K
K
Shearman
C A
CA
Gasson
M J
MJ
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular; D003227:Conjugation, Genetic; D017931:DNA Primers / Q000235:genetics; D005144:F Factor / Q000235:genetics*; D015870:Gene Expression; D005798:Genes, Bacterial; D013294:Lactococcus lactis / Q000235:genetics*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D017931:DNA Primers