Molecular characterization of the p100 gene of Borrelia burgdorferi strain PKo.
The p100 gene coding for the p100 protein of Borrelia burgdorferi strain PKo has been cloned, sequenced and expressed in Escherichia coli. An open reading frame including upstream and downstream sequences with potential translation and transcription signals could be identified. The reading frame consists of 1989 nucleotides corresponding to a protein of 663 amino acids and a calculated molecular mass of 75.8 kDa. The protein has a leader peptide and is processed without modification at the N-terminus. A high percentage of amino acid sequence identity could be found to the high-molecular mass protein p83/p93 of B. burgdorferi strain B31.
Jauris-Heipke
S
S
Abteilung Serologie, Max von Pettenkofer Institute, Munich, FRG.
Fuchs
R
R
Hofmann
A
A
Lottspeich
F
F
Preac-Mursic
V
V
Soutschek
E
E
Will
G
G
Wilske
B
B
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D015748:Borrelia burgdorferi Group / Q000737:chemistry / Q000145:classification / Q000235:genetics*; D005798:Genes, Bacterial / Q000235:genetics*; D008969:Molecular Sequence Data; D013045:Species Specificity
D001426:Bacterial Proteins; C085289:p100 protein, Borrelia