
Identification, sequence, and expression of Treponema denticola mcpA , a putative chemoreceptor gene
Author(s) -
Greene Shermalyn R,
Stamm Lola V
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb12780.x
Subject(s) - mcpa , treponema denticola , peptide sequence , gene , biology , nucleic acid sequence , multiple sequence alignment , homology (biology) , microbiology and biotechnology , biochemistry , amino acid , sequence alignment , genetics , chemistry , bacteria , porphyromonas gingivalis , pesticide , agronomy
The nucleotide sequence of a methyl‐accepting chemotaxis protein gene, mcpA , from Treponema denticola has been determined. The mcpA gene encodes a 729‐amino acid protein whose deduced amino acid sequence has significant homology with several bacterial MCPs. T . denticola McpA contains two N‐terminal transmembrane regions and two C‐terminal putative methylation sequences that are separated by a highly conserved signaling domain. The organization of these structural features is characteristic of MCPs. The observed molecular mass of the in vitro synthesized McpA (76.0 kDa) correlates with the predicted molecular mass of the protein (80.1 kDa).