TCP pilus biosynthesis in Vibrio cholerae O1 : gene sequence of tcpC encoding an outer membrane lipoprotein

The nucleotide sequence of the tcpC gene has been determined. It encodes a 53995-Da protein precursor with a signal sequence and cleavage site typical of a number of outer membrane lipoproteins, which are cleaved by the equivalent of signal peptidase II (Lsp) of Escherichia coli. The location of the...

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Veröffentlicht in:FEMS microbiology letters 1992-10, Vol.97 (1-2), p.179-184
Hauptverfasser: OGIERMAN, M. A, MANNING, P. A
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description The nucleotide sequence of the tcpC gene has been determined. It encodes a 53995-Da protein precursor with a signal sequence and cleavage site typical of a number of outer membrane lipoproteins, which are cleaved by the equivalent of signal peptidase II (Lsp) of Escherichia coli. The location of the tcpC gene is such that it is predicted to be translationally coupled to the 5' and 3' flanking genes, tcpY and tcpD, respectively, indicating that it forms part of an operon. Together with the lipoprotein signal sequence and the several hydrophobic domains it seems likely that TcpC is a surface-anchored trans-outer membrane lipoprotein.
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source MEDLINE; Wiley Online Library All Journals; Alma/SFX Local Collection; Oxford University Press Journals Digital Archive Legacy
subjects Amino Acid Sequence
Bacterial Outer Membrane Proteins - biosynthesis
Bacterial Outer Membrane Proteins - genetics
Bacterial Toxins - biosynthesis
Bacterial Toxins - genetics
Base Sequence
Biological and medical sciences
DNA, Bacterial - genetics
Fimbriae, Bacterial - metabolism
Fundamental and applied biological sciences. Psychology
Genes, Bacterial
Lipoproteins - biosynthesis
Lipoproteins - genetics
Microbiology
Molecular Sequence Data
Morphology, structure, chemical composition, physicochemical properties
Sequence Homology, Amino Acid
Vibrio cholerae - genetics
Vibrio cholerae - metabolism
Virology
title TCP pilus biosynthesis in Vibrio cholerae O1 : gene sequence of tcpC encoding an outer membrane lipoprotein
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