Characterization of lipoprotein EnvA in Chlamydia psittaci 6BC.
The primary sequence of the small cysteine-rich protein (EnvA) of Chlamydia psittaci 6BC has been shown to possess a potential lipid modification/signal peptidase II-processing site, and the mature protein was labeled by a [3H]palmitic acid precursor. We further characterized the mature EnvA, showing that it lacks the N-terminal methionine of the primary peptide, is hydrophobic despite a peptide sequence that is predicted to be hydrophilic, and appears to be lipid modified at an N-terminal cysteine in a manner analogous to that of murein lipoproteins of gram-negative bacteria. We also report the fatty acid content of the small cysteine-rich proteins of C. psittaci and Chlamydia trachomatis L2 as determined by combined gas chromatography-mass spectrometry.
Everett
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Department of Microbiology and Immunology, University of Tennessee, Memphis 38163.
Desiderio
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Hatch
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D000143:Acids; D000468:Alkalies; D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D002692:Chlamydia trachomatis / Q000737:chemistry; D002691:Chlamydophila psittaci / Q000737:chemistry*; D003545:Cysteine / Q000737:chemistry; D005227:Fatty Acids / Q000032:analysis; D008401:Gas Chromatography-Mass Spectrometry; D006868:Hydrolysis; D008074:Lipoproteins / Q000737:chemistry*; D008565:Membrane Proteins; D008715:Methionine / Q000737:chemistry; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational
D000143:Acids; D000468:Alkalies; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; C089638:EnvA protein, Chlamydia psittaci; D005227:Fatty Acids; D008074:Lipoproteins; D008565:Membrane Proteins; C063931:Omp2 protein, bacteria; D008715:Methionine; D003545:Cysteine