Sampson J S, O'Connor S P, Holloway B P, Plikaytis B B, Carlone G M, Mayer L W
Division of Bacterial Diseases, Centers for Disease Control, Atlanta, Georgia 30333.
Infect Immun. 1990 Sep;58(9):3154-7. doi: 10.1128/iai.58.9.3154-3157.1990.
Gene htpB, which encodes the 58-kilodalton protein of Legionella pneumophila, was cloned in Escherichia coli and its complete nucleotide sequence was determined. Analysis of this sequence revealed an open reading frame of 1,644 nucleotides encoding a protein with a predicted molecular mass of 57,952 daltons. Data obtained by amino-terminal sequencing of the purified 58-kilodalton protein agreed, except for one amino acid residue, with the predicted amino acid sequence, identifying this open reading frame as htpB. A comparison of the primary structure of this protein to other proteins of similar molecular weights from E. coli, Mycobacterium leprae, M. tuberculosis, and Coxiella burnetii revealed significant regions of sequence similarity, which are discussed.
编码嗜肺军团菌58千道尔顿蛋白的基因htpB在大肠杆菌中克隆,并测定了其完整的核苷酸序列。对该序列的分析揭示了一个1644个核苷酸的开放阅读框,编码一种预测分子量为57952道尔顿的蛋白质。通过对纯化的58千道尔顿蛋白进行氨基末端测序获得的数据,除一个氨基酸残基外,与预测的氨基酸序列一致,从而确定该开放阅读框为htpB。将该蛋白的一级结构与来自大肠杆菌、麻风分枝杆菌、结核分枝杆菌和伯纳特柯克斯体的其他相似分子量的蛋白质进行比较,发现了显著的序列相似区域,并对其进行了讨论。