Noble J A, Innis M A, Koonin E V, Rudd K E, Banuett F, Herskowitz I
Cetus Corporation, Emeryville, CA 94608.
Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10866-70. doi: 10.1073/pnas.90.22.10866.
The hflA (high frequency of lysogenization) locus of Escherichia coli governs the lysis-lysogeny decision of bacteriophage lambda by controlling stability of the phage cII protein. hflA contains three genes, hflX, hflK, and hflC, encoding polypeptides of 50, 46, and 37 kDa, respectively. We have determined the nucleotide sequence of 3843 base pairs containing hflA and have found three large open reading frames corresponding to hflX, hflK, and hflC. HflX contains the three sequence motifs typical of GTP-binding proteins and appears to be a member of a distinct family of putative GTPases. HflC and HflK appear to be integral membrane proteins which show some similarity to each other and to a human membrane protein. The C-terminal region of HflC contains a domain resembling the catalytic domain of ClpP, a bacterial ATP-dependent protease. We hypothesize that HflK and HflC constitute a distinct membrane-bound protease whose activity may be modulated by HflX GTPase.
大肠杆菌的hflA（高频溶原化）位点通过控制噬菌体cII蛋白的稳定性来决定噬菌体λ的裂解-溶原化。hflA包含三个基因，hflX、hflK和hflC，分别编码50 kDa、46 kDa和37 kDa的多肽。我们测定了包含hflA的3843个碱基对的核苷酸序列，并发现了三个与hflX、hflK和hflC相对应的大的开放阅读框。HflX含有GTP结合蛋白典型的三个序列基序，似乎是一个独特的假定GTP酶家族的成员。HflC和HflK似乎是整合膜蛋白，它们彼此之间以及与一种人类膜蛋白有一些相似性。HflC的C末端区域包含一个类似于ClpP（一种细菌ATP依赖性蛋白酶）催化结构域的结构域。我们推测HflK和HflC构成一种独特的膜结合蛋白酶，其活性可能受HflX GTP酶调节。
