2 GENES PRESENT ON A TRANSPOSON-LIKE STRUCTURE IN LACTOCOCCUS-LACTIS ARE INVOLVED IN A CLP-FAMILY PROTEOLYTIC ACTIVITY
2 GENES PRESENT ON A TRANSPOSON-LIKE STRUCTURE IN LACTOCOCCUS-LACTIS ARE INVOLVED IN A CLP-FAMILY PROTEOLYTIC ACTIVITY
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DOI:
10.1111/j.1365-2958.1993.tb01187.x
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发表时间:
1993-03-01
影响因子:
3.6
通讯作者:
NOVEL, M
中科院分区:
文献类型:
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作者:
HUANG, DC;HUANG, XF;NOVEL, M
The lactose-protease plasmid pUCL22 of Lactococcus lactis subsp. lactis strain CNRZ270 contained two inverted copies of IS1076 flanking a region of 3.7 kb. This internal region was sequenced and found to contain two large open reading frames, ORF1 and ORFP in opposite orientations. ORF1 consists of 2289 bp; the deduced 763-amino-acid sequence is similar to the ATPases of the ClpA family. It contains two well-conserved consensus ATP-binding sites. It was named ClpL. ORFP consists of 930 bp encoding a protein of 310 amino acids. No similarity with any known protein was found in GenBank data for ORFP. Increased ATP-dependent proteolytic activity was detected in extracts from Escherichia coli cells expressing the clpL and ORFP genes.