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Two genes present on a transposon‐like structure in Lactococcus lactis are involved in a Clp‐family proteolytic activity
Author(s) -
Huang Dao Chao,
Huang Xian Fang,
Novel Georges,
Novel Madeleine
Publication year - 1993
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1993.tb01187.x
Subject(s) - biology , lactococcus lactis , genbank , transposable element , plasmid , open reading frame , genetics , gene , escherichia coli , nucleic acid sequence , protease , peptide sequence , amino acid , conserved sequence , biochemistry , mutant , bacteria , enzyme , lactic acid
Summary The lactose‐protease plasmid pUCL22 of Lactococcus lactis subsp. lactis strain CNRZ270 contained two inverted copies of IS 1076 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.