PMID:2318304
| Citation |
Hirvas, L, Coleman, J, Koski, P and Vaara, M (1990) Bacterial 'histone-like protein I' (HLP-I) is an outer membrane constituent? FEBS Lett. 262:123-6 |
|---|---|
| Abstract |
The nucleoid-associated 'histone-like protein I' (HLP-I) protein of E. coli was found to be homologous with the cationic 16-kDa outer membrane protein OmpH of Salmonella typhimurium. Deduced from the nucleotide sequence, the HLP-I protein has 91% identical residues with the OmpH protein. Both proteins have very similar cleavable signal sequences. The nucleotide sequence similarity between the corresponding genes hlpA and ompH is 87%. The ompH gene is located in a gene cluster resembling the hlpA-ORF17 region of E. coli which is close to the Ipx genes involved in the biosynthesis of lipopolysaccharides. The localization of the OmpH/HLP-I protein in the cell is discussed. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Outer Membrane Proteins/analysis; Bacterial Outer Membrane Proteins/genetics; Bacterial Proteins/analysis; Bacterial Proteins/genetics; DNA-Binding Proteins/analysis; DNA-Binding Proteins/genetics; Lipoproteins/metabolism; Molecular Sequence Data |
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