High-molecular-weight protein 2 of Yersinia enterocolitica is homologous to AngR of Vibrio anguillarum and belongs to a family of proteins involved in nonribosomal peptide synthesis

• Published in: Journal of Bacteriology Vol. 175; no. 17; pp. 5488 - 5504
• Main Authors: GUILVOUT, I, MERCEREAU-PUIJALON, O, BONNEFOY, S, PUGSLEY, A. P, CARNIEL, E
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for Microbiology 01.09.1993
• Subjects: Amino Acid Sequence; Anti-Bacterial Agents - biosynthesis; Bacterial Outer Membrane Proteins - genetics; Bacterial Outer Membrane Proteins - metabolism; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacteriology; Base Sequence; Binding Sites; Biological and medical sciences; Cloning, Molecular; DNA, Bacterial; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Fundamental and applied biological sciences. Psychology; Genetics; Iron-Binding Proteins; Microbiology; Molecular Sequence Data; Molecular Weight; Peptide Biosynthesis; Periplasmic Binding Proteins; Phylogeny; Promoter Regions, Genetic; Proteins; Ribosomes - metabolism; Sequence Homology, Amino Acid; Transcription Factors; Vibrio - classification; Vibrio - genetics; Vibrio - metabolism; Yersinia enterocolitica; Yersinia enterocolitica - genetics; Yersinia enterocolitica - metabolism; Upstream sequence; Nucleotide sequence; Transcription promoter; Sequence alignment; Homology; Phylogeny; Structure function relationship; Yersinia enterocolitica; DNA; Bacteria; Regulatory sequence; Molecular domain; Comparative study; Aminoacid sequence; Enterobacteriaceae
• ISSN: 0021-9193; 1067-8832; 1098-5530
• DOI: 10.1128/jb.175.17.5488-5504.1993

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