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Fig. 5 | BMC Microbiology

Fig. 5

From: Revealing biophysical properties of KfrA-type proteins as a novel class of cytoskeletal, coiled-coil plasmid-encoded proteins

Fig. 5

Amino acid composition of KfrAR751, KfrARA3 and the domain structure of KfrA homologs. a Grey lines indicate average values calculated in a reference set of 800 parallel dimeric coiled-coils (KfrAR751 residues 77–327 and KfrARA3 residues 76–326), whereas the red lines depict values obtained from a given sequence. The seven heptad positions group residues according to their position relative to the coiled-coil bundle hydrophobic core (positions a and d are facing the core; b, c, and f the solvent, while e and g are in-between). b Each row denotes a single full-length KfrA sequence. Blue regions indicate the presence of HTH domain (PFAM family KfrA_N), whereas orange and red regions correspond to coiled-coil domains predicted with medium (p ≥ 0.5) and high (p ≥ 0.75) confidence. Grey background indicates the actual length of an individual KfrA homolog

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