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. 1998 Nov;180(21):5739–5748. doi: 10.1128/jb.180.21.5739-5748.1998

FIG. 2.

FIG. 2

(A) AgpA is similar to oligopeptide binding proteins of periplasmic transport systems. The deduced amino acid sequence of AgpA was compared to the sequences of other members of the oligopeptide binding protein family with the Pileup program of the Wisconsin Genetics Computer Group sequence analysis package, Clustal W and SeqVu. The peptides used in the lineup are R. meliloti AgpA (Rm AgpA), Agrobacterium tumefaciens agrocinopine transport protein AccA (At AccT) (17), B. subtilis oligopeptide transport protein Spo0K (Bs Spo0K) (41), E. coli dipeptide transport protein DppA (Ec DppA), E. coli nickel transport protein NikA (Ec NikA) (34), Streptococcus pneumoniae oligopeptide pheromone binding protein AmiA (Sp AmiA) (1), and S. typhimurium oligopeptide binding protein OppA (St OppA) (18). The small inverted triangle indicates the location of the PhoA fusion site in R. meliloti SG1001. (B) MelA from R. meliloti is similar to MelA, an α-galactosidase, of E. coli. The deduced amino acid sequence of R. meliloti MelA was compared to that of E. coli MelA with the Pileup program of the Wisconsin Genetics Computer Group sequence analysis package.