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. 2001 May;183(10):3160–3168. doi: 10.1128/JB.183.10.3160-3168.2001

FIG. 1.

FIG. 1

(A) Alignment of B. subtilis ComEA and amino acid sequence derived from the GC FA1090 ORF. Identical residues and conservative substitutions are indicated. The predicted signal peptide cleavage site between residues 19 and 20 of the GC ORF is marked by an arrow. The putative flexible hinge in B. subtilis ComEA is underlined. (B) Multiple alignment of amino acid sequences sharing homology with the GC ComE region containing HhH motifs. Residues conserved in at least 5 of the 13 sequences are shown in bold. The sequences (and their accession numbers in GenBank, for protein or nucleotide) are from B. subtilis ComEA (B. sub, AAC36905), S. pneumoniae CelA (S.pne, AF052208), D. nodosus ORF E (partial) (D.nod, AAB41275), E. coli hypothetical protein (E.col, AAB40198), Pseudomonas aeruginosa (P.aer, AF147795), Haemophilus influenzae hypothetical protein (H.inf, HI1008), Haemophilus ducreyi ORF (H.duc, AF087414), Campylobacter jejuni putative protein (C.jej, CAB72504), Deinococcus radiodurans (D.rad, AAF11406), Mycobacterium tuberculosis hypothetical protein (M.tub, AB03744), Synechocystis sp. protein (Synec, BAA10416), and Thermotoga maritima protein (T.mar, AAD36129).