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. 2013 Nov 8;8(11):e80252. doi: 10.1371/journal.pone.0080252

Table 2. Comparison of the conservation of amino acid residues from P. aeruginosa EF-G1A and EF-G1B with corresponding factors from other organisms.

Organism EF-G1B EF-G1A Accession Number
(% similar/identical) (% similar/identical)
E. coli 1 EF-G 80/67 78/67 0905186A
B. burgdorferi EF-G1 59/44 58/43 YP_005806724
B. burgdorferi EF-G2 55/36 55/36 YP_005806873
H. sapiens EF-G1mt 54/39 54/38 NP_079272
H. sapiens EF-G2mt 47/33 47/34 AAH30612
M. smegmatis EF-G1 71/58 70/57 YP_006566130
M. smegmatis EF-G2 45/29 44/28 YP_890748
T. thermophilus EF-G1 75/60 73/58 YP_005300
T. thermophilus EF-G2 51/33 51/32 YP_005103
S. typhimurium EF-G 80/69 79/69 AAL22309
S. aureus EF-G 72/59 71/57 A7WYX4
B. bronchiseptica (707) EF-G2 79/66 76/64 NP_890794
B. bronchiseptica (700) EF-G 81/67 80/66 CAE30528
B. rhizoxinica (703) EF-G 79/67 77/64 CBW74068
B. rhizoxinica (700) EF-G 79/66 78/66 CBW74549

1 The organisms analyzed are Escherichia coli, Borrelia burgdorferi, Homo sapiens, Mycobacterium smegmatis, Thermus thermophilus, Salmonella typhimurium, Staphylococcus aureus, Bordetella bronchiseptica, Burkholderia rhizoxinica.

2 The EF-G molecules from B. bronchiseptica and B. rhizoxinica could not be differentiated by sequence alignment and are differentiated here by the number of amino acids composing the proteins as shown in parenthesis.