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. 2006 May;188(9):3264–3272. doi: 10.1128/JB.188.9.3264-3272.2006

TABLE 1.

Identification of proteins in NDH-1 from the source 15Q chromatographic stepa

Swiss-Prot accession no. Protein Gene Predicted mass (Da) No. of peptide matches Protein score
Q8FH47 Hypothetical protein YdiJ ydiJ 113,164 2 39
Q8ZLT3 Polynucleotide phosporylase pnp 76,991 13 589
P0A1H3 Elongation factor G fusA 77,419 10 425
Q8FAL6 Fumarate reductase flavoprotein subunitb frdA 65,948 5 130
Q8FAL6 Fumarate reductase flavoprotein subunitb frdA 65,948 5 106
P0A1Y7 NADH dehydrogenase I, subunit NuoCD nuoCD 68,817 4 88
O66026 60-kDa chaperonin groL 57,003 18 602
Q8XG95 ATP synthase alpha subunit atpA 55,079 15 644
P0ABB4 ATP synthase beta subunit atpD 50,163 19 671
P0A6N1 Elongation factor Tu tufA 43,286 6 201
Q7WRJ3 1,3-Propanediol oxidoreductase dhaT 41,518 2 73
Q8ZH40 d-Methionine binding protein metQ 29,359 2 83
Q83BR3 NADH dehydrogenase I, subunit NuoI nuoI 18,985 1 29
a

Polypeptides subjected to tryptic digestion and mass spectroscopic analysis are indicated in the SDS-PAGE gel shown in Fig. 1. Results were compared with the UniRef100 database (http://www.ebi.ac.uk/uniref/) using the Mascot search engine (Matrix Science Ltd., United Kingdom). In cases where the identified K. pneumoniae protein is not deposited in the Swiss-Prot database, the accession number of the corresponding enterobacterial protein with the highest sequence similarity is given as a reference.

b

Both polypeptides separated by SDS-PAGE (Fig. 1) were assigned to frdA.