Table 3.

Protein identification using MS/MS peptide fragmentation and Swiss-Prot database search.

Spota	Swiss-prot accession number	Identified proteinb	Fold changec	Length	Mass (kDa)d	pIe	Mascot scoref	Functional classification
1	C7JC25	Heat shock protein DnaK	2.05	634	67.5	4.9	1965	coping with heat or external environmental pressure
2	C7JBN6	Trigger factor	4.52	444	49.3	4.78	580	peptidyl-prolyl cis-trans isomerase
3	C7JAP1	Thioredoxin	2.57	319	34.4	4.88	317	protein disulfide oxidoreductase activity
4	C7JDY6	Glutamine synthetase	3.64	481	53.1	5.34	147	ATP binding
5	C7JAQ5	Aldehyde dehydrogenase	6.32	463	50.6	5.27	1061	oxidoreductase activity
6	Q5HXK5	NAD(P)H-dependent 2-cyclohexen-1-one reductase	−2.79	354	39.3	5.96	1056	oxidoreductase activity
7	C7JBD3	Alkyl hydroperoxide reductase AhpD	5.73	175	18.4	5.87	576	response to oxidative stress
8	C7JAW8	Alcohol dehydrogenase large subunit	5.05	742	81.6	6.77	305	oxidoreductase activity
9	C7JG48	Aconitate hydratase	−2.34	897	97.7	6.21	1098	aconitate hydratase activity
10	C7JFQ0	50S ribosomal protein L1	4.17	230	23.9	6.87	702	direct binding to 23S rRNA
11	NI	Uncharacterized protein	NI	NI	NI	NI	NI	NI
12	C7JG40	Transcription termination/antitermination protein NusA	−2.46	514	57.6	4.61	348	translation elongation factor activity
13	C7JIQ0	NADH:flavin oxidoreductase	−3.12	357	39.5	5.96	557	oxidoreductase activity
14	F1YU43	Chaperonin	5.32	546	58	5.49	576	ATP binding
15	M9WQJ0	Elongation factor Tu	2.69	836	74.9	5.22	158	translation elongation factor activity
16	C7JCS6	Thiosulfate sulfurtransferase	3.67	292	32.5	5.54	79	transferase activity
17	A0A0K0TA70	S-adenosylmethionine synthase	2.73	960	68.5	5.3	154	ATP+L-methionine+H2O = phosphate+diphosphate+S-adenosyl-L-methionine
18	C7JDV2	Esterase/lipase	3.12	388	40.8	4.98	254	lipolysis
19	NI	Uncharacterized protein	NI	NI	NI	NI	NI	NI

^aNumber as shown in Figure 6.

^bProtein spots whose expression level changed more than 50% as calculated by PDQuest 8.0 software. Nineteen spots were identified, of which 17 were researched and named as described in Table 3.

^cFold changes in the expression of proteins between original and engineered strains. A minus sign indicates down-regulation, otherwise it denotes up-regulation.

^dTheoretical protein molecular mass as derived from amino acid sequences.

^eIsoelectric point of the protein as calculated from amino acid sequences.

^fPercentage of predicted protein sequence covered by matched peptides via MASCOT (http://www.matrixscience.com/).

NI represented the protein spot could not be identified.