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. 2012 Jan 4;75(3):1031–1042. doi: 10.1016/j.jprot.2011.10.015

Table 2.

Summary of altered-protein expression of stationary phase parental B. pseudomallei strain 153 type I and isogenic colony variant types II and III.

Functional category Altered protein Spot number Gene designation Locus ID Mass PI Score Ratio type II/I or III/I
Protein location/specific function
II III
Upregulated proteins
Amino acid transport and metabolism Arginine deiminase 66 arcA BPSL1743 46,422 5.57 359 1.58 2.42 Cytoplasmic
Arginine deiminase 67 arcA BPSL1743 46,422 5.57 241 10.38 21.0 Catalyzes the degradation of arginine to citruline and ammonia
Carbamate kinase 20 arcC BPSL1745 33,507 5.54 129 1.99 3.01 Cytoplasmic
Carbamate kinase 45 arcC BPSL1745 33,507 5.54 130 6.67 10.13 Reversible synthesis of carbamate and ATP from carbamoyl phosphate and ADP
Hypothetical 32 BPSL1591 40,435 5.78 208 3.55 2.82 Cytoplasmic
Similar to Agrobacterium tumefaciens dehydrogenase
Energy production and conversion Ferredoxin-NADP(H) reductase 75 fpr BPSL0241 28,983 5.78 155 2.82 2.49 Cytoplasmic
FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin
Carbohydrate metabolism UDP-glucose dehydrogenase 73 udg BPSL2511 50,802 5.34 93 1.53 3.47 May have multiple localization sites
Cell wall/membrane biogenesis
Chaperone Chaperonin GroEL 29 groEL BPSL2697 57,137 5.13 159 0.51 3.00 Cytoplasmic
60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions
Cell motility Flagellin 6 fliC BPSL3319 39,233 5.05 106 10.72 15.63 Extracellular
Structural flagella protein



Down-regulated proteins
Lipid transport and metabolism Succinyl-CoA:3-ketoacid-coenzyme A transferase subunit A 53 scoA BPSL1955 25,373 5.6 155 0.103 0.105 Cytoplasmic
Coenzyme A (CoA) transferases catalyze the reversible transfer of CoA from one carboxylic acid to another
Succinyl-CoA:3-ketoacid-coenzyme A transferase subunit B 54 scoB BPSL1954 22,330 4.7 131 0.133 0.322 Cytoplasmic
Coenzyme A (CoA) transferases catalyze the reversible transfer of CoA from one carboxylic acid to another
Energy production and conversion Inorganic pyrophosphatase 22 ppa BPSL1021 19,206 5.37 88 0 0 Cytoplasmic
Catalyzes the hydrolysis of pyrophosphate to phosphate
Betaine aldehyde dehydrogenase 61 aldA BPSL1550 50,738 5.67 250 0.490 0.412 Cytoplasmic
Catalyses the conversion of betaine aldehyde to glycine betaine
Amino acid transport and metabolism/ 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase 74 BPSL2169 29,660 5.68 181 0.136 0.386 Cytoplasmic
Catalyzes the formation of N-succinyl-2-amino-6-ketopimelate from succinyl-CoA and tetrahydrodipicolinate in the lysine biosynthetic pathway
Inorganic ion transport and metabolism Sulfurtransferase 49 sseA BPSS1766 31,119 5.98 127 0.345 0.170 Cytoplasmic Cyanide detoxification
Catalyzes thiosulfate and cyanide to sulfite and thiocyanate
Secondary metabolites biosynthesis, transport and catabolism Non-ribosomally encoded peptide/polyketide synthase 35 phyH BPSS1183 35,611 5.77 102 0.725 0.142 Cytoplasmic membrane
Pseudomonas syringae syringomycin biosynthesis enzyme or B. thailandensis bactobolin
Posttranslational modification, protein turnover Oxido-reductase 62 BPSL2748 23,904 5.75 95 0.085 0.081 Cytoplasmic
Peroxidase
Antioxidant proteins
Multifunctional Acetoacetyl-CoA reductase 72 phbB BPSS1916 26,583 6.3 190 0.763 0.105 Cytoplasmic
Synthesizes polyhydroxybutyrate (PHB) from acetyl coenzyme A (acetyl-CoA) in Ralstonia eutropha.
Unknown Hypothetical protein 71 BPSL1549 23,384 5.14 66 0.417 0.091 Unknown

Protein spots were separated using a pH range 4–7 and examined using 2D Image master software. Only those proteins with a reproducible change in spot intensity volume between types I versus II or I versus III colony variants of ≥ 1.5-fold in two independent experiments are reported. Functional groups were identified based on COG functional category (http://www.ncbi.nlm.nih.gov). PSORTb was used to predict protein localization (http://www.psort.org/psortb).