title: High-resolution proteome maps of Bacillus licheniformis cells growing in minimal medium.
abstract: Bacillus licheniformis is an important host for the industrial production of enzymes mainly because of its ability to secrete large amounts of protein. We analyzed the proteome of B. licheniformis cells growing in a minimal medium. Beside the cytosolic proteome, the membrane and the extracellular proteome were studied. We could identify 1470 proteins; 1168 proteins were classified as cytosolic proteins, 195 proteins with membrane-spanning domains were classified as membrane proteins, and 107 proteins, with either putative signals peptides or flagellin-like sequences, were classified as secreted proteins. The identified proteins were grouped into functional categories and used to reconstruct cellular functions and metabolic pathways of growing B. licheniformis cells. The largest group was proteins with functions in basic metabolic pathways such as carbon metabolism, amino acid and nucleotide synthesis and synthesis of fatty acids and cofactors. Many proteins detected were involved in DNA replication, transcription, and translation. Furthermore, a high number of proteins employed in the transport of a wide variety of compounds were found to be expressed in the cells. All MS data have been deposited in the ProteomeXchange with identifier PXD000791 (http://proteomecentral.proteomexchange.org/dataset/PXD000791).
authors: Institute for Microbiology, Ernst-Moritz-Arndt-University, Greifswald, Germany.
authors: Birgit
authors: B
authors: Voigt
authors: Institute for Microbiology, Ernst-Moritz-Arndt-University, Greifswald, Germany.
authors: Dirk
authors: D
authors: Albrecht
authors: Institute for Microbiology, Ernst-Moritz-Arndt-University, Greifswald, Germany.
authors: Susanne
authors: S
authors: Sievers
authors: Institute for Microbiology, Ernst-Moritz-Arndt-University, Greifswald, Germany.
authors: Dörte
authors: D
authors: Becher
authors: Department of Chemistry and Biotechnology, Aachen University of Applied Sciences, Jülich, Germany.
authors: Johannes
authors: J
authors: Bongaerts
authors: Henkel AG & Co. KGaA, Düsseldorf, Germany.
authors: Stefan
authors: S
authors: Evers
authors: Institute of Pharmacy, Ernst-Moritz-Arndt-University, Greifswald, Germany.
authors: Thomas
authors: T
authors: Schweder
authors: AB Enzymes GmbH, Darmstadt, Germany.
authors: Karl-Heinz
authors: KH
authors: Maurer
authors: Institute for Microbiology, Ernst-Moritz-Arndt-University, Greifswald, Germany.
authors: Michael
authors: M
authors: Hecker
mesh_terms: D001407:Bacillus / Q000187:drug effects / Q000378:metabolism*; D001426:Bacterial Proteins / Q000032:analysis* / Q000145:classification / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D002468:Cell Physiological Phenomena; D003470:Culture Media / Q000494:pharmacology; D003600:Cytosol / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D004734:Energy Metabolism; D008074:Lipoproteins / Q000032:analysis / Q000378:metabolism; D008565:Membrane Proteins / Q000032:analysis / Q000378:metabolism; D053858:Metabolic Networks and Pathways; D020543:Proteome / Q000032:analysis* / Q000145:classification / Q000378:metabolism; D040901:Proteomics / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D001426:Bacterial Proteins; D003470:Culture Media; D008074:Lipoproteins; D008565:Membrane Proteins; D020543:Proteome
keywords: B. licheniformis; Metabolic pathways; Proteome maps