Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Phage shock protein A homolog; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Amino acid racemase; Amino-acid racemase able to utilize a broad range of substrates. Preferentially catalyzes the epimerization of LL- diaminopimelate, as well as the racemization of D-lysine, L-arginine, L-ornithine, L-lysine and D-arginine. Has lower activity against D- ornithine, L-histidine, L-alanine, L-tyrosine, L-phenylalanine, L- serine, L-glutamine, L-methionine, L-asparagine and L-homoserine. Has weak activity against L-norleucine, L-aminobutyric acid and L- norvaline. Has no activity toward nine L-amino acids (Thr, Glu, Asp, Val, Leu, Ile, Trp, Cit and Aad). D-amino acids m [...]

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

anti-sigma(W) factor; The anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-W (SigW). Holds SigW, its cognate ECF sigma factor, in an inactive form until released by regulated intramembrane proteolysis (RIP). SigW and RsiW mediate cell response to cell wall stress. RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, PrsW) , then within the membrane itself (site-2 protease, S2P [...]

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

RNA polymerase ECF(extracytoplasmic function)-type sigma factor W; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Sigma-W controls genes involved in response to cell envelope stress such as antimicrobial peptides , alkaline pH , transport processes and detoxification.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Signal peptide peptidase; Digestion of cleaved signal peptides (By similarity). Required for efficient processing of precursors under conditions of hyper-secretion. Has a preference for leucine-rich substrate peptides. Belongs to the peptidase S49 family.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Putative exported hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Putative phage replication protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type h: extrachromosomal origin.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Putative peroxydase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Putative membrane bound hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; Product type cp: cell process.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Putative ABC transporter (ATP-binding protein); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter; Belongs to the ABC transporter superfamily.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Putative ABC transporter (permease); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Putative membrane integrity integral membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Putative flotillin-like protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.

Penicillin-binding protein 4*; Probably involved in peptidoglycan modification during cortex synthesis.

Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.

Protease required for RsiW anti-sigma(W) degradation; Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and r [...]

Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane.

Protease required for RsiW anti-sigma(W) degradation; Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and r [...]

anti-sigma(W) factor; The anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-W (SigW). Holds SigW, its cognate ECF sigma factor, in an inactive form until released by regulated intramembrane proteolysis (RIP). SigW and RsiW mediate cell response to cell wall stress. RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, PrsW) , then within the membrane itself (site-2 protease, S2P [...]

Protease required for RsiW anti-sigma(W) degradation; Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and r [...]

RNA polymerase ECF(extracytoplasmic function)-type sigma factor W; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Sigma-W controls genes involved in response to cell envelope stress such as antimicrobial peptides , alkaline pH , transport processes and detoxification.