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mprF | Phosphatidylglycerol lysyltransferase involved in lysinylation of phospholipids; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects B.subtilis against its own CAMPs and against those produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with po [...] (856 aa) | ||||
cspB | Major cold-shock protein, RNA helicase co-factor, RNA co-chaperone; Binds to the pentamer sequences ATTGG and CCAAT with highest affinity in single-stranded DNA, and also to other sequences. Has greater affinity for ATTGG than CCAAT. Can act as transcriptional activator of cold shock genes by recognizing putative ATTGG-box elements present in promoter regions of genes induced under cold shock conditions. (67 aa) | ||||
htrA | Membrane bound serine protease Do, quality control protease (heat-shock protein); Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. (449 aa) | ||||
clpE | ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. (699 aa) | ||||
hfq | Hfq RNA chaperone; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Belongs to the Hfq family. (73 aa) | ||||
sodF | Superoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. (281 aa) | ||||
cspD | Cold-shock protein, molecular chaperone, RNA-helicase co-factor; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor. (66 aa) | ||||
sodA | Superoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family. (202 aa) | ||||
dnaJ | Co-factor of molecular chaperone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...] (375 aa) | ||||
dnaK | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. (611 aa) | ||||
hrcA | Transcriptional regulator of heat-shock genes; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (343 aa) | ||||
rarA | DNA-dependent ATPase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 subfamily. (421 aa) | ||||
rsh | GTP pyrophosphokinase (RelA/SpoT); In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp, it is probably the hydrolysis activity that is required for optimal growth (Probable); Belongs to the RelA/SpoT family. (734 aa) | ||||
clpP | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] (197 aa) | ||||
dltA | D-alanine:D-alanyl-carrier protein ligase; Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. Belongs to the ATP [...] (503 aa) | ||||
dltB | Putative D-alanine esterase for lipoteichoic acid and wall teichoic acid; Involved in the D-alanylation of lipoteichoic acid (LTA). Could be involved in the transport of activated D-alanine through the membrane. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. (395 aa) | ||||
treA | Trehalose-6-phosphate hydrolase; Hydrolyzes trehalose-6-phosphate to glucose and glucose 6- phosphate. Can also very effectively hydrolyzes p-nitrophenyl-alpha-D- glucopyranoside, but not lactose, maltose, sucrose or sucrose-6- phosphate. Trehalose is also hydrolyzed, but to a much smaller extent than trehalose-6-phosphate; Belongs to the glycosyl hydrolase 13 family. (561 aa) | ||||
groEL | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (544 aa) | ||||
groES | Chaperonin small subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. (94 aa) | ||||
sigB | RNA polymerase sigma-37 factor (sigma(B)); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Sigma B is not essential for sporulation; rather it is required for maximal expression of ctc and csbA which are transcribed in the early stationary phase under conditions inimical to sporulation. May play a role in the ability of the bacterium to adapt to various stresses but is not essential for its survival under these conditions. Positively regulates expression of its own operon; Belongs to the sigma-70 fac [...] (262 aa) | ||||
dtpT | Di-tripeptide-proton ABC symporter; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type t: transporter. (492 aa) | ||||
rplJ | Ribosomal protein L10 (BL5); Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors (such as IF-2, EF-Tu, EF-G and RF3). (166 aa) | ||||
clpC | Class III stress response-related ATPase, AAA+ superfamily; Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK; Belongs to the ClpA/ClpB family. ClpC subfamily. (810 aa) | ||||
mcsB | Protein tyrosine kinase; Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix- turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under str [...] (363 aa) | ||||
mcsA | Activator of protein kinase McsB; Activates the phosphorylation activity of the protein- arginine kinase McsB. Is required for the delocalization of competence proteins from the cell poles. (185 aa) | ||||
ctsR | Transcriptional regulator; Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB. Acts as a repressor of these class III stress genes by binding to a directly repeated heptanucleotide operator sequence (A/GGTCAAA NAN A/GGTCAAA). After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR negatively autoregulates its own synthesis. (154 aa) | ||||
ctc | Ribosomal protein Ctc, binding 5S RNA; Not required for exponential growth; probably functions in vegetatively growing cells, maybe required for accurate translation under stress conditions. (204 aa) |