4 GO Annotations
| GO Term | Gene Name |
|---|---|
| GO:0000155 | IPR008358 |
| GO:0004673 | IPR008358 |
| GO:0000160 | IPR008358 |
| GO:0016020 | IPR008358 |
4 Ontology Annotations
| GO Term | Gene Name |
|---|---|
| GO:0000155 | IPR008358 |
| GO:0004673 | IPR008358 |
| GO:0000160 | IPR008358 |
| GO:0016020 | IPR008358 |
| Type: | Family | Name: | Signal transduction histidine kinase/phosphatase, lantibiotic regulatory protein MprB |
| Description: | Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions []. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk []. These pathways have been adapted to response to a wide variety of stimuli, including nutrients, cellular redox state, changes in osmolarity, quorum signals, antibiotics, and more []. Two-component systems are comprised of a sensor histidine kinase (HK) and its cognate response regulator (RR) []. The HK catalyses its own auto-phosphorylation followed by the transfer of the phosphoryl group to the receiver domain on RR; phosphorylation of the RR usually activates an attached output domain, which can then effect changes in cellular physiology, often by regulating gene expression. Some HK are bifunctional, catalysing both the phosphorylation and dephosphorylation of their cognate RR. The input stimuli can regulate either the kinase or phosphatase activity of the bifunctional HK.A variant of the two-component system is the phospho-relay system. Here a hybrid HK auto-phosphorylates and then transfers the phosphoryl group to an internal receiver domain, rather than to a separate RR protein. The phosphoryl group is then shuttled to histidine phosphotransferase (HPT) and subsequently to a terminal RR, which can evoke the desired response [, ].Signal transducing histidine kinases are the key elements in two-component signal transduction systems, which control complex processes such as the initiation of development in microorganisms [, ]. Examples of histidine kinases are EnvZ, which plays a central role in osmoregulation [], and CheA, which plays a central role in the chemotaxis system []. Histidine kinases usually have an N-terminal ligand-binding domain and a C-terminal kinase domain, but other domains may also be present. The kinase domain is responsible for the autophosphorylation of the histidine with ATP, the phosphotransfer from the kinase to an aspartate of the response regulator, and (with bifunctional enzymes) the phosphotransfer from aspartyl phosphate back to ADP or to water []. The kinase core has a unique fold, distinct from that of the Ser/Thr/Tyr kinase superfamily. HKs can be roughly divided into two classes: orthodox and hybrid kinases [, ]. Most orthodox HKs, typified by the Escherichia coliEnvZ protein, function as periplasmic membrane receptors and have a signal peptide and transmembrane segment(s) that separate the protein into a periplasmic N-terminal sensing domain and a highly conserved cytoplasmic C-terminal kinase core. Members of this family, however, have an integral membrane sensor domain. Not all orthodox kinases are membrane bound, e.g., the nitrogen regulatory kinase NtrB (GlnL) is a soluble cytoplasmic HK []. Hybrid kinases contain multiple phosphodonor and phosphoacceptor sites and use multi-step phospho-relay schemes instead of promoting a single phosphoryl transfer. In addition to the sensor domain and kinase core, they contain a CheY-like receiver domain and a His-containing phosphotransfer (HPt) domain.Pathogenic bacteria produce a number of virulence factors to facilitate host infection, and to combat competing species. Antibiotics are secreted by some pathogenic prokaryotes to lyse cells, some of which have been adapted by humans for use against virulent microbes. Amongst these are the lantibiotics, produced exclusively by Gram-positive bacteria. Lantibiotics are small, heavily post-translationally modified peptides that inhibit rival cell growth and are strongly cationic. Lantibiotic genes reside on the bacterial chromosome, where they cluster with genes that adapt and secrete them to the extracellular space. Many of these so-called 'pathogenicity islands' have been characterised, including the epidermin (epi) cluster in Staphylococcus epidermis, and the nisin (nis) cluster in Lactococcus lactis[]. The gene encoding the lantibiotic is flanked by 3 regulatory genes: 2 that are usually involved in a 2-component regulatory system, and another that cleaves the signal peptide from the precursor to produce the mature lantibiotic.The archetypal example of lantibiotic synthesis is witnessed in the Lactococcus lactisnis operon. In this cluster, the 2-component regulatory system is controlled by the nisK/nisR genes. NisK is believed to function as a membrane-associated protein kinase that phosphorylates NisR in response to external stimuli []. It shows some similarity to other bacterial kinases, and contains a single histidine kinase domain. | Short Name: | Sig_transdc_His_kin/Pase_MprB |
| GO Term | Gene Name |
|---|---|
| GO:0000155 | IPR008358 |
| GO:0004673 | IPR008358 |
| GO:0000160 | IPR008358 |
| GO:0016020 | IPR008358 |
| GO Term | Gene Name |
|---|---|
| GO:0000155 | IPR008358 |
| GO:0004673 | IPR008358 |
| GO:0000160 | IPR008358 |
| GO:0016020 | IPR008358 |
