Protein encoded by the organellar chromatophore genome or a protein targeted to the organellar chromatophore. The organellar chromatophore is the photosynthetic inclusion found in Paulinella species, which are photosynthetic thecate amoeba. It probably derives from a different endosymbiotic event than that which led to all other plastids. Houses the machinery necessary for photosynthesis and CO(2) fixation; it also has the genetic capacity to synthesize some amino acids, some fatty acids and a few cofactors. It contains thylakoid membranes, and a residual peptidoglycan wall between the 2 envelope membranes. There are 1 or 2 chromatophores per cell
Protein which, if defective, causes Diamond-Blackfan anemia, a rare congenital non-regenerative hypoplastic anemia that usually presents early in infancy. The disease is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of developing leukemia. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies
Small transmembrane protein that homo-oligomerizes to form a viral ion channel usually expressed in the viral envelope and host cell membranes. These channels affect membrane permeability to ions and play an important role in facilitating virus entry, assembly and release, as well as modulating the ion homeostasis of host cells Viral ion channels are not necessarily required for the production of infectious virions, although their expression usually significantly increases growth. During influenza A virus entry for example, the M2 proton channel allows protons from the acidic endosome to enter the enveloped virion, initiating pH-dependent uncoating of the genome. In certain influenza A subtypes, M2 also equilibrates the intraluminal pH of the trans-Golgi network with the cytoplasm, preventing premature conformational changes in the viral fusion protein during budding
Component of the inflammasome complex involved in innate immunity and inflammation. Inflammasomes are supramolecular micron-sized complexes that assemble in the cytosol adjacent to the nucleus in response to pathogens and other damage-associated signals. The core of inflammasomes consists of at least 2 components: a signal sensor and an effector inflammatory caspase (mostly CASP1). However, most inflammasomes contain a third element, an adaptor (often ASC/PYCARD) In response to a danger signal, the sensor homooligomerizes and interacts with the adaptor that polymerizes and forms a platform to recruit caspase precursors. This results in increased local concentration of the enzyme, leading to trans-autocleavage and activation. Active caspases process proinflammatory IL1B and IL18 cytokine precursors, which are then secreted in the extracellular milieu and induce inflammatory responses. In adaptor-independent inflammasomes, the sensor directly recruits the caspase. Additional proteins may interaction with the core complex. Inflammasomes also induce pyroptosis, an inflammatory form of programmed cell death
Viral protein involved in the integration of a virus genome into the host DNA. Integrated viral DNA is referred to as a provirus in the case of retroviruses or prophage in the case of prokaryotic viruses The integrated viral genome does not necessarily make new DNA copies of itself while integrated into a host genome. Instead, it can remain latent and be passively replicated along with the host genome and passed on to the original cell's offspring; all descendants of the infected cell will also bear it in their genomes. The host's environmental conditions changes can however reactivate the virus leading to viral transcription and production of new infectious viruses (productive infection). Integration is a crucial step in replication of retroviruses, as well as some phages. Integration is not part of the viral replication cycle of phycodnaviruses, adeno- associated virus type 2, and human herpesvirus 6A genome, but can occasionally occur
Viral protein expressed primarily to establish, maintain or terminate latency, the part of the viral life cycle during which a virus lies dormant (latent) within a cell. This part of the virus life cycle is called the lysogenic part in prokaryotic viruses. During latency, the viral genome can either exist as a provirus integrated in the host genome (proviral latency) or as a linear or circular plasmid in the host cell (episomal latency). The virus does not replicate, but is passively duplicated when the host divides. In eukaryotes for example, HHV-1 and HHV-3 establish episomal latency in neurons. HIV is integrated as a provirus in the genome of resting CD4-positive T cells, allowing the virus to persist for years. Following changes in the environmental conditions of the host, reactivation of the virus can occur leading to viral transcription and production of new infectious viruses
Protein involved in the synthesis of peptidoglycan which consists of a glycosaminoglycan formed by alternating residues of D-glucosamine and either muramic acid {2-amino-3-O-[(R)-1-carboxyethyl]-2-deoxy-D- glucose} or L-talosaminuronic acid (2-amino-2-deoxy-L-taluronic acid), which are usually N-acetylated or N-glycoloylated. The carboxyl group of the muramic acid is commonly substituted by a peptide containing residues of both L- and D-amino acids, whereas that of L- talosaminuronic acid is substituted by a peptide consisting of L-amino acids only. These peptide units may be cross-linked by a peptide bond, thereby giving rise to a giant macromolecule that forms the rigid cell wall (sacculus or murein sacculus). This macromolecule is known to occur as a monomolecular layer between the inner and outer membrane in Gram-negative bacteria and as a multimolecular layer, often associated covalently or non-covalently with various additional compounds (teichoic acids, neutral polysaccharides. etc.) in Gram-positive bacteria. In the archaebacteria, several organisms contain a peptidoglycan, also called pseudomurein, which differs in certain respects from those of the eubacteria
The archaellum (archaeal flagellum) is the motility apparatus of archaea which propels the cell through liquid medium. The archaellum is the functional equivalent of the bacterial flagellum but its architecture, composition and mode of assembly is completely unrelated. The archaellum is thinner (10-15 nm) compared to the bacterial flagellum (18-24 nm). Its filament is assembled from archaellin subunits, which are N-glycosylated proteins. The archaellum is considered to be a type IV pilus-like structure and accordingly is assembled from the base into a 3-start helix. Archaellins have a type III signal sequence which is removed by the pre-archaellin peptidase Core components of the assembly machinery are ArlI and ArlJ (previously FlaI, FlaJ) which are distantly related to PilB and PilC from type II secretion systems and type IV pills assembly systems ArlI is a dual function ATPase which first assembles the filament and then rotates it by using the energy from ATP hydrolysis. Ion gradients are not used for archaellum rotation
Protein which is involved in the formation, organization or maintenance of the archaellum (archaeal flagellum) the motility apparatus of archaea which propels the cell through liquid medium. The archaellum is the functional equivalent of the bacterial flagellum but its architecture, composition and mode of assembly is completely unrelated. The archaellum is thinner (10-15 nm) compared to the bacterial flagellum (18-24 nm). Its filament is assembled from archaellin subunits (archaeal flagellin), N-glycosylated proteins. The archaellum is considered to be a type IV pilus-like structure and accordingly is assembled from the base into a 3-start helix Archaellins have a type III signal sequence which is removed by the pre-archaellin peptidase. Core components of the assembly machinery are ArlI and ArlJ (previously FlaI, FlaJ) which are distantly related to PilB and PilC from type II secretion systems and type IV pills assembly systems. ArlI is a dual function ATPase which first assembles the filament and then rotates it by using the energy from ATP hydrolysis
Protein which is part of an anion channel found in the plasma membrane and in intracellular membranes. These channels are permeable for various anions, such as iodide, bromide, but also for nitrates, phosphates and even negatively charged amino acids. They are called chloride channels, because chloride is the most abundant anion and the predominant permeating species in all organisms. They have been classified according to their gating mechanisms, which may depend on changes in the transmembrane electric field (voltage-dependent/gated chloride channels, e.g. ClC family), on a protein kinase/nucleotide mediated mechanism (CFTR), an increase in intracellular calcium (calcium activated chloride channels, e.g. CaCC), cell swelling (volume-regulated anion channels, e.g. VRAC) or binding of a ligand, e.g. glycine or - aminobutyric acid (GABA) activated channels. In contrast with cation channels, they are not involved in the initiation or spread of excitation, but in the regulation of excitability in nerve and muscle. They also participate in many housekeeping processes, such as volume regulation, pH regulation in organelles, electrogenesis and control of synaptic activity. The chloride channels are crucial for transepithelial transport and the control of water flow, and often provide unexpected permeation pathways for a large variety of anions
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