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Hol44 Family
The Holin Hol44 (Hol44) Family (TC# 1.E.29) is a group of transporters belonging to the Holin Superfamily V. A representative list of proteins belonging to the Hol44 family from caudovirales and Bacillota can be found in thTransporter Classification Database. One characteristic member of the Hol44 family is oenophage fOg44 (Lys44TC# 1.E.29.2.1, which secretes an endolysin that '' Oenococcus oeni'' cells are intrinsically resistant to. Full activity of Lys44 requires dissipation of the proton motive force induced by fOg44 holin during phage infection. See also * Holin * Lysin Lysins, also known as endolysins or murein hydrolases, are hydrolytic enzymes produced by bacteriophages in order to cleave the host's cell wall during the final stage of the lytic cycle. Lysins are highly evolved enzymes that are able to target ... * Transporter Classification Database Further reading "hol44 - Hol44 - Oenococcus phage fOg44 - hol44 gene & protein" ''www.uniprot.org''. Retrieved 20 ...
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Holin Superfamily V
The Holin superfamily V is a superfamily of integral membrane transport proteins. It is one of the seven different holin superfamilies in total. In general, these proteins are thought to play a role in regulated cell death, although functionality varies between families and individual members. The Holin superfamily V includes the TC families: 1.E.21- The Listeria Phage A118 Holin (Hol118) Family 1.E.29- The Holin Hol44 (Hol44) Family Superfamily V includes protein families classified in the Transporter Classification Database aTC# 1.E.21anTC# 1.E.29 Both families possess members from ''Bacillota'', ''Actinomycetota'' and ''Chloroflexota''. Proteins of this superfamily all appear to have 3 transmembrane segments (TMSs) and have average sizes of 97 and 101 amino acyl residues (aas), respectively. See also * Holin * Lysin Lysins, also known as endolysins or murein hydrolases, are hydrolytic enzymes produced by bacteriophages in order to cleave the host's cell wall during the ...
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Caudovirales
''Caudovirales'' is an order of viruses known as the tailed bacteriophages (''cauda'' is Latin for "tail"). Under the Baltimore classification scheme, the ''Caudovirales'' are group I viruses as they have double stranded DNA (dsDNA) genomes, which can be anywhere from 18,000 base pairs to 500,000 base pairs in length. The virus particles have a distinct shape; each virion has an icosahedral head that contains the viral genome, and is attached to a flexible tail by a connector protein. The order encompasses a wide range of viruses, many containing genes of similar nucleotide sequence and function. However, some tailed bacteriophage genomes can vary quite significantly in nucleotide sequence, even among the same genus. Due to their characteristic structure and possession of potentially homologous genes, it is believed these bacteriophages possess a common origin. There are 14 families, 73 subfamilies, 927 genera, and 2,814 species in the order. This makes ''Caudovirales'' the ...
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Bacillota
The Bacillota (synonym Firmicutes) are a phylum of bacteria, most of which have gram-positive cell wall structure. The renaming of phyla such as Firmicutes in 2021 remains controversial among microbiologists, many of whom continue to use the earlier names of long standing in the literature. The name "Firmicutes" was derived from the Latin words for "tough skin," referring to the thick cell wall typical of bacteria in this phylum. Scientists once classified the Firmicutes to include all gram-positive bacteria, but have recently defined them to be of a core group of related forms called the low- G+C group, in contrast to the Actinomycetota. They have round cells, called cocci (singular coccus), or rod-like forms (bacillus). A few Firmicutes, such as ''Megasphaera'', ''Pectinatus'', ''Selenomonas'' and ''Zymophilus'', have a porous pseudo-outer membrane that causes them to stain gram-negative. Many Bacillota (Firmicutes) produce endospores, which are resistant to desiccation and can ...
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Oenococcus Oeni
''Oenococcus oeni'' (known as ''Leuconostoc oeni'' until 1995) is a Gram-positive bacterial species in the genus of ''Oenococcus''. It was the only species in the genus until 2006, when the species ''Oenococcus kitaharae'' was identified. As its name implies, ''Oe. oeni'' holds major importance in the field of oenology, where it is the primary bacterium involved in completing the malolactic fermentation.Kunkee, R. E. 1973. Malo-Lactic Fermentation and Winemaking. In, The Chemistry of Winemaking, Adv. Chem. Ser. 137, A. D. Webb, Ed. American Chemical Society. Washington DC. Diacetyl Diacetyl in wine is produced by lactic acid bacteria, mainly ''Oe. oeni''. In low levels, it can impart positive nutty or caramel characters, but at levels above 5 mg/L, it creates an intense buttery or butterscotch flavour, where it is perceived as a flaw. The sensory threshold for the compound can vary depending on the levels of certain wine components, such as sulfur dioxide. It can be produ ...
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Chemiosmosis
Chemiosmosis is the movement of ions across a semipermeable membrane bound structure, down their electrochemical gradient. An important example is the formation of adenosine triphosphate (ATP) by the movement of hydrogen ions (H+) across a membrane during cellular respiration or photosynthesis. Hydrogen ions, or protons, will diffuse from a region of high proton concentration to a region of lower proton concentration, and an electrochemical concentration gradient of protons across a membrane can be harnessed to make ATP. This process is related to osmosis, the movement of water across a selective membrane, which is why it is called "chemiosmosis". ATP synthase is the enzyme that makes ATP by chemiosmosis. It allows protons to pass through the membrane and uses the free energy difference to phosphorylate adenosine diphosphate (ADP), making ATP. The generation of ATP by chemiosmosis occurs in mitochondria and chloroplasts, as well as in most bacteria and archaea. For instan ...
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Holin
Holins are a diverse group of small proteins produced by dsDNA bacteriophages in order to trigger and control the degradation of the host's cell wall at the end of the lytic cycle. Holins form pores in the host's cell membrane, allowing lysins to reach and degrade peptidoglycan, a component of bacterial cell walls. Holins have been shown to regulate the timing of lysis with great precision. Over 50 unrelated gene families encode holins, making them the most diverse group of proteins with common function. Together with lysins, holins are being studied for their potential use as antibacterial agents. While canonical holins act by forming large pores, pinholins such as the S protein of lambdoid phage 21 act by forming heptameric channels that depolarize the bacterial membrane. They are associated with SAR endolysins, which remain inactive in the periplasm prior to the depolarization of the membrane. Viruses that infect eukaryotic cells may use similar channel-forming proteins called ...
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Lysin
Lysins, also known as endolysins or murein hydrolases, are hydrolytic enzymes produced by bacteriophages in order to cleave the host's cell wall during the final stage of the lytic cycle. Lysins are highly evolved enzymes that are able to target one of the five bonds in peptidoglycan (murein), the main component of bacterial cell walls, which allows the release of progeny virions from the lysed cell. Cell-wall-containing Archaea are also lysed by specialized pseudomurein-cleaving lysins, while most archaeal viruses employ alternative mechanisms. Similarly, not all bacteriophages synthesize lysins: some small single-stranded DNA and RNA phages produce membrane proteins that activate the host's autolytic mechanisms such as autolysins. Lysins are being used as antibacterial agents due to their high effectiveness and specificity in comparison with antibiotics, which are susceptible to bacterial resistance. Structure Double-stranded DNA phage lysins tend to lie within the 25 to 40 ...
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Holins
Holins are a diverse group of small proteins produced by dsDNA bacteriophages in order to trigger and control the degradation of the host's cell wall at the end of the lytic cycle. Holins form pores in the host's cell membrane, allowing lysins to reach and degrade peptidoglycan, a component of bacterial cell walls. Holins have been shown to regulate the timing of lysis with great precision. Over 50 unrelated gene families encode holins, making them the most diverse group of proteins with common function. Together with lysins, holins are being studied for their potential use as antibacterial agents. While canonical holins act by forming large pores, pinholins such as the S protein of lambdoid phage 21 act by forming heptameric channels that depolarize the bacterial membrane. They are associated with SAR endolysins, which remain inactive in the periplasm prior to the depolarization of the membrane. Viruses that infect eukaryotic cells may use similar channel-forming proteins calle ...
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