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Protein A is a 42 kDa surface protein originally found in the cell wall of the bacteria Staphylococcus aureus. It is encoded by the spa gene and its regulation is controlled by DNA topology, cellular osmolarity, and a two-component system called ArlS-ArlR. It has found use in biochemical research because of its ability to bind immunoglobulins ...
Protein A in various recombinant forms has been used for decades to bind and purify a wide range of antibodies by immunoaffinity chromatography. Transpeptidases, such as the sortases responsible for anchoring factors like protein A to the staphylococcal peptidoglycan, are being studied in hopes of developing new antibiotics to target MRSA ...
Bacterial proteins are proteins from which any bacterium may be comprised in its natural state. Subcategories. This category has the following 4 subcategories, out of ...
Motility protein A (MotA), is a bacterial protein that is encoded by the motA gene. It is a component of the flagellar motor. [1] More specifically, MotA and MotB make the stator of a H + driven bacterial flagella and surround the rotor as a ring of about 8–10 particles. MotA and MotB are integral membrane proteins. [2] MotA has four ...
Bacterial microcompartments are widespread, organelle-like structures that are made of a protein shell that surrounds and encloses various enzymes. provide a further level of organization; they are compartments within bacteria that are surrounded by polyhedral protein shells, rather than by lipid membranes. These "polyhedral organelles ...
Replication protein A (RPA) is the major protein that binds to single-stranded DNA (ssDNA) in eukaryotic cells. [ 1 ] [ 2 ] In vitro , RPA shows a much higher affinity for ssDNA than RNA or double-stranded DNA. [ 3 ]
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The bacterial flagellum is made of about 20 proteins, with approximately another 30 proteins required for its regulation and assembly. [145] The flagellum is a rotating structure driven by a reversible motor at the base that uses the electrochemical gradient across the membrane for power.