Bacterial proteins

Cas9 (CRISPR-associated protein 9, formerly Cas5, Csn1, or Csx12) is a DNA cutting enzyme that is part of the CRISPR immune system in bacteria and archaea. It has been adapted to be used as a CRISPR genome editing tool that enables targeted modification of DNA sequences and permanently changes a cell’s genome.

protein complex secreted by the bacterium Vibrio cholerae

Streptavidin is a 52 kDa protein (tetramer) purified from the bacterium Streptomyces avidinii. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin (also known as vitamin B7 or vitamin H). With a dissociation constant (Kd) on the order of ≈10−14 mol/L, the binding of biotin to streptavidin is one of the strongest non-covalent interactions known in nature. Streptavidin is used extensively in molecular biology and bionanotechnology due to the streptavidin-biotin complex's resistance to organic solvents, denaturants (e.g. guanidinium chloride), detergents (e.g. SDS, Triton

Flagellins are a family of proteins present in flagellated bacteria which arrange themselves in a hollow cylinder to form the filament in a bacterial flagellum. Flagellin has a mass on average of about 40,000 daltons. Flagellins are the principal component of bacterial flagella that have a crucial role in bacterial motility.

FtsZ is a protein encoded by the ftsZ gene that assembles into a ring at the future site of bacterial cell division (also called the Z ring). FtsZ is a prokaryotic homologue of the eukaryotic protein tubulin. The initials FtsZ mean "Filamenting temperature-sensitive mutant Z." The hypothesis was that cell division mutants of E. coli would grow as filaments due to the inability of the daughter cells to separate from one another. FtsZ is found in almost all bacteria, many archaea, all chloroplasts and some mitochondria, where it is essential for cell division. FtsZ assembles the cytoskeletal sca

prokaryotic protein

RecA is a 38 kilodalton protein essential for the repair and maintenance of DNA in bacteria. Structural and functional homologs to RecA have been found in all kingdoms of life. RecA serves as an archetype for this class of homologous DNA repair proteins. The homologous protein is called RAD51 in eukaryotes and RadA in archaea.

class of proteins

organelle-like structure in bacteria with a protein shell containing enzymes

Phycobiliproteins are water-soluble proteins present in cyanobacteria and certain algae (rhodophytes, cryptomonads, glaucocystophytes). They capture light energy, which is then passed on to chlorophylls during photosynthesis. Phycobiliproteins are formed of a complex between proteins and covalently bound phycobilins that act as chromophores (the light-capturing part). They are most important constituents of the phycobilisomes. thumb|Phycobilisome structure

DNA-binding protein

Pilin refers to proteins that create pilus structures in bacteria. These structures can be used for the exchange of genetic material, or as a cell adhesion mechanism. Although not all bacteria have pili or fimbriae, bacterial pathogens often use their fimbriae to attach to host cells. In Gram-negative bacteria, where pili are more common, individual pilin molecules are linked by noncovalent protein-protein interactions, while Gram-positive bacteria often have polymerized LPXTG pilin.

Barstar is a small protein synthesized by the bacterium Bacillus amyloliquefaciens. Its function is to inhibit the ribonuclease activity of its binding partner barnase, with which it forms an extraordinarily tightly bound complex within the cell until barnase is secreted. Expression of barstar is necessary to counter the lethal effect of expressed active barnase. The structure of the barnase-barnstar complex is known.

thumb|Allophycocyanin dodekamer, Gloeobacter violaceus () Allophycocyanin ("other algal blue protein"; from Greek: (allos) meaning "other", (phykos) meaning “alga”, and (kyanos) meaning "blue") is a protein from the light-harvesting phycobiliprotein family, along with phycocyanin, phycoerythrin and phycoerythrocyanin. It is an accessory pigment to chlorophyll. All phycobiliproteins are water-soluble and therefore cannot exist within the membrane like carotenoids, but aggregate, forming clusters that adhere to the membrane called phycobilisomes. Allophycocyanin absorbs and emits red light (650

Crescentin is a protein which is a bacterial relative of the intermediate filaments found in eukaryotic cells. Just as tubulins and actins, the other major cytoskeletal proteins, have prokaryotic homologs in, respectively, the FtsZ and MreB proteins, intermediate filaments are linked to the crescentin protein. Some of its homologs are erroneously labelled Chromosome segregation protein ParA. This protein family is found in Caulobacter and Methylobacterium.

Proteorhodopsin (PR or pRhodopsin) belongs to the family of bacterial transmembrane rhodopsins (retinylidene proteins). In 1971, the first microbial transmembrane rhodopsin - Bacteriorhodopsin was discovered in archea domain by Dieter Oesterhelt and Walther Stoeckenius. Later in 2000, the first bacterial transmembrane rhodopsins was discovered by Oded Béjà and Edward DeLong. The Proteorhodopsin is widely expressed in various type of aquatic habitats. It functions as light-driven proton pumps with the help of retinal chromophore at the active site. The light-driven proton pump gives bacteria en

The encapsulins are a family of bacterial proteins that serve as the main structural components of encapsulin nanocompartments. There are several different encapsulin proteins, including EncA, which forms the shell, and EncB, EncC, and EncD, which form the core. They are found in bacteria and archaea. They serve as intracellular structures that compartmentalize specific biochemical reactions. They are highly versatile systems and protect cargo proteins from environmental damage and optimize the efficiency of enzymatic processes.

DnaG is a bacterial DNA primase and is encoded by the dnaG gene. The enzyme DnaG, and any other DNA primase, synthesizes short strands of RNA known as oligonucleotides during DNA replication. These oligonucleotides are known as primers because they act as a starting point for DNA synthesis. DnaG catalyzes the synthesis of oligonucleotides that are 10 to 60 nucleotides (the fundamental unit of DNA and RNA) long, however most of the oligonucleotides synthesized are 11 nucleotides. These RNA oligonucleotides serve as primers, or starting points, for DNA synthesis by bacterial DNA polymerase III (

protein