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Serratia is a genus of Gram-negative, facultatively anaerobic, rod-shaped bacteria of the family Yersiniaceae. According to the List of Prokaryotic names with Standing Nomenclature (LPSN), there are currently 19 species of Serratia that are credibly published with accurate names as of 2020: S. aquatilis, S. entomophila, S. ficaria, S. fonticola, S. grimesii, S. liquefaciens, S. marcescens, S. microhaemolytica, S. myotis, S. nematodiphila, S. odoriferae, S. oryzae, S. plymuthica, S. proteamaculans, S. quinivorans corrig, S. rubidaea, S. symbiotica, S. ureilytica, S. vespertilionis. They are typically 1–5 μm in length, do not produce spores, and can be found in water, soil, plants, and animals. Some members of this genus produce a characteristic red pigment, prodigiosin, and can be distinguished from other members of the order Enterobacterales by their unique production of three enzymes: DNase (nucA), lipase, and gelatinase (serralysin). Serratia was thought to be a harmless environmental bacteria until it was discovered that the most common species in the genus, S. marcescens, is an opportunistic pathogen of many animals, including humans. In humans, S. marcescens is mostly associated with nosocomial, or hospital-acquired, infections, but can also cause urinary tract infections, pneumonia, and endocarditis. S. marcescens is frequently found in showers, toilet bowls, and around wet tiles as a pinkish to red biofilm but only causes disease in immunocompromised individuals. Aside from S. marcescens, some rare strains of the Serratia species S. plymuthica, S. liquefaciens, S. rubidaea, and S. odoriferae have been shown to cause infection such as osteomyelitis and endocarditis.
Aspergillopepsin I is an enzyme. This enzyme catalyses the following chemical reaction
Mezlocillin is a broad-spectrum penicillin antibiotic. It is active against both Gram-negative and some Gram-positive bacteria. Unlike most other extended spectrum penicillins, it is excreted by the liver, therefore it is useful for biliary tract infections, such as ascending cholangitis.
Actinidain is a type of cysteine protease enzyme found in fruits including kiwifruit, pineapple, mango, banana, figs, and papaya. This enzyme is part of the peptidase C1 family of papain-like proteases.
Swarming motility is a rapid and coordinated translocation of a bacterial population across solid or semi-solid surfaces, and is an example of bacterial multicellularity and swarm behaviour. Swarming motility was first reported by Jorgen Henrichsen and has been mostly studied in genus Serratia, Salmonella, Aeromonas, Bacillus, Yersinia, Pseudomonas, Proteus, Vibrio and Escherichia.
In molecular biology, Proteinase K is a broad-spectrum serine protease. The enzyme was discovered in 1974 in extracts of the fungus Parengyodontium album. Proteinase K is able to digest hair (keratin), hence, the name "Proteinase K". The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. It is commonly used for its broad specificity. This enzyme belongs to Peptidase family S8 (subtilisin). The molecular weight of Proteinase K is 28,900 daltons.
Serratiopeptidase is a proteolytic enzyme (protease) produced by enterobacterium Serratia sp. E-15, now known as Serratia marcescens ATCC 21074. This microorganism was originally isolated in the late 1960s from silkworm intestine. Serratiopeptidase is present in the silkworm intestine and allows the emerging moth to dissolve its cocoon. Serratiopeptase is produced by purification from culture of Serratia E-15 bacteria. It is a member of the Peptidase M10B (Matrixin) family.
Cathepsin X is an enzyme. This enzyme catalyses the following chemical reaction
Viable but nonculturable (VBNC) bacteria refers as to bacteria that are in a state of very low metabolic activity and do not divide, but are alive and have the ability to become culturable once resuscitated.
Serratia marcescens nuclease is an enzyme. This enzyme catalyses the following chemical reaction
Lysyl endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Oryzin is an enzyme. This enzyme catalyses the following chemical reaction
Mucorpepsin is an enzyme. This enzyme catalyses the following chemical reaction
Leucolysin is an enzyme. This enzyme catalyses the following chemical reaction
Pseudolysin is an enzyme. This enzyme catalyses the following chemical reaction
Bacillolysin is an enzyme. This enzyme catalyses the following chemical reaction
Aureolysin is an extracellular metalloprotease expressed by Staphylococcus aureus. This protease is a major contributor to the bacterium's virulence, or ability to cause disease, by cleaving host factors of the innate immune system as well as regulating S. aureus secreted toxins and cell wall proteins. To catalyze its enzymatic activities, aureolysin requires zinc and calcium which it obtains from the extracellular environment within the host.
Mycolysin is an enzyme. This enzyme catalyses the following chemical reaction
The HP1 Holin Family is a member of the Holin Superfamily II. Proteins in this family are typically found to contain two transmembrane segments (TMSs) and range between 70 and 80 amino acyl residues (aas) in length. A representative list of proteins belonging to the HP1 holin family can be found in the Transporter Classification Database.
The sedolisin family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin") found in Pseudomonas bacteria, xanthomonalisin ("sedolisin-B"), physarolisin as well as animal tripeptidyl peptidase I. It is also known as sedolysin or serine-carboxyl peptidase. This group of enzymes contains a variation on the catalytic triad: unlike S8 which uses Ser-His-Asp, this group runs on Ser-Glu-Asp, with an additional acidic residue Asp in the oxyanion hole.
References
- ↑ Morihara K, Tsuzuki H, Oka T (March 1968). "Comparison of the specificities of various neutral proteinases from microorganisms". Archives of Biochemistry and Biophysics. 123 (3): 572–88. doi:10.1016/0003-9861(68)90179-3. PMID 4967801.
- ↑ Morihara K, Tsuzuki H, Oka T (June 1973). "On the specificity of Pseudomonas aeruginosa alkaline proteinase with synthetic peptides". Biochimica et Biophysica Acta (BBA) - Enzymology. 309 (2): 414–29. doi:10.1016/0005-2744(73)90040-5. PMID 4199986.
- ↑ Nakajima M, Mizusawa K, Yoshida F (May 1974). "Purification and properties of an extracellular proteinase of psychrophilic Escherichia freundii". European Journal of Biochemistry. 44 (1): 87–96. doi: 10.1111/j.1432-1033.1974.tb03460.x . PMID 4212288.
- ↑ Decedue CJ, Broussard EA, Larson AD, Braymer HD (August 1979). "Purification and characterization of the extracellular proteinase of Serratia marcescens". Biochimica et Biophysica Acta (BBA) - Enzymology. 569 (2): 293–301. doi:10.1016/0005-2744(79)90065-2. PMID 383155.
- ↑ Doerr M, Traub WH (May 1984). "Purification and characterization of two Serratia marcescens proteases". Zentralblatt für Bakteriologie, Mikrobiologie, und Hygiene. Series A, Medical Microbiology, Infectious Diseases, Virology, Parasitology. 257 (1): 6–19. PMID 6380155.
- ↑ Nakahama K, Yoshimura K, Marumoto R, Kikuchi M, Lee IS, Hase T, Matsubara H (July 1986). "Cloning and sequencing of Serratia protease gene". Nucleic Acids Research. 14 (14): 5843–55. doi:10.1093/nar/14.14.5843. PMC 311595 . PMID 3016665.
- ↑ Dahler GS, Barras F, Keen NT (October 1990). "Cloning of genes encoding extracellular metalloproteases from Erwinia chrysanthemi EC16". Journal of Bacteriology. 172 (10): 5803–15. doi:10.1128/jb.172.10.5803-5815.1990. PMC 526898 . PMID 2211513.
- ↑ Okuda K, Morihara K, Atsumi Y, Takeuchi H, Kawamoto S, Kawasaki H, Suzuki K, Fukushima J (December 1990). "Complete nucleotide sequence of the structural gene for alkaline proteinase from Pseudomonas aeruginosa IFO 3455". Infection and Immunity. 58 (12): 4083–8. doi:10.1128/IAI.58.12.4083-4088.1990. PMC 313780 . PMID 2123832.
