Summary: Bacteriocin (Lactococcin_972)
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Bacteriocin Edit Wikipedia article
Bacteriocins are proteinaceous toxins produced by bacteria to inhibit the growth of similar or closely related bacterial strain(s). They are typically considered to be narrow spectrum antibiotics, though this has been debated. They are phenomenologically analogous to yeast and paramecium killing factors, and are structurally, functionally, and ecologically diverse.
Bacteriocins were first discovered by A. Gratia in 1925. He was involved in the process of searching for ways to kill bacteria, which also resulted in the development of antibiotics and the discovery of bacteriophage, all within a span of a few years. He called his first discovery a colicine because it killed E. coli.
Classification of bacteriocins
Bacteriocins are categorized in several ways, including producing strain, common resistance mechanisms, and mechanism of killing. There are several large categories of bacteriocin which are only phenomenologically related. These include the bacteriocins from gram-positive bacteria, the colicins, the microcins, and the bacteriocins from Archaea. The bacteriocins from E. coli are called colicins (formerly called 'colicines,' meaning 'coli killers'). They are the longest studied bacteriocins. They are a diverse group of bacteriocins and do not include all the bacteriocins produced by E. coli. For example the bacteriocins produced by Staphylococcus warneri are called as warnerin or warnericin. In fact, one of the oldest known so-called colicins was called colicin V and is now known as microcin V. It is much smaller and produced and secreted in a different manner than the classic colicins.
This naming system is problematic for a number of reasons. First, naming bacteriocins by what they putatively kill would be more accurate if their killing spectrum were contiguous with genus or species designations. The bacteriocins frequently possess spectra that exceed the bounds of their named taxa and almost never kill the majority of the taxa for which they are named. Further, the original naming is generally derived not from the sensitive strain the bacteriocin kills, but instead the organism that produces the bacteriocin. This makes the use of this naming system a problematic basis for theory; thus the alternative classification systems.
Methods of classification
Alternative methods of classification include: method of killing (pore forming, dnase, nuclease, murein production inhibition, etc.), genetics (large plasmids, small plasmids, chromosomal), molecular weight and chemistry (large protein, polypeptide, with/without sugar moiety, containing atypical amino acids like lanthionine) and method of production (ribosomal, post ribosomal modifications, non-ribosomal).
One method of classification fits the bacteriocins into Class I, Class IIa/b/c, and Class III. 
Class I bacteriocins
Class II bacteriocins
The class II bacteriocins are small (<10 kDa) heat-stable proteins. This class is subdivided into five subclassses. The class IIa bacteriocins (pediocin-like bacteriocins) are the largest subgroup and contain an N-terminal consensus sequence -Tyr-Gly-Asn-Gly-Val-Xaa-Cys across this group. The C-terminal is responsible for species-specific activity, causing cell-leakage by permeabilizing the target cell wall.
Class IIa bacteriocins have a large potential for use in food preservation as well medical applications, due to their strong antilisterial activity, and broad range of activity. One example of Class IIa bacteriocin is pediocin PA-1.
The class IIb bacteriocins (two-peptide bacteriocins) require two different peptides for activity. One such an example is lactococcin G, which permeabilizes cell membranes for monovalent ions such as Na and K, but not for divalents ones. Almost all of this bacteriocins have a GxxxG motifs. This motif is also found in transmembrane proteins where they are involved in helix-helix interactions. The bacteriocins GxxxG motifs can interact with the motifs in the membranes of the bacterial cells and kill the bacteria by doing so.
Class IIc encompasses cyclic peptides, which possesses the N-terminal and C-terminal regions covalentely linked. Enterocin AS-48 is the prototype of this group.
Class IId cover single-peptide bacteriocins, which are not post-translated modified and do not show the pediocin-like signature. The best example of this group is the highly stable aureocin A53. This bacteriocin is stable under highly acidic environment (HCl 6 N), not affected by proteases and thermoresistant.
The most recently proposed subclass is the Class IIe, which encompasses those bacteriocins composed by three or four non-pediocin like peptides. The best example is aureocin A70, a four-peptides bacteriocin, highly active against L. monocytogenes, with potential biotechnological applications.
Class III bacteriocins
Class III bacteriocins are large, heat-labile (>10 kDa) protein bacteriocins. This class is subdivided in two subclasses: subclass IIIa or bacteriolysins and subclass IIIb. Subclass IIIa comprises those peptides that kill bacterial cells by cell-wall degradation, thus causing cell lysis. The best studied bacteriolysin is lysostaphin, a 27 kDa peptide that hydrolises several Staphylococcus spp. cell walls, principally S. aureus. Subclass IIIb, in contrast, comprises those peptides that do not cause cell lysis, killing the target cells by disrupting the membrane potential, which causes ATP efflux .
Class IV bacteriocins
Class IV bacteriocins are defined as complex bacteriocins containing lipid or carbohydrate moities. Confirmatory experimental data was only recently established with the characterisation of Sublancin and Glycocin F (GccF) by two independent groups.
Bacteriocins are of interest in medicine because they are made by non-pathogenic bacteria that normally colonize the human body. Loss of these harmless bacteria following antibiotic use may allow opportunistic pathogenic bacteria to invade the human body.
Bacteriocins have also been suggested as a cancer treatment. They have shown distinct promise as a diagnostic agent for some cancers, but their status as a form of therapy remains experimental and outside the main thread of cancer research. Partly this is due to questions about their mechanism of action and the presumption that anti-bacterial agents have no obvious connection to killing mammalian tumor cells. Some of these questions have been addressed, at least in part.
Bacteriocins[which?] were tested as AIDS drugs around 1990, but did not progress beyond in-vitro tests on cell lines. Bacteriocins can target individual bacterial species, or provide broad-spectrum killing of many microbes. As with today's antibiotics, bacteria can evolve to resist bacteriocins. However, they can be bioengineered to regain their effectiveness. Further, they could be produced in the body by intentionally introduced beneficial bacteria, as some probiotics do.
There are many ways to demonstrate bacteriocin production, depending on the sensitivity and labor intensiveness desired. To demonstrate their production, technicians stab inoculate multiple strains on separate multiple nutrient agar Petri dishes, incubate at 30 °C for 24 h., overlay each plate with one of the strains (in soft agar), incubate again at 30 °C for 24 h. After this process, the presence of bacteriocins can be inferred if there are zones of growth inhibition around stabs. This is the simplest and least sensitive way. It will often mistake phage for bacteriocins. Some methods prompt production with UV radiation, Mitomycin C, or heat shock. UV radiation and Mitomycin C are used because the DNA damage they produce stimulates the SOS response. Cross streaking may be substituted for lawns. Similarly, production in broth may be followed by dripping the broth on a nascent bacterial lawn, or even filtering it. Precipitation (ammonium sulfate) and some purification (e.g. column or HPLC) may help exclude lysogenic and lytic phage from the assay.
Bacteriocins by name
- Farkas-Himsley H (1980). "Bacteriocins--are they broad-spectrum antibiotics?". J. Antimicrob. Chemother. 6 (4): 424–6. doi:10.1093/jac/6.4.424. PMID 7430010.
- Gratia A (1925). "Sur un remarquable example d'antagonisme entre deux souches de colibacille". Compt. Rend. Soc. Biol. 93: 1040–2.
- Gratia JP (October 2000). "André Gratia: a forerunner in microbial and viral genetics". Genetics 156 (2): 471–6. PMC 1461273. PMID 11014798.
- Cascales E, Buchanan SK, Duché D, et al. (March 2007). "Colicin Biology". Microbiol. Mol. Biol. Rev. 71 (1): 158–229. doi:10.1128/MMBR.00036-06. PMC 1847374. PMID 17347522.
- Prema P, Bharathy S, Palavesam A, Sivasubramanian M, Immanuel G (2006). "Detection, purification and efficacy of warnerin produced by Staphylococcus warneri". World Journal of Microbiology and Biotechnology 22 (8): 865–72. doi:10.1007/s11274-005-9116-y.
- Cotter PD, Hill C, Ross RP (2006). "What's in a name? Class distinction for bacteriocins". Nature Reviews Microbiology 4 (2). doi:10.1038/nrmicro1273-c2. is author reply to comment on article :Cotter PD, Hill C, Ross RP (2005). "Bacteriocins: developing innate immunity for food". Nature Reviews Microbiology 3 (?): 777–88. doi:10.1038/nrmicro1273. PMID 16205711.
- HENG, C. K. N., WESCOMBE, P. A., BURTON, J. P., JACK, R. W., & TAGG, J. R. (2007). The diversity of bacteriocins in Gram-positive bacteria. In: Bacteriocins: Ecology and Evolution. 1st ed., Riley, M. A. & Chavan, M. A., Eds. Springer, Hildberg, p. 45-83.
- USA (2013-08-12). "Structure-function relationships of th... [Curr Pharm Biotechnol. 2009] - PubMed - NCBI". Ncbi.nlm.nih.gov. PMID 19149588. Retrieved 2013-12-21.
- NETZ D. J., POHL , BECK-SICKINGER A. G., SELMER , PIERIK , SAHL H. G. (2002). "Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus". J. Mol. Biol 319: 745–756.
- NETZ D. J. A., SAHL , NASCIMENTO , OLIVEIRA , SOARES , BASTOS M. C. F. (2001). "Molecular characterisation of aureocin A70, a multiple-peptide bacteriocin isolated from Staphylococcus aureus". J. Mol. Biol 311: 939–949.
- Bastos M.C.F., Coutinho B.G., Coelho M.L.V. Lysostaphin: A Staphylococcal Bacteriolysin with Potential Clinical Applications. Pharmaceuticals. 2010; 3(4):1139-1161.
- Oman T. J., Boettcher J. M., Wang H., Okalibe X. N., & Van der Donk W. A: Sublancin is not a Lantibiotic but an s-Linked Glycopeptide. Nat Chem Biol. 2011; 7(2):78-80.
- Stepper J., Shastri S., Loo T. S., Preston J. C., Novak P., Man P., Moore C. H., Havlíček V., Patchett M. L., and Norris G. E:Cysteine s-Glycosylation, A New Post-Translational Modification Found In Glycopeptide Bacteriocins. FEBS letters. 2011; 585:645-650.
- de Jong A, van Hijum S A F T, Bijlsma J J E, Kok J, Kuipers O P (2006). "BAGEL: a web-based bacteriocin genome mining tool". Nucleic Acids Research 34 (9): W273–W279. doi:10.1093/nar/gkl237. PMID 1538908.
- Hammami R, Zouhir A, Ben Hamida J, Fliss I (2007). "BACTIBASE: a new web-accessible database for bacteriocin characterization". BMC Microbiology 7: 89. doi:10.1186/1471-2180-7-89. PMC 2211298. PMID 17941971.
- Hammami R, Zouhir A, Le Lay C, Ben Hamida J, Fliss I (2010). "BACTIBASE second release: a database and tool platform for bacteriocin characterization". BMC Microbiology 10: 22. doi:10.1186/1471-2180-10-22. PMC 2824694. PMID 20105292.
- Farkas-Himsley H, Yu H (1985). "Purified colicin as cytotoxic agent of neoplasia: comparative study with crude colicin". Cytobios 42 (167–168): 193–207. PMID 3891240.
- Baumal R, Musclow E, Farkas-Himsley H, Marks A (1982). "Variants of an interspecies hybridoma with altered tumorigenicity and protective ability against mouse myeloma tumors". Cancer Res. 42 (5): 1904–8. PMID 7066902.
- Saito H, Watanabe T, Osasa S, Tado O (1979). "Susceptibility of normal and tumor cells to mycobacteriocin and mitomycin C". Hiroshima J. Med. Sci. 28 (3): 141–6. PMID 521305.
- Cruz-Chamorro L, Puertollano MA, Puertollano E, de Cienfuegos GA, de Pablo MA (2006). "In vitro biological activities of magainin alone or in combination with nisin". Peptides 27 (6): 1201–9. doi:10.1016/j.peptides.2005.11.008. PMID 16356589.
- Sand SL, Haug TM, Nissen-Meyer J, Sand O (2007). "The bacterial peptide pheromone plantaricin A permeabilizes cancerous, but not normal, rat pituitary cells and differentiates between the outer and inner membrane leaflet". J. Membr. Biol. 216 (2–3): 61–71. doi:10.1007/s00232-007-9030-3. PMID 17639368.
- Farkas-Himsley H, Hill R, Rosen B, Arab S, Lingwood CA (1995). "The bacterial colicin active against tumor cells in vitro and in vivo is verotoxin 1". Proceedings of the National Academy of Sciences of the United States of America 92 (15): 6996–7000. doi:10.1073/pnas.92.15.6996. PMC 41458. PMID 7624357.
- Musclow CE, Farkas-Himsley H, Weitzman SS, Herridge M (1987). "Acute lymphoblastic leukemia of childhood monitored by bacteriocin and flowcytometry". Eur J Cancer Clin Oncol 23 (4): 411–8. doi:10.1016/0277-5379(87)90379-8. PMID 3475205.
- Farkas-Himsley H, Zhang YS, Yuan M, Musclow CE (1992). "Partially purified bacteriocin kills malignant cells by apoptosis: programmed cell death". Cell. Mol. Biol. (Noisy-le-grand) 38 (5–6): 643–51. PMID 1483114.
- Farkas-Himsley H, Musclow CE (1986). "Bacteriocin receptors on malignant mammalian cells: are they transferrin receptors?". Cell. Mol. Biol. 32 (5): 607–17. PMID 3779762.
- Farkas-Himsley H, Freedman J, Read SE, Asad S, Kardish M (1991). "Bacterial proteins cytotoxic to HIV-1-infected cells". AIDS 5 (7): 905–7. doi:10.1097/00002030-199107000-00025. PMID 1892605. "Could someone please quote the relevant text"
- "What Comes After Antibiotics? 5 Alternatives to Stop Superbugs". Popular Mechanics. Retrieved 2013-12-21.
- Mørtvedt, C. I.; Nissen-Meyer, J.; Sletten, K.; Nes, I. F. (1991). "Purification and amino acid sequence of lactocin S, a bacteriocin produced by Lactobacillus sake L45". Applied and environmental microbiology 57 (6): 1829–1834. PMC 183476. PMID 1872611.
- Michel-Briand, Y.; Baysse, C. (2002). "The pyocins of Pseudomonas aeruginosa". Biochimie 84 (5–6): 499–510. PMID 12423794.
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Bacteriocin (Lactococcin_972) Provide feedback
These sequences represent bacteriocins related to lactococcin. Members tend to be found in association with a seven transmembrane putative immunity protein.
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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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|Author:||TIGRFAMs, Coggill P|
|Number in seed:||6|
|Number in full:||605|
|Average length of the domain:||60.30 aa|
|Average identity of full alignment:||44 %|
|Average coverage of the sequence by the domain:||66.27 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the More....
This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.
How the sunburst is generated
The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:
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Segments of the tree are coloured approximately according to their superkingdom. For example, archeal branches are coloured with shades of orange, eukaryotes in shades of purple, etc. The colour assignments are shown under the sunburst controls. Where space allows, the name of the taxonomic level will be written on the arc itself.
As you move your mouse across the sunburst, the current node will be highlighted. In the top section of the controls panel we show a summary of the lineage of the currently highlighed node. If you pause over an arc, a tooltip will be shown, giving the name of the taxonomic level in the title and a summary of the number of sequences and species below that node in the tree.
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There are some situations that the sunburst tree cannot easily handle and for which we have work-arounds in place.
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Some species in the taxonomic tree may not have one or more of the main eight levels that we display. For example, Bos taurus is not assigned an order in the NCBI taxonomic tree. In such cases we mark the omitted level with, for example, "No order", in both the tooltip and the lineage summary.
Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
So that these nodes are not simply omitted from the sunburst tree, we group them together in a separate branch (or segment of the sunburst tree). Since we cannot determine the lineage for these unmapped species, we show all levels between the superkingdom and the species as "uncategorised".
Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
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For large species trees, you may see blank regions in the outer layers of the sunburst. These occur when there are large numbers of arcs to be drawn in a small space. If an arc is less than approximately one pixel wide, it will not be drawn and the space will be left blank. You may still be able to get some information about the species in that region by moving your mouse across the area, but since each arc will be very small, it will be difficult to accurately locate a particular species.
The tree shows the occurrence of this domain across different species. More...
We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.
Unfortunately we have found that there are problems viewing the interactive tree when the it becomes larger than a certain limit. Furthermore, we have found that Internet Explorer can become unresponsive when viewing some trees, regardless of their size. We therefore show a text representation of the species tree when the size is above a certain limit or if you are using Internet Explorer to view the site.
If you are using IE you can still load the interactive tree by clicking the "Generate interactive tree" button, but please be aware of the potential problems that the interactive species tree can cause.
For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.
Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
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