Summary: Encapsulating protein for peroxidase
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Encapsulating protein for peroxidase Provide feedback
The Linocin_M18 is found in eubacteria and archaea [1,2]. These proteins, referred to as encapsulins, form nanocompartments within the bacterium which contain ferritin-like proteins or peroxidases, enzymes involved in oxidative-stress response. These enzymes are targeted to the interior of encapsulins via unique C-terminal extensions .
Valdes-Stauber N, Scherer S; , Appl Environ Microbiol 1996;62:1283-1286.: Nucleotide sequence and taxonomical distribution of the bacteriocin gene lin cloned from Brevibacterium linens M18. PUBMED:8919789 EPMC:8919789
Sutter M, Boehringer D, Gutmann S, Gunther S, Prangishvili D, Loessner MJ, Stetter KO, Weber-Ban E, Ban N;, Nat Struct Mol Biol. 2008;15:939-947.: Structural basis of enzyme encapsulation into a bacterial nanocompartment. PUBMED:19172747 EPMC:19172747
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007544Many Gram-positive bacteria produce antimicrobial peptides, generally termed bacteriocins. These peptides are usually cationic, less than 50 amino acid residues long, contain an amphiphilic or hydrophobic region, and often kill their target cells by permeabilizing the cell membrane. Antimicrobial peptides with these characteristics are also produced by plants and a wide variety of animals, including humans, and are thus widely distributed in nature. The Linocin_M18 region is found mostly in eubacteria, though homologous sequences have been identified in archaea [PUBMED:8919789, PUBMED:7986050].
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|Molecular function||peptidase activity (GO:0008233)|
|Biological process||defense response to bacterium (GO:0042742)|
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Curation and family details
|Author:||Waterfield DI, Finn RD|
|Number in seed:||59|
|Number in full:||323|
|Average length of the domain:||246.00 aa|
|Average identity of full alignment:||34 %|
|Average coverage of the sequence by the domain:||89.18 %|
|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:||7|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Linocin_M18 domain has been found. There are 13 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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