Summary: Type II secretion system (T2SS), protein L
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Type II secretion system (T2SS), protein L Provide feedback
This family consists of Type II secretion system protein L sequences from several Gram-negative (diderm) bacteria. The Type II secretion system, also called Secretion-dependent pathway (SDP), is responsible for extracellular secretion of a number of different proteins, including proteases and toxins. This pathway supports secretion of proteins across the cell envelope in two distinct steps, in which the second step, involving translocation through the outer membrane, is assisted by at least 13 different gene products. T2SL is predicted to contain a large cytoplasmic domain represented by this family and has been shown to interact with the autophosphorylating cytoplasmic membrane protein T2SE. It is thought that the tri-molecular complex of T2SL, T2SE (PF00437) and T2SM (PF04612) might be involved in regulating the opening and closing of the secretion pore and/or transducing energy to the site of outer membrane translocation .
Sandkvist M, Hough LP, Bagdasarian MM, Bagdasarian M; , J Bacteriol 1999;181:3129-3135.: Direct interaction of the EpsL and EpsM proteins of the general secretion apparatus in Vibrio cholerae. PUBMED:10322014 EPMC:10322014
Peabody CR, Chung YJ, Yen MR, Vidal-Ingigliardi D, Pugsley AP, Saier MH Jr;, Microbiology. 2003;149:3051-3072.: Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella. PUBMED:14600218 EPMC:14600218
Desvaux M, Hebraud M, Talon R, Henderson IR;, Trends Microbiol. 2009;17:139-145.: Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. PUBMED:19299134 EPMC:19299134
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR024230
The general secretion pathway of Gram-negative bacteria is responsible for extracellular secretion of a number of different proteins, including proteases and toxins. This pathway supports secretion of proteins across the cell envelope in two distinct steps, in which the second step, involving translocation through the outer membrane, is assisted by at least 13 different gene products. GspL is predicted to contain a large cytoplasmic domain and has been shown to interact with the autophosphorylating cytoplasmic membrane protein GspE. It is thought that the tri-molecular complex of GspL, GspE and GspM might be involved in regulating the opening and closing of the secretion pore and/or transducing energy to the site of outer membrane translocation [PUBMED:10322014].
This N-terminal domain is found in general secretion pathway protein L sequences from several Gram-negative bacteria. It is a cytoplasmic domain that shows structural homology with the superfamily of actin-like ATPases [PUBMED:15533433].
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Curation and family details
|Seed source:||Pfam-B_6494 (release 7.7)|
|Author:||Moxon SJ, Bateman A, Desvaux M|
|Number in seed:||19|
|Number in full:||962|
|Average length of the domain:||221.90 aa|
|Average identity of full alignment:||22 %|
|Average coverage of the sequence by the domain:||57.66 %|
|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:||8|
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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 T2SL domain has been found. There are 4 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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