type II secretion system protein L (GspL) is an inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm
N-terminal domain of type II secretion system protein L (T2SSL) and similar proteins; Type II ...
4-238
5.07e-46
N-terminal domain of type II secretion system protein L (T2SSL) and similar proteins; Type II secretion system is composed of four main components: the outer membrane complex, the inner membrane complex, the cytoplasmic secretion ATPase and the periplasm-spanning pseudopilus. T2SSL, also called T2SS protein L, or general secretion pathway protein L, is an inner membrane component of the type II secretion system, also called secretion-dependent pathway (SDP), required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. T2SSL is predicted to contain a large cytoplasmic domain and has been shown to interact with the autophosphorylating cytoplasmic membrane protein T2SSE. It is thought that the tri-molecular complex of T2SSL, T2SSE and T2SSM might be involved in regulating the opening and closing of the secretion pore and/or transducing energy to the site of outer membrane translocation. The model corresponds to the N-terminal domain of T2SSL. It is a cytoplasmic domain that shows structural homology with the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains. T2SSL is entirely missing domains 1B and 2B of the typical ASKHA proteins. The domain 2B of the ASKHA superfamily is critically important for binding the adenosine part of ATP. Due to the absence of 2B domain in T2SSL, it is therefore unlikely that T2SSL is an ATP-binding protein.
Pssm-ID: 466867 [Multi-domain] Cd Length: 226 Bit Score: 157.92 E-value: 5.07e-46
type II secretion system protein L; This model represents GspL, protein L of the main terminal ...
12-402
1.23e-35
type II secretion system protein L; This model represents GspL, protein L of the main terminal branch of the general secretion pathway, also called type II secretion. It transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273768 [Multi-domain] Cd Length: 384 Bit Score: 134.50 E-value: 1.23e-35
Type II secretion system (T2SS), protein L; This family consists of Type II secretion system ...
24-238
1.96e-22
Type II secretion system (T2SS), protein L; 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 (pfam00437) and T2SM (pfam04612) might be involved in regulating the opening and closing of the secretion pore and/or transducing energy to the site of outer membrane translocation.
Pssm-ID: 282928 [Multi-domain] Cd Length: 230 Bit Score: 94.76 E-value: 1.96e-22
N-terminal domain of type II secretion system protein L (T2SSL) and similar proteins; Type II ...
4-238
5.07e-46
N-terminal domain of type II secretion system protein L (T2SSL) and similar proteins; Type II secretion system is composed of four main components: the outer membrane complex, the inner membrane complex, the cytoplasmic secretion ATPase and the periplasm-spanning pseudopilus. T2SSL, also called T2SS protein L, or general secretion pathway protein L, is an inner membrane component of the type II secretion system, also called secretion-dependent pathway (SDP), required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. T2SSL is predicted to contain a large cytoplasmic domain and has been shown to interact with the autophosphorylating cytoplasmic membrane protein T2SSE. It is thought that the tri-molecular complex of T2SSL, T2SSE and T2SSM might be involved in regulating the opening and closing of the secretion pore and/or transducing energy to the site of outer membrane translocation. The model corresponds to the N-terminal domain of T2SSL. It is a cytoplasmic domain that shows structural homology with the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains. T2SSL is entirely missing domains 1B and 2B of the typical ASKHA proteins. The domain 2B of the ASKHA superfamily is critically important for binding the adenosine part of ATP. Due to the absence of 2B domain in T2SSL, it is therefore unlikely that T2SSL is an ATP-binding protein.
Pssm-ID: 466867 [Multi-domain] Cd Length: 226 Bit Score: 157.92 E-value: 5.07e-46
type II secretion system protein L; This model represents GspL, protein L of the main terminal ...
12-402
1.23e-35
type II secretion system protein L; This model represents GspL, protein L of the main terminal branch of the general secretion pathway, also called type II secretion. It transports folded proteins across the bacterial outer membrane and is widely distributed in Gram-negative pathogens. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273768 [Multi-domain] Cd Length: 384 Bit Score: 134.50 E-value: 1.23e-35
Type II secretion system (T2SS), protein L; This family consists of Type II secretion system ...
24-238
1.96e-22
Type II secretion system (T2SS), protein L; 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 (pfam00437) and T2SM (pfam04612) might be involved in regulating the opening and closing of the secretion pore and/or transducing energy to the site of outer membrane translocation.
Pssm-ID: 282928 [Multi-domain] Cd Length: 230 Bit Score: 94.76 E-value: 1.96e-22
GspL periplasmic domain; This domain is the periplasmic domain of the GspL/EpsL family ...
245-402
8.97e-10
GspL periplasmic domain; This domain is the periplasmic domain of the GspL/EpsL family proteins. These proteins are involved in type II secretion systems.
Pssm-ID: 432724 Cd Length: 158 Bit Score: 57.01 E-value: 8.97e-10
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ...
37-133
7.51e-03
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 38.03 E-value: 7.51e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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(labeled illustration).
Domains are color coded according to superfamilies
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Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
mapped to the query sequence.
Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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