Summary: Type II secretion system protein C
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Type II secretion system protein C Provide feedback
This is the greater N-terminal region of GspC-type proteins. GspC proteins form part of the sophisticated transport mechanism of Gram-negative pathogens for injecting divers proteins into their hosts, a type-II secretion system - T2SS. The region is made up of a short N-terminal cytoplasmic domain that is followed by the single transmembrane helix, a Pro-rich linker, and the so-called homology region domain in the periplasm. This inner membrane GspC interacts with the outer membrane secretin GspD via periplasmic domains, an interaction which is critical for the effectiveness of type II secretion [1].
Literature references
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Korotkov KV, Johnson TL, Jobling MG, Pruneda J, Pardon E, Heroux A, Turley S, Steyaert J, Holmes RK, Sandkvist M, Hol WG;, PLoS Pathog. 2011;7:e1002228.: Structural and functional studies on the interaction of GspC and GspD in the type II secretion system. PUBMED:21931548 EPMC:21931548
Internal database links
SCOOP: | Peptidase_M50 |
Similarity to PfamA using HHSearch: | T2SSB |
This tab holds annotation information from the InterPro database.
InterPro entry IPR024961
This is the N-terminal region of GspC proteins, which is part of the Type II secretion system. The region is made up of a short N-terminal cytoplasmic domain that is followed by the single transmembrane helix, a Pro-rich linker, and the so-called homology region domain in the periplasm. This inner membrane GspC interacts with the outer membrane secretin GspD via periplasmic domains, an interaction which is critical for the effectiveness of type II secretion [ PUBMED:21931548 ]. This domain can also be found in GspN from Pseudomonas aeruginosa.
The type II secretion system (T2SS) is one of several extracellular secretion systems in gram-negative bacteria. It delivers toxins and a range of hydrolytic enzymes including proteases, lipases and carbohydrate-active enzymes to the cell surface or extracellular space [ PUBMED:30767847 ]. T2SS systems are composed of 11 to 15 different proteins, which are generally called GspA to GspO and GspS. The T2SS spans the two bacterial membranes and ensures secretion of folded proteins across the outer membrane pore formed by GspD. The inner membrane complex contains GspC, GspL, GspM, and GspF. The cytoplasmic domains of GspL and GspF interact with an ATPase, GspE. GspE is thought to energize the formation of a short pseudopilus by several pilin-like proteins, GspG to GspK [ PUBMED:22523076 ]. GspD has been shown to interact with the inner membrane component GspC [ PUBMED:19217396 ].
The T2SS pseudopilus is a periplasmic filament composed of the major pseudopilin, EpsG, and four minor pseudopilins, EpsH, EpsI, EpsJ and EpsK. Pseudopilus is assembled by the polymerization of GspG (also known as PulG) subunits. Pseudopilin proteins have a conserved N-terminal hydrophobic segment followed by a more variable C-terminal periplasmic and globular domain [ PUBMED:28258547 ].
Domain organisation
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Pfam Clan
Alignments
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Seed (26) |
Full (1223) |
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RP15 (195) |
RP35 (593) |
RP55 (1255) |
RP75 (2309) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (26) |
Full (1223) |
Representative proteomes | UniProt (7904) |
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RP15 (195) |
RP35 (593) |
RP55 (1255) |
RP75 (2309) |
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Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Curation and family details
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Curation
Seed source: | Pfam-B_3750 (release 23.0) |
Previous IDs: | Pilus_PilP; T2SC; T4SC; |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Pollington J |
Number in seed: | 26 |
Number in full: | 1223 |
Average length of the domain: | 132.2 aa |
Average identity of full alignment: | 21 % |
Average coverage of the sequence by the domain: | 51.22 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 145 | ||||||||||||
Family (HMM) version: | 11 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
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 T2SSC domain has been found. There are 17 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 sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.