Summary: Type VI secretion system effector, Hcp
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Type VI secretion system effector, Hcp Provide feedback
HCP is a family of proteins which are expressed in up to 1000 copies in Gram-negative bacteria. Together these copies aggregate into a needle-like shaft or tube that will penetrate other bacteria via a puncturing protein attached to its head [1]. Initially Hcp forms a hexameric structure with a central channel of 40 Angstroms. These hexamers pile up one on top of each other forming nanotubes resembling the gp19 tail phage tube [2].
Literature references
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Filloux A;, F1000Prime Rep. 2013;5:52.: The rise of the Type VI secretion system. PUBMED:24381728 EPMC:24381728
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Mougous JD, Cuff ME, Raunser S, Shen A, Zhou M, Gifford CA, Goodman AL, Joachimiak G, Ordonez CL, Lory S, Walz T, Joachimiak A, Mekalanos JJ;, Science. 2006;312:1526-1530.: A virulence locus of Pseudomonas aeruginosa encodes a protein secretion apparatus. PUBMED:16763151 EPMC:16763151
Internal database links
Similarity to PfamA using HHSearch: | TssD |
This tab holds annotation information from the InterPro database.
InterPro entry IPR008514
This entry consists of Hcp-like proteins. Hcp appears to be part of the type VI secretion system of Gram-negative bacteria. Hcp is not only a secreted effector protein, but also might act as machine component [ PUBMED:18617888 ].
Several bacterial pathogens mediate interactions with their hosts through protein secretion, often involving Hcp-like virulence loci, which are widely distributed among pathogenic bacteria. Homologues of Hcp are found in various bacteria of which most, but not all, are known pathogens. Many bacteria have two copies of hcp genes [ PUBMED:22184413 , PUBMED:23519162 ]. In Pseudomonas syringae, Hcp1 is a virulence protein, while Hcp2 seems to be required for survival in competition with enterobacteria and yeasts, and its function is associated with the suppression of the growth of these competitors [ PUBMED:22753062 ].
Hcp1 monomers form a hexameric ring with a large internal diameter. Assembly of this particle is likely to occur following secretion, and could have a role in building a channel for the transport of other macromolecules [ PUBMED:16763151 ].
The type VI secretion system (T6SS) is a supra-molecular bacterial complex that resembles phage tails. It is a toxin delivery systems which fires toxins into target cells upon contraction of its TssBC sheath [ PUBMED:27288401 ]. Thirteen essential core proteins are conserved in all T6SSs: the membrane associated complex TssJ-TssL-TssM, the baseplate proteins TssE, TssF, TssG, and TssK, the bacteriophage-related puncturing complex composed of the tube (Hcp), the tip/puncturing device VgrG, and the contractile sheath structure (TssB and TssC). Finally, the starfish-shaped dodecameric protein, TssA, limits contractile sheath polymerization at its distal part when TagA captures TssA [ PUBMED:31379775 ].
Domain organisation
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Alignments
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Seed (152) |
Full (2196) |
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RP15 (229) |
RP35 (842) |
RP55 (2253) |
RP75 (5465) |
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PP/heatmap | 1 |
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Seed (152) |
Full (2196) |
Representative proteomes | UniProt (20021) |
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RP15 (229) |
RP35 (842) |
RP55 (2253) |
RP75 (5465) |
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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_9698 (release 8.0) |
Previous IDs: | DUF796; HCP; |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Moxon SJ |
Number in seed: | 152 |
Number in full: | 2196 |
Average length of the domain: | 133.40 aa |
Average identity of full alignment: | 24 % |
Average coverage of the sequence by the domain: | 76.50 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
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Model length: | 129 | ||||||||||||
Family (HMM) version: | 14 | ||||||||||||
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 T6SS_HCP domain has been found. There are 87 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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