Summary: Saf-pilin pilus formation protein
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This is the Wikipedia entry entitled "Saf pilin N-terminal extension". More...
Saf pilin N-terminal extension Edit Wikipedia article
| Saf-Nte_pilin | |||||||||
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| Salmonella enterica SafA pilin in complex with a 19-residue SafA Nte peptide (f17a mutant) | |||||||||
| Identifiers | |||||||||
| Symbol | Saf-Nte_pilin | ||||||||
| Pfam | PF09460 | ||||||||
| InterPro | IPR018569 | ||||||||
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In molecular biology, the protein domain, Saf pilin N-terminal extension refers to a domain only found in bacteria, more specifically, in gram-negative bacteria. Pili need to be formed by bacteria, as they are a method of adhering to the host organism which helps them infect the host cell. In other words, they are the bacteria's virulence factor. This particular protein domain helps the pili to form, via a complex mechanism named the chaperone/usher pathway. This protein domain is highly important for such bacteria, as without pili formation, they could not infect the host.
Contents |
[edit] Function
This protein domain, has an important function in forming pili. These are virulence factors crucial for cell adhesion to the host and biofilm formation which successful infection.[1]
[edit] Structure
This protein domain consists of the adjacent Saf-Nte and Saf-pilin chains of the pilus-forming complex. They are Chaperone/usher (CU) pili, and have an N-terminal extension (Nte) of around 10-20 amino acids. Salmonella Saf pili, which are assembled by FGl chaperones. The structure has been well conserved, as they contain a set of alternating hydrophobic residues that form an essential part of the subunitâsubunit interaction.[2]
[edit] Mechanism
The mechanism for the assembly reaction is termed donor strand exchange DSE which Pilus assembly in Gram-negative bacteria involves a Donor-strand exchange mechanism between the C- and the N-termini of this domain. The C-terminal subunit forms an incomplete Ig-fold which is then complemented by the 10-18 residue N terminus of another.
The N terminus sequences contain a motif of alternating hydrophobic residues that occupy the P2 to P5 binding pockets in the groove of the first pilus subunit.[3]
[edit] References
- ^ Salih O, Remaut H, Waksman G, Orlova EV (2008). "Structural analysis of the Saf pilus by electron microscopy and image processing.". J Mol Biol 379 (1): 174â87. doi:10.1016/j.jmb.2008.03.056. PMID 18448124. http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=18448124.
- ^ Waksman G, Hultgren SJ (2009). "Structural biology of the chaperone-usher pathway of pilus biogenesis.". Nat Rev Microbiol 7 (11): 765â74. doi:10.1038/nrmicro2220. PMID 19820722. http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=19820722.
- ^ Remaut H, Rose RJ, Hannan TJ, Hultgren SJ, Radford SE, Ashcroft AE, Waksman G (June 2006). "Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism". Mol. Cell 22 (6): 831â42. doi:10.1016/j.molcel.2006.05.033. PMID 16793551.
This article incorporates text from the public domain Pfam and InterPro IPR018569
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Saf-pilin pilus formation protein Provide feedback
This domain consists of the adjacent Saf-Nte and Saf-pilin chains of the pilus-forming complex. Pilus assembly in Gram-negative bacteria involves a Donor-strand exchange mechanism between the C- and the N-termini of this domain. The C-terminal subunit forms an incomplete Ig-fold which is then complemented by the 10-18 residue N-terminus of another, incoming, pilus subunit which is not involved in the Ig-fold. The N-terminus sequences contain a motif of alternating hydrophobic residues that occupy the P2 to P5 binding pockets in the groove of the first pilus subunit [1].
Literature references
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Remaut H, Rose RJ, Hannan TJ, Hultgren SJ, Radford SE, Ashcroft AE, Waksman G; , Mol Cell. 2006;22:831-842.: Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism. PUBMED:16793551 EPMC:16793551
External database links
| PANDIT: | PF09460 |
| Pseudofam: | PF09460 |
| SYSTERS: | Saf-Nte_pilin |
This tab holds annotation information from the InterPro database.
InterPro entry IPR018569
This domain consists of the adjacent Saf-Nte and Saf-pilin chains of the pilus-forming complex. Pilus assembly in Gram-negative bacteria involves a Donor-strand exchange mechanism between the C- and the N-termini of this domain. The C-terminal subunit forms an incomplete Ig-fold which is then complemented by the 10-18 residue N terminus of another, incoming, pilus subunit which is not involved in the Ig-fold. The N terminus sequences contain a motif of alternating hydrophobic residues that occupy the P2 to P5 binding pockets in the groove of the first pilus subunit [PUBMED:16793551].
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (4) |
Full (84) |
Representative proteomes | NCBI (51) |
Meta (0) |
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| RP15 (0) |
RP35 (0) |
RP55 (1) |
RP75 (1) |
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| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (4) |
Full (84) |
Representative proteomes | NCBI (51) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (0) |
RP35 (0) |
RP55 (1) |
RP75 (1) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | pdb_2co1 |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Coggill P |
| Number in seed: | 4 |
| Number in full: | 84 |
| Average length of the domain: | 138.30 aa |
| Average identity of full alignment: | 60 % |
| Average coverage of the sequence by the domain: | 90.19 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 145 | ||||||||||||
| Family (HMM) version: | 5 | ||||||||||||
| 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 Saf-Nte_pilin domain has been found. There are 19 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence