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PR01880

Identifier
FIBRITIN  [View Relations]  [View Alignment]  
Accession
PR01880
No. of Motifs
5
Creation Date
23-JUL-2004
Title
Fibritin signature
Database References

PDB; 1AA0; 1AVY
SCOP; 1AA0; 1AVY
CATH; 1AA0; 1AVY
Literature References
1. SOBOLEV, B.N. AND MESYANZHINOV, V.V.
The wac gene product of bacteriophage T4 contains coiled-coil
structural patterns.
J.BIOMOL.STRUCT.DYN. 8 953-965 (1991).
 
2. EFIMOV, V.P., NEPLUEV, I.V., SOBOLEV, B.N., ZURABISHVILI, T.G., 
SCHULTHESS, T., LUSTIG, A., ENGEL, J., HAENER, M., AEBI, U., 
VENYAMINOV, S.Y., POTEKHIN, S.A. AND MESYANZHINOV, V.V.
Fibritin encoded by bacteriophage T4 gene wac has a parallel triple- 
stranded alpha-helical coiled-coil structure.
J.MOL.BIOL. 242 470-486 (1994).
 
3. TAO, Y., STRELKOV, S.V., MESYANZHINOV, V.V. AND ROSSMANN, M.G.
Structure of bacteriophage T4 fibritin: a segmented coiled coil and the 
role of the C-terminal domain.
STRUCTURE 5 789-798 (1997).

Documentation
Fibritin is a chaperone that mediates a specific phage-assembly 
process, namely assembly of the long tail fibres and their subsequent
attachment to the tail baseplate; it is also a sensor that controls
the retraction of the long tail fibres in adverse environments,
thereby preventing infection [1-3]. The protein forms fibrous
structures on the neck of the virion, termed whiskers [1]. During
phage assembly, 6 fibritin molecules attach to each virion neck
via their N-terminal domains, forming a collar with 6 whiskers.
 
Sequence analysis of fibritin has indicated 10 alpha-helical domains
(19-40 residues in length) with coiled-coil structural patterns. These
domains comprise ~70% of the entire sequence [1], giving rise to a
structure that was predicted to be mainly a triple-helical coiled
coil [2].
 
The 3D structure of fibritin E, a wild-type deletion mutant, has been
determined to 2.2A resolution by means of X-ray crystallography [3].
Three identical 119-residue subunits form a trimeric parallel coiled-
coil domain and a small globular C-terminal domain: the coiled-coil
domain comprises three segments separated by loops; the C-terminal
domain, comprising 30 residues from each subunit, contains a beta-
propeller-like structure with a hydrophobic interior [3]. 
 
The C-terminal domain is important for correct fibritin assembly. It
is thought that the interplay between the stabilising effect of the
C-terminal domain and the labile coiled-coil domain may be essential
for the fibritin function, and indeed for the correct functioning of
many other alpha-fibrous proteins [3].
 
FIBRITIN is a 5-element fingerprint that provides a signature for
fibritin. The fingerprint was derived from an initial alignment of
4 sequences: the motifs were drawn from conserved regions spanning
the C-terminal quarter of the alignment - motif 1 includes helix 1;
motif 2 spans the N-terminus of helix 2; motifs 3 and 4 encompass
helix 4; and motif 5 includes strand 1. A single iteration on
SPTR41_24f was required to reach convergence, no further sequences
being identified beyond the starting set.
Summary Information
4 codes involving  5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
544444
400000
300000
200000
12345
True Positives
Q38405        Q38650        Q8JU37        WAC_BPT4      
Sequence Titles
Q38405      Fibritin - Bacteriophage K3.                  
Q38650 Fibritin - Bacteriophage Ox2, and Bacteriophage T2.
Q8JU37 Fibritin protein gpwac - Phage AR1.
WAC_BPT4 Fibritin (Whisker antigen control protein) (Collar protein) - Bacteriophage T4.
Scan History
SPTR41_24f 1  100  NSINGLE    
Initial Motifs
Motif 1  width=27
Element Seqn Id St Int Rpt
VSGLNNDVQNLQVEIGNNSTGIKGQVV Q38405 372 372 -
VSGLNNDVQNLQVEIGNNSAGIKGQVV Q38650 372 372 -
VSGLNNAVQNLQVEIGNNSAGIKGQVV WAC_BPT4 371 371 -
VNRLNNDVQNLQVEIGNNNSGIKGQVV Q8JU37 370 370 -

Motif 2 width=22
Element Seqn Id St Int Rpt
ALNTLVNGTNPNGSTVEERGLT Q38405 399 0 -
ALNTLVNGTNPNGSTVEERGLT Q38650 399 0 -
ALNTLVNGTNPNGSTVEERGLT WAC_BPT4 398 0 -
TLNKLVNGTNPNGSTVEERGLT Q8JU37 397 0 -

Motif 3 width=22
Element Seqn Id St Int Rpt
NSIKANETNIASVTQEVNTAKG Q38405 421 0 -
NSIKANETNIASVTQEVNTAKG Q38650 421 0 -
NSIKANETNIASVTQEVNTAKG WAC_BPT4 420 0 -
NSIKANETNISSINQEIRSTKG Q8JU37 419 0 -

Motif 4 width=20
Element Seqn Id St Int Rpt
NISSLQGDVQALQEAGYIPE Q38405 443 0 -
NISSLQSGVQALQEAGYIPE Q38650 443 0 -
NISSLQGDVQALQEAGYIPE WAC_BPT4 442 0 -
NVSSLQRDVQTLQEAGYIPE Q8JU37 441 0 -

Motif 5 width=22
Element Seqn Id St Int Rpt
APRDGQAYVRKDGEWVLLSTFL Q38405 463 0 -
APRDGQAYVRKDGEWVLLSTFL Q38650 463 0 -
APRDGQAYVRKDGEWVFLSTFL WAC_BPT4 462 0 -
APKDGQAYVRKDGEWVLLSTFL Q8JU37 461 0 -
Final Motifs
Motif 1  width=27
Element Seqn Id St Int Rpt
VSGLNNDVQNLQVEIGNNSTGIKGQVV Q38405 372 372 -
VSGLNNDVQNLQVEIGNNSAGIKGQVV Q38650 372 372 -
VSGLNNAVQNLQVEIGNNSAGIKGQVV WAC_BPT4 371 371 -
VNRLNNDVQNLQVEIGNNNSGIKGQVV Q8JU37 370 370 -

Motif 2 width=22
Element Seqn Id St Int Rpt
ALNTLVNGTNPNGSTVEERGLT Q38405 399 0 -
ALNTLVNGTNPNGSTVEERGLT Q38650 399 0 -
ALNTLVNGTNPNGSTVEERGLT WAC_BPT4 398 0 -
TLNKLVNGTNPNGSTVEERGLT Q8JU37 397 0 -

Motif 3 width=22
Element Seqn Id St Int Rpt
NSIKANETNIASVTQEVNTAKG Q38405 421 0 -
NSIKANETNIASVTQEVNTAKG Q38650 421 0 -
NSIKANETNIASVTQEVNTAKG WAC_BPT4 420 0 -
NSIKANETNISSINQEIRSTKG Q8JU37 419 0 -

Motif 4 width=20
Element Seqn Id St Int Rpt
NISSLQGDVQALQEAGYIPE Q38405 443 0 -
NISSLQSGVQALQEAGYIPE Q38650 443 0 -
NISSLQGDVQALQEAGYIPE WAC_BPT4 442 0 -
NVSSLQRDVQTLQEAGYIPE Q8JU37 441 0 -

Motif 5 width=22
Element Seqn Id St Int Rpt
APRDGQAYVRKDGEWVLLSTFL Q38405 463 0 -
APRDGQAYVRKDGEWVLLSTFL Q38650 463 0 -
APRDGQAYVRKDGEWVFLSTFL WAC_BPT4 462 0 -
APKDGQAYVRKDGEWVLLSTFL Q8JU37 461 0 -