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PR01006

Identifier
FLGHOOKFLIE  [View Relations]  [View Alignment]  
Accession
PR01006
No. of Motifs
3
Creation Date
27-NOV-1998  (UPDATE 15-JUN-1999)
Title
Flagellar hook-basal body complex protein FliE signature
Database References

INTERPRO; IPR001624
Literature References
1. ZUBERI A.R., YING C., BISCHOFF D.S. AND ORDAL G.W.
Gene-protein relationships in the flagellar hook-basal body complex of 
Bacillus subtilis: sequences of the flgB, flgC, flgG, fliE and fliF genes.
GENE 101 23-31 (1991).
 
2. MULLER, V., JONES, C.J., KAWAGISHI, I., AIZAWA, S. AND MACNAB, R.M.
Characterization of the fliE genes of Escherichia coli and Salmonella
typhimurium and identification of the FliE protein as a component of the
flagellar hook-basal body complex.
J.BACTERIOL. 174 2298-2304 (1992).

Documentation
Four genes from the major B.subtilis chemotaxis locus have been shown to
encode proteins that are similar to the S.typhimurium FlgB, FlgC, FlgG and 
FliF proteins; a further gene product is similar to the E.coli FliE protein
[1]. All of these proteins are thought to form part of the hook-basal body
complex of the bacterial flagella [1]. The FlgB, FlgC and FlgG proteins are
components of the proximal and distal rods; FliF forms the M-ring that
anchors the rod assembly to the membrane; but the role of FliE has not yet
been determined [1]. The similarity between the proteins in these two 
organisms suggests that the structures of the M-ring and the rod may be
similar [1]. Nevertheless, some differences in size and amino acid 
composition between some of the homologues suggest the basal body proteins
may be organised slightly differently within B.subtilis [1]. 
 
From gel electrophoresis and autoradiography of 35S-labelled S.typhimurium
hook-basal body complexes and the deduced number of sulphur-containing
residues in FliE, the stoichiometry of the protein in the hook-basal body
complex has been estimated to be about nine subunits [2]. FliE does not 
undergo cleavage of a signal peptide, nor does it show any similarity to
the axial components like the rod or hook proteins, which are thought to be
exported by the flagellum-specific export pathway [2]. On this evidence, 
it has been suggested that FliE may be in the vicinity of the MS ring,
perhaps acting as an adaptor protein between ring and rod substructures [2].
 
FLGHOOKFLIE is a 3-element fingerprint that provides a fingerprint for
flagellar hook protein FliE. The fingerprint was derived from an initial
alignment of 5 sequences: the motifs were drawn from short conserved
regions spanning virtually the full alignment length. Two iterations on
OWL30.2 were required to reach convergence, at which point a true set
comprising 6 sequences was identified. Two partial matches were also 
found, both of which fail to make a significant match with one motif:
RSFLIEGEN is a FliE protein from Rhodobacter sphaeroides; and E64714 
is a flagellar basal-body protein from Helicobacter pylori.
 
An update on SPTR37_9f identified a true set of 8 sequences.
Summary Information
8 codes involving  3 elements
0 codes involving 2 elements
Composite Feature Index
3888
2000
123
True Positives
FLIE_BACSU    FLIE_BORBU    FLIE_ECOLI    FLIE_PSEAE    
FLIE_SALTY O26079 O67242 P95713
Sequence Titles
FLIE_BACSU  FLAGELLAR HOOK-BASAL BODY COMPLEX PROTEIN FLIE - BACILLUS SUBTILIS. 
FLIE_BORBU FLAGELLAR HOOK-BASAL BODY COMPLEX PROTEIN FLIE - BORRELIA BURGDORFERI (LYME DISEASE SPIROCHETE).
FLIE_ECOLI FLAGELLAR HOOK-BASAL BODY COMPLEX PROTEIN FLIE - ESCHERICHIA COLI.
FLIE_PSEAE FLAGELLAR HOOK-BASAL BODY COMPLEX PROTEIN FLIE - PSEUDOMONAS AERUGINOSA.
FLIE_SALTY FLAGELLAR HOOK-BASAL BODY COMPLEX PROTEIN FLIE - SALMONELLA TYPHIMURIUM.
O26079 FLAGELLAR BASAL-BODY PROTEIN (FLIE) - HELICOBACTER PYLORI (CAMPYLOBACTER PYLORI), AND HELICOBACTER PYLORI J99.
O67242 FLAGELLAR HOOK-BASAL BODY PROTEIN - AQUIFEX AEOLICUS.
P95713 FLAGELLAR HOOK-BASAL BODY COMPLEX PROTEIN FLIE - SHIGELLA BOYDII.
Scan History
OWL30_2    2  300  NSINGLE    
SPTR37_9f 2 200 NSINGLE
Initial Motifs
Motif 1  width=17
Element Seqn Id St Int Rpt
SFAGQLHAALDRISDTQ FLIE_ECOLI 32 32 -
SFAGQLHAALDRISDRQ FLIE_SALTY 32 32 -
SFSEMLSQAVDKVNETQ FLIE_PSEAE 38 38 -
SFSELLKNSISSLNESQ FLIE_BACSU 36 36 -
TFKDVLINSITDVNKSQ FLIE_BORBU 40 40 -

Motif 2 width=17
Element Seqn Id St Int Rpt
LNDVMTDMQKASVSMQM FLIE_ECOLI 67 18 -
LNDVMADMQKASVSMQM FLIE_SALTY 67 18 -
LTDVMIASQKASVSFQA FLIE_PSEAE 73 18 -
LDEVMIAAQKASISLTA FLIE_BACSU 70 17 -
VHDVVIAMSKANMNLSI FLIE_BORBU 75 18 -

Motif 3 width=14
Element Seqn Id St Int Rpt
RNKLVAAYQEVMSM FLIE_ECOLI 88 4 -
RNKLVAAYQEVMSM FLIE_SALTY 88 4 -
RNKLVQAYQDIMQM FLIE_PSEAE 94 4 -
RNKAVEAYQEIMRM FLIE_BACSU 91 4 -
VERGVKAYQDIINI FLIE_BORBU 96 4 -
Final Motifs
Motif 1  width=17
Element Seqn Id St Int Rpt
SFAGQLHAALDRISDTQ FLIE_ECOLI 32 32 -
SFAGQLHAALDRISDTQ P95713 32 32 -
SFAGQLHAALDRISDRQ FLIE_SALTY 32 32 -
SFSEMLSQAVDKVNETQ FLIE_PSEAE 38 38 -
SFSELLKNSISSLNESQ FLIE_BACSU 36 36 -
TFKDVLINSITDVNKSQ FLIE_BORBU 40 40 -
EFSKLLKQSINELNNTQ O26079 39 39 -
DIVENFVNFVEWVNEKQ O67242 23 23 -

Motif 2 width=17
Element Seqn Id St Int Rpt
LNDVMTDMQKASVSMQM FLIE_ECOLI 67 18 -
LNDVMTDMQKASVSMQM P95713 67 18 -
LNDVMADMQKASVSMQM FLIE_SALTY 67 18 -
LTDVMIASQKASVSFQA FLIE_PSEAE 73 18 -
LDEVMIAAQKASISLTA FLIE_BACSU 70 17 -
VHDVVIAMSKANMNLSI FLIE_BORBU 75 18 -
LHQAAIAIGKAETSMKL O26079 73 17 -
LHEIVIEAEKAKVALNL O67242 57 17 -

Motif 3 width=14
Element Seqn Id St Int Rpt
RNKLVAAYQEVMSM FLIE_ECOLI 88 4 -
RNKLVAAYQEVMSM P95713 88 4 -
RNKLVAAYQEVMSM FLIE_SALTY 88 4 -
RNKLVQAYQDIMQM FLIE_PSEAE 94 4 -
RNKAVEAYQEIMRM FLIE_BACSU 91 4 -
VERGVKAYQDIINI FLIE_BORBU 96 4 -
RNKAISAYKELLRT O26079 94 4 -
RNKLLEAYNELMKM O67242 78 4 -