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PROSITE documentation PDOC00342

Prokaryotic N-terminal methylation site

Description:

A number of bacteria express filamentous adhesins known as pili. The pili are polar flexible filaments of about 5.4 nm diameter and 2500 nm average length; they consist of a single polypeptide chain (called pilin or fimbrial protein) arranged in a helical configuration of five subunits per turn in the assembled pilus. Gram-negative bacteria produce pilin which are characterized by the presence of a very short leader peptide of 6 to 7 residues, followed by a methylated N-terminal phenylalanine residue and by a highly conserved sequence of about 24 hydrophobic residues. This class of pilin is often referred to as NMePhe or type-4 pili [1,2].

Recently a number of bacterial proteins have been sequenced which share the following structural characteristics with type-4 pili [3]:

 a) The N-terminal residue, which  is  methylated, is hydrophobic (generally a
    phenylalanine or a methionine);
 b) The leader peptide is hydrophilic, consists of 5 to  10 residues (with two
    exceptions, see below) and ends with a glycine;
 c) The fifth residue of the mature  sequence is a glutamate which seems to be
    required for the methylation step;
 d) The first twenty residues of the mature sequence are highly hydrophobic.

These proteins are listed below:

We developed a signature pattern based on the N-terminal conserved region of all these proteins.

Last update:

November 1995 / Text revised.

Technical section:

PROSITE method (with tools and information) covered by this documentation:

PROKAR_NTER_METHYL, PS00409Prokaryotic N-terminal methylation site  (PATTERN)
Consensus pattern: [KRHEQSTAG] - G - [FYLIVM] - [ST] - [LT] - [LIVP] - E - [LIVMFWSTAG](14)
The residue after the G is methylated
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
Retrieve the sequence logo from the alignment
Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00409
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00409
Scan Swiss-Prot/TrEMBL entries against PS00409
view ligand binding statistics

References:

1 AuthorsParanchych W., Frost L.S.
TitleThe physiology and biochemistry of pili.
SourceAdv. Microb. Physiol. 29:53-114(1988).
PubMed ID2898203
2 AuthorsDalrymple B., Mattick J.S.
TitleAn analysis of the organization and evolution of type 4 fimbrial (MePhe) subunit proteins.
SourceJ. Mol. Evol. 25:261-269(1987).
PubMed ID3118043
3 AuthorsHobbs M., Mattick J.S.
TitleCommon components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein complexes.
SourceMol. Microbiol. 10:233-243(1993).
PubMed ID7934814
4 AuthorsSalmond G.P.C., Reeves P.J.
TitleMembrane traffic wardens and protein secretion in gram-negative bacteria.
SourceTrends Biochem. Sci. 18:7-12(1993).
PubMed ID8438237

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