PROSITE documentation PDOC00055

Ribosomal protein S17 signature

Description:

Ribosomal protein S17 is one of the proteins from the small ribosomal subunit. In Escherichia coli, S17 is known to bind specifically to the 5' end of 16S ribosomal RNA and is thought to be involved in the recognition of termination codons. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities [1,2,3], groups:

  • Eubacterial S17.
  • Plant chloroplast S17 (nuclear encoded).
  • Red algal chloroplast S17.
  • Cyanelle S17.
  • Archaebacterial S17.
  • Mammalian and plant cytoplasmic S11.
  • Yeast S18a and S18b (RP41; YS12).

As a signature pattern, we selected the best conserved regions located in the C-terminal section of these proteins.

Last update:

November 1997 / Pattern and text revised.

Technical section:

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

RIBOSOMAL_S17, PS00056Ribosomal protein S17 signature  (PATTERN)
Consensus pattern: G-D-x-[LIV]-x-[LIVA]-x-[QEK]-x-[RK]-P-[LIV]-S
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 PS00056
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00056
Scan Swiss-Prot/TrEMBL entries against PS00056
view ligand binding statistics
Matching PDB structures: 1EG0 1FJG 1GIX 1HNW ... [ALL]

References:

1 AuthorsGantt J.S., Thompson M.D.
TitlePlant cytosolic ribosomal protein S11 and chloroplast ribosomal protein CS17. Their primary structures and evolutionary relationships.
SourceJ. Biol. Chem. 265:2763-2767(1990).
PubMed ID2406240
2 AuthorsHerfurth E., Hirano H., Wittmann-Liebold B.
TitleThe amino-acid sequences of the Bacillus stearothermophilus ribosomal proteins S17 and S21 and their comparison to homologous proteins of other ribosomes.
SourceBiol. Chem. Hoppe-Seyler 372:955-961(1991).
PubMed ID1772592
3 AuthorsOtaka E., Hashimoto T., Mizuta K.
SourceProtein Seq. Data Anal. 5:285-300(1993).

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