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P0C018 (RL18_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L18
Gene names
Name:rplR
Ordered Locus Names:b3304, JW3266
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length117 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. Ref.6

Subunit structure

Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs. Ref.9

Domain

The basic N-terminus is not necessary for binding to 5S rRNA. It is however required for cooperative binding of L5 and L18 to 5S rRNA as well as for binding of the 5S rRNA/L5/L18 complex to the 23S rRNA. HAMAP-Rule MF_01337_B

Post-translational modification

The protein has been shown to contain a phosphoserine, which was required for the protein to bind to 5S rRNA (Ref.11). However, the presence of this phosphoserine is controversial, and it has not been seen by mass spectrometry. HAMAP-Rule MF_01337_B

Sequence similarities

Belongs to the ribosomal protein L18P family.

Mass spectrometry

Molecular mass is 12769.8 Da from positions 1 - 117. Determined by MALDI. Ref.12

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11711750S ribosomal protein L18 HAMAP-Rule MF_01337_B
PRO_0000131258

Regions

Region1 – 1717Required for binding of the 5S rRNA/L5/L18 complex to the 23S rRNA HAMAP-Rule MF_01337_B

Secondary structure

....................... 117
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C018 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: CA1082FF9B5D9697

FASTA11712,770
        10         20         30         40         50         60 
MDKKSARIRR ATRARRKLQE LGATRLVVHR TPRHIYAQVI APNGSEVLVA ASTVEKAIAE 

        70         80         90        100        110 
QLKYTGNKDA AAAVGKAVAE RALEKGIKDV SFDRSGFQYH GRVQALADAA REAGLQF 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of the 5S RNA binding protein L18 from Escherichia coli ribosomes."
Brosius J., Schiltz E., Chen R.
FEBS Lett. 56:359-361(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: K.
[2]"The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Stoichiometry, cooperativity, and stability of interactions between 5S RNA and proteins L5, L18, and L25 from the 50S ribosomal subunit of Escherichia coli."
Spierer P., Zimmermann R.A.
Biochemistry 17:2474-2479(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: FORMATION OF THE 5S RRNA/L5/L18/L25 SUBCOMPLEX.
[6]"Fragment of protein L18 from the Escherichia coli ribosome that contains the 5S RNA binding site."
Newberry V., Brosius J., Garrett R.
Nucleic Acids Res. 5:1753-1766(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE BASIC N-TERMINUS.
[7]"Cooperative interactions among protein and RNA components of the 50S ribosomal subunit of Escherichia coli."
Spierer P., Wang C.-C., Marsh T.L., Zimmermann R.A.
Nucleic Acids Res. 6:1669-1682(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION OF 5S RRNA/L5/L18 WITH 23S RRNA.
Strain: MRE-600.
[8]"The role of the basic N-terminal region of protein L18 in 5S RNA-23S RNA complex formation."
Newberry V., Garrett R.A.
Nucleic Acids Res. 8:4131-4142(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: REQUIREMENT OF N-TERMINUS FOR FORMATION OF 5S RRNA-23S RRNA COMPLEX.
Strain: MRE-600.
[9]"Assembly map of the large subunit (50S) of Escherichia coli ribosomes."
Rohl R., Nierhaus K.H.
Proc. Natl. Acad. Sci. U.S.A. 79:729-733(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: REQUIREMENT FOR INCORPORATION OF 5S RRNA INTO THE 50S SUBUNIT.
Strain: MRE-600.
[10]"5S rRNA sugar-phosphate backbone protection in complexes with specific ribosomal proteins."
Shpanchenko O.V., Zvereva M.I., Dontsova O.A., Nierhaus K.H., Bogdanov A.A.
FEBS Lett. 394:71-75(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF A 5S RRNA/L5/L18/L25 SUBCOMPLEX.
Strain: K12 / A19.
[11]"Phosphorylation of ribosomal protein L18 is required for its folding and binding to 5S rRNA."
Bloemink M.J., Moore P.B.
Biochemistry 38:13385-13390(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[12]"Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
Arnold R.J., Reilly J.P.
Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[13]"Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
Strain: MRE-600.
[14]"Structures of the bacterial ribosome at 3.5 A resolution."
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.
Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01563 Genomic DNA. Translation: CAA25721.1.
U18997 Genomic DNA. Translation: AAA58101.1.
U00096 Genomic DNA. Translation: AAC76329.1.
AP009048 Genomic DNA. Translation: BAE77987.1.
PIRR5EC18. A02803.
RefSeqNP_417763.1. NC_000913.3.
YP_492128.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00q2-117[»]
1P85electron microscopy12.30M1-117[»]
1P86electron microscopy11.50M1-117[»]
1VS6X-ray3.46O1-117[»]
1VS8X-ray3.46O1-117[»]
1VT2X-ray3.30O1-117[»]
2AW4X-ray3.46O1-117[»]
2AWBX-ray3.46O1-117[»]
2GYAelectron microscopy15.00M3-115[»]
2GYCelectron microscopy15.00M3-115[»]
2I2TX-ray3.22O1-117[»]
2I2VX-ray3.22O1-117[»]
2J28electron microscopy8.00O1-117[»]
2QAMX-ray3.21O1-117[»]
2QAOX-ray3.21O1-117[»]
2QBAX-ray3.54O1-117[»]
2QBCX-ray3.54O1-117[»]
2QBEX-ray3.30O1-117[»]
2QBGX-ray3.30O1-117[»]
2QBIX-ray4.00O1-117[»]
2QBKX-ray4.00O1-117[»]
2QOVX-ray3.93O1-117[»]
2QOXX-ray3.93O1-117[»]
2QOZX-ray3.50O1-117[»]
2QP1X-ray3.50O1-117[»]
2RDOelectron microscopy9.10O1-117[»]
2VHMX-ray3.74O1-117[»]
2VHNX-ray3.74O1-117[»]
2WWQelectron microscopy5.80O2-117[»]
2Z4LX-ray4.45O1-117[»]
2Z4NX-ray4.45O1-117[»]
3BBXelectron microscopy10.00O1-117[»]
3DF2X-ray3.50O1-117[»]
3DF4X-ray3.50O1-117[»]
3E1Belectron microscopy-H1-117[»]
3E1Delectron microscopy-H1-117[»]
3FIKelectron microscopy6.70O2-117[»]
3I1NX-ray3.19O1-117[»]
3I1PX-ray3.19O1-117[»]
3I1RX-ray3.81O1-117[»]
3I1TX-ray3.81O1-117[»]
3I20X-ray3.71O1-117[»]
3I22X-ray3.71O1-117[»]
3IZTelectron microscopy-P1-117[»]
3IZUelectron microscopy-P1-117[»]
3J01electron microscopy-O1-117[»]
3J0Telectron microscopy12.10Q1-117[»]
3J0Welectron microscopy14.70Q1-117[»]
3J0Yelectron microscopy13.50Q1-117[»]
3J11electron microscopy13.10Q1-117[»]
3J12electron microscopy11.50Q1-117[»]
3J14electron microscopy11.50Q1-117[»]
3J19electron microscopy8.30O2-117[»]
3J37electron microscopy9.80S1-117[»]
3J4Xelectron microscopy12.00O1-117[»]
3J50electron microscopy20.00O1-117[»]
3J51electron microscopy17.00O1-117[»]
3J52electron microscopy12.00O1-117[»]
3J54electron microscopy13.00O1-117[»]
3J56electron microscopy15.00O1-117[»]
3J58electron microscopy17.00O1-117[»]
3J5Aelectron microscopy12.00O1-117[»]
3J5Celectron microscopy17.00O1-117[»]
3J5Eelectron microscopy17.00O1-117[»]
3J5Gelectron microscopy20.00O1-117[»]
3J5Ielectron microscopy15.00O1-117[»]
3J5Kelectron microscopy9.00O1-117[»]
3J5Lelectron microscopy6.60O2-117[»]
3J5Oelectron microscopy6.80O1-117[»]
3J5Uelectron microscopy7.60Q1-117[»]
3J5Welectron microscopy7.60R1-117[»]
3KCRelectron microscopy-O1-117[»]
3OASX-ray3.25O2-117[»]
3OATX-ray3.25O2-117[»]
3OFCX-ray3.19O2-117[»]
3OFDX-ray3.19O2-117[»]
3OFQX-ray3.10O2-117[»]
3OFRX-ray3.10O2-117[»]
3OFZX-ray3.29O2-117[»]
3OG0X-ray3.29O2-117[»]
3ORBX-ray3.30O1-117[»]
3R8SX-ray3.00O2-117[»]
3R8TX-ray3.00O2-117[»]
3SGFX-ray3.20S1-117[»]
3UOSX-ray3.70S1-117[»]
4GARX-ray3.30O1-117[»]
4GAUX-ray3.30O1-117[»]
4KIXX-ray2.90O1-117[»]
4KIZX-ray2.90O1-117[»]
4KJ1X-ray2.90O1-117[»]
4KJ3X-ray2.90O1-117[»]
4KJ5X-ray2.90O1-117[»]
4KJ7X-ray2.90O1-117[»]
4KJ9X-ray2.90O1-117[»]
4KJBX-ray2.90O1-117[»]
ProteinModelPortalP0C018.
SMRP0C018. Positions 2-117.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47908N.
IntActP0C018. 35 interactions.
MINTMINT-1293631.
STRING511145.b3304.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0C018.
PRIDEP0C018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76329; AAC76329; b3304.
BAE77987; BAE77987; BAE77987.
GeneID12934402.
947804.
KEGGecj:Y75_p3872.
eco:b3304.
PATRIC32122040. VBIEscCol129921_3397.

Organism-specific databases

EchoBASEEB0872.
EcoGeneEG10879. rplR.

Phylogenomic databases

eggNOGCOG0256.
HOGENOMHOG000248742.
KOK02881.
OMAIDDEKGH.
OrthoDBEOG64NB48.
PhylomeDBP0C018.

Enzyme and pathway databases

BioCycEcoCyc:EG10879-MONOMER.
ECOL316407:JW3266-MONOMER.

Gene expression databases

GenevestigatorP0C018.

Family and domain databases

HAMAPMF_01337_B. Ribosomal_L18_B.
InterProIPR005484. Ribosomal_L18/L5.
IPR004389. Ribosomal_L18_bac-type.
[Graphical view]
PfamPF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
TIGRFAMsTIGR00060. L18_bact. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0C018.
PROP0C018.

Entry information

Entry nameRL18_ECOLI
AccessionPrimary (citable) accession number: P0C018
Secondary accession number(s): P02419, Q2M6W9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene