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P0ADY7 (RL16_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. 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 L16
Gene names
Name:rplP
Ordered Locus Names:b3313, JW3275
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood. HAMAP-Rule MF_01342

Subunit structure

Part of the 50S ribosomal subunit. Cross-links to the A and P site tRNAs. Ref.6

Post-translational modification

Is hydroxylated on Arg-81 by YcfD. The modification is nearly suppressed when E.coli is grown in anoxia. HAMAP-Rule MF_01342

Sequence similarities

Belongs to the ribosomal protein L16P family.

Mass spectrometry

Molecular mass is 15326.2 Da from positions 1 - 136. Determined by MALDI. Ref.8

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13613650S ribosomal protein L16 HAMAP-Rule MF_01342
PRO_0000062101

Amino acid modifications

Modified residue11N-methylmethionine HAMAP-Rule MF_01342
Modified residue811(3R)-3-hydroxyarginine HAMAP-Rule MF_01342

Secondary structure

.......................... 136
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ADY7 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 445A9B167F7564D1

FASTA13615,281
        10         20         30         40         50         60 
MLQPKRTKFR KMHKGRNRGL AQGTDVSFGS FGLKAVGRGR LTARQIEAAR RAMTRAVKRQ 

        70         80         90        100        110        120 
GKIWIRVFPD KPITEKPLAV RMGKGKGNVE YWVALIQPGK VLYEMDGVPE ELAREAFKLA 

       130 
AAKLPIKTTF VTKTVM 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of protein L16 located at the peptidyltransferase center of Escherichia coli ribosomes."
Brosius J., Chen R.
FEBS Lett. 68:105-109(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: K.
[2]"Structure of the Escherichia coli S10 ribosomal protein operon."
Zurawski G., Zurawski S.M.
Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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]"DNA sequence of the promoter region for the alpha ribosomal protein operon in Escherichia coli."
Post L.E., Arfsten A.E., Davis G.R., Nomura M.
J. Biol. Chem. 255:4653-4659(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-80.
[6]"Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
Herold M., Nierhaus K.H.
J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
Strain: K12.
[7]"The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
Osswald M., Doering T., Brimacombe R.
Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
Strain: MRE-600.
[8]"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.
[9]"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.
[10]"Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans."
Ge W., Wolf A., Feng T., Ho C.H., Sekirnik R., Zayer A., Granatino N., Cockman M.E., Loenarz C., Loik N.D., Hardy A.P., Claridge T.D., Hamed R.B., Chowdhury R., Gong L., Robinson C.V., Trudgian D.C., Jiang M. expand/collapse author list , Mackeen M.M., McCullagh J.S., Gordiyenko Y., Thalhammer A., Yamamoto A., Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M., Kessler B.M., Ratcliffe P.J., Preston G.M., Coleman M.L., Schofield C.J.
Nat. Chem. Biol. 8:960-962(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: HYDROXYLATION AT ARG-81 BY YCFD.
Strain: K12.
[11]"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
X02613 Genomic DNA. Translation: CAA26467.1.
U18997 Genomic DNA. Translation: AAA58110.1.
U00096 Genomic DNA. Translation: AAC76338.1.
AP009048 Genomic DNA. Translation: BAE77978.1.
M12490 Genomic DNA. Translation: AAA83901.1.
PIRR5EC16. I23129.
RefSeqNP_417772.1. NC_000913.3.
YP_492119.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30K1-136[»]
1P86electron microscopy11.50K1-136[»]
1VS6X-ray3.46M1-136[»]
1VS8X-ray3.46M1-136[»]
1VT2X-ray3.30M1-136[»]
2AW4X-ray3.46M1-136[»]
2AWBX-ray3.46M1-136[»]
2GYAelectron microscopy15.00K3-133[»]
2GYCelectron microscopy15.00K3-133[»]
2I2TX-ray3.22M1-136[»]
2I2VX-ray3.22M1-136[»]
2J28electron microscopy8.00M1-136[»]
2QAMX-ray3.21M1-136[»]
2QAOX-ray3.21M1-136[»]
2QBAX-ray3.54M1-136[»]
2QBCX-ray3.54M1-136[»]
2QBEX-ray3.30M1-136[»]
2QBGX-ray3.30M1-136[»]
2QBIX-ray4.00M1-136[»]
2QBKX-ray4.00M1-136[»]
2QOVX-ray3.93M1-136[»]
2QOXX-ray3.93M1-136[»]
2QOZX-ray3.50M1-136[»]
2QP1X-ray3.50M1-136[»]
2RDOelectron microscopy9.10M1-136[»]
2VHMX-ray3.74M1-136[»]
2VHNX-ray3.74M1-136[»]
2WWQelectron microscopy5.80M1-136[»]
2Z4LX-ray4.45M1-136[»]
2Z4NX-ray4.45M1-136[»]
3BBXelectron microscopy10.00M1-136[»]
3E1Belectron microscopy-F1-136[»]
3E1Delectron microscopy-F1-136[»]
3FIKelectron microscopy6.70M1-136[»]
3I1NX-ray3.19M1-136[»]
3I1PX-ray3.19M1-136[»]
3I1RX-ray3.81M1-136[»]
3I1TX-ray3.81M1-136[»]
3I20X-ray3.71M1-136[»]
3I22X-ray3.71M1-136[»]
3IZTelectron microscopy-N1-136[»]
3IZUelectron microscopy-N1-136[»]
3J01electron microscopy-M1-136[»]
3J0Telectron microscopy12.10O1-136[»]
3J0Welectron microscopy14.70O1-136[»]
3J0Yelectron microscopy13.50O1-136[»]
3J11electron microscopy13.10O1-136[»]
3J12electron microscopy11.50O1-136[»]
3J14electron microscopy11.50O1-136[»]
3J19electron microscopy8.30M1-136[»]
3J37electron microscopy9.80Q1-136[»]
3J4Xelectron microscopy12.00M1-136[»]
3J50electron microscopy20.00M1-136[»]
3J51electron microscopy17.00M1-136[»]
3J52electron microscopy12.00M1-136[»]
3J54electron microscopy13.00M1-136[»]
3J56electron microscopy15.00M1-136[»]
3J58electron microscopy17.00M1-136[»]
3J5Aelectron microscopy12.00M1-136[»]
3J5Celectron microscopy17.00M1-136[»]
3J5Eelectron microscopy17.00M1-136[»]
3J5Gelectron microscopy20.00M1-136[»]
3J5Ielectron microscopy15.00M1-136[»]
3J5Kelectron microscopy9.00M1-136[»]
3J5Lelectron microscopy6.60M1-136[»]
3J5Oelectron microscopy6.80M1-136[»]
3J5Uelectron microscopy7.60O1-136[»]
3J5Welectron microscopy7.60P1-136[»]
3KCRelectron microscopy-M1-136[»]
3OASX-ray3.25M1-136[»]
3OATX-ray3.25M1-136[»]
3OFCX-ray3.19M1-136[»]
3OFDX-ray3.19M1-136[»]
3OFQX-ray3.10M1-136[»]
3OFRX-ray3.10M1-136[»]
3OFZX-ray3.29M1-136[»]
3OG0X-ray3.29M1-136[»]
3ORBX-ray3.30M1-136[»]
3R8SX-ray3.00M1-136[»]
3R8TX-ray3.00M1-136[»]
3SGFX-ray3.20Q1-136[»]
3UOSX-ray3.70Q1-136[»]
4GARX-ray3.30M1-136[»]
4GAUX-ray3.30M1-136[»]
4KIXX-ray2.90M1-136[»]
4KIZX-ray2.90M1-136[»]
4KJ1X-ray2.90M1-136[»]
4KJ3X-ray2.90M1-136[»]
4KJ5X-ray2.90M1-136[»]
4KJ7X-ray2.90M1-136[»]
4KJ9X-ray2.90M1-136[»]
4KJBX-ray2.90M1-136[»]
ProteinModelPortalP0ADY7.
SMRP0ADY7. Positions 1-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35976N.
IntActP0ADY7. 34 interactions.
MINTMINT-1302401.
STRING511145.b3313.

Chemistry

ChEMBLCHEMBL2363135.

PTM databases

PhosSiteP0810431.

Proteomic databases

PaxDbP0ADY7.
PRIDEP0ADY7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76338; AAC76338; b3313.
BAE77978; BAE77978; BAE77978.
GeneID12934115.
947806.
KEGGecj:Y75_p3863.
eco:b3313.
PATRIC32122058. VBIEscCol129921_3406.

Organism-specific databases

EchoBASEEB0870.
EcoGeneEG10877. rplP.

Phylogenomic databases

eggNOGCOG0197.
HOGENOMHOG000164573.
KOK02878.
OMALKTTFVT.
OrthoDBEOG6WHNWS.
PhylomeDBP0ADY7.

Enzyme and pathway databases

BioCycEcoCyc:EG10877-MONOMER.
ECOL316407:JW3275-MONOMER.

Gene expression databases

GenevestigatorP0ADY7.

Family and domain databases

Gene3D3.90.1170.10. 1 hit.
HAMAPMF_01342. Ribosomal_L16.
InterProIPR016180. Ribosomal_L10e/L16.
IPR000114. Ribosomal_L16.
IPR020798. Ribosomal_L16_CS.
[Graphical view]
PANTHERPTHR12220. PTHR12220. 1 hit.
PfamPF00252. Ribosomal_L16. 1 hit.
[Graphical view]
PRINTSPR00060. RIBOSOMALL16.
SUPFAMSSF54686. SSF54686. 1 hit.
TIGRFAMsTIGR01164. rplP_bact. 1 hit.
PROSITEPS00586. RIBOSOMAL_L16_1. 1 hit.
PS00701. RIBOSOMAL_L16_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ADY7.
PROP0ADY7.

Entry information

Entry nameRL16_ECOLI
AccessionPrimary (citable) accession number: P0ADY7
Secondary accession number(s): P02414, Q2M6X8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 89 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