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Protein

50S ribosomal protein L16

Gene

rplP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. rRNA binding Source: EcoCyc
  2. structural constituent of ribosome Source: GO_Central
  3. tRNA binding Source: EcoCyc

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10877-MONOMER.
ECOL316407:JW3275-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L16
Gene namesi
Name:rplP
Ordered Locus Names:b3313, JW3275
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10877. rplP.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Chemistry

DrugBankiDB00446. Chloramphenicol.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13613650S ribosomal protein L16PRO_0000062101Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-methylmethionine1 Publication
Modified residuei81 – 811(3R)-3-hydroxyarginine1 Publication

Post-translational modificationi

Is hydroxylated on Arg-81 by RoxA. The modification is nearly suppressed when E.coli is grown in anoxia.1 Publication

Keywords - PTMi

Hydroxylation, Methylation

Proteomic databases

PaxDbiP0ADY7.
PRIDEiP0ADY7.

Expressioni

Gene expression databases

GenevestigatoriP0ADY7.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-35976N.
IntActiP0ADY7. 34 interactions.
MINTiMINT-1302401.
STRINGi511145.b3313.

Structurei

Secondary structure

1
136
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Beta strandi28 – 358Combined sources
Beta strandi39 – 424Combined sources
Helixi43 – 5715Combined sources
Beta strandi61 – 655Combined sources
Beta strandi71 – 755Combined sources
Beta strandi82 – 854Combined sources
Beta strandi88 – 969Combined sources
Beta strandi101 – 1088Combined sources
Helixi110 – 12112Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1325Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00M1-136[»]
2RDOelectron microscopy9.10M1-136[»]
3BBXelectron microscopy10.00M1-136[»]
3J5Lelectron microscopy6.60M1-136[»]
3J7Zelectron microscopy3.90M1-136[»]
4CSUelectron microscopy5.50M1-136[»]
4U1UX-ray2.95BM/DM1-136[»]
4U1VX-ray3.00BM/DM1-136[»]
4U20X-ray2.90BM/DM1-136[»]
4U24X-ray2.90BM/DM1-136[»]
4U25X-ray2.90BM/DM1-136[»]
4U26X-ray2.80BM/DM1-136[»]
4U27X-ray2.80BM/DM1-136[»]
4V47electron microscopy12.30AK1-136[»]
4V48electron microscopy11.50AK1-136[»]
4V4HX-ray3.46BM/DM1-136[»]
4V4QX-ray3.46BM/DM1-136[»]
4V4Velectron microscopy15.00BK3-133[»]
4V4Welectron microscopy15.00BK3-133[»]
4V50X-ray3.22BM/DM1-136[»]
4V52X-ray3.21BM/DM1-136[»]
4V53X-ray3.54BM/DM1-136[»]
4V54X-ray3.30BM/DM1-136[»]
4V55X-ray4.00BM/DM1-136[»]
4V56X-ray3.93BM/DM1-136[»]
4V57X-ray3.50BM/DM1-136[»]
4V5BX-ray3.74AM/CM1-136[»]
4V5Helectron microscopy5.80BM1-136[»]
4V5YX-ray4.45BM/DM1-136[»]
4V64X-ray3.50BM/DM1-136[»]
4V65electron microscopy9.00BF1-136[»]
4V66electron microscopy9.00BF1-136[»]
4V69electron microscopy6.70BM1-136[»]
4V6CX-ray3.19BM/DM1-136[»]
4V6DX-ray3.81BM/DM1-136[»]
4V6EX-ray3.71BM/DM1-136[»]
4V6Kelectron microscopy8.25AN1-136[»]
4V6Lelectron microscopy13.20BN1-136[»]
4V6Melectron microscopy7.10BM1-136[»]
4V6Nelectron microscopy12.10AO1-136[»]
4V6Oelectron microscopy14.70BO1-136[»]
4V6Pelectron microscopy13.50BO1-136[»]
4V6Qelectron microscopy11.50BO1-136[»]
4V6Relectron microscopy11.50BO1-136[»]
4V6Selectron microscopy13.10AO1-136[»]
4V6Telectron microscopy8.30BM1-136[»]
4V6Velectron microscopy9.80BQ1-136[»]
4V6Yelectron microscopy12.00BM1-136[»]
4V6Zelectron microscopy12.00BM1-136[»]
4V70electron microscopy17.00BM1-136[»]
4V71electron microscopy20.00BM1-136[»]
4V72electron microscopy13.00BM1-136[»]
4V73electron microscopy15.00BM1-136[»]
4V74electron microscopy17.00BM1-136[»]
4V75electron microscopy12.00BM1-136[»]
4V76electron microscopy17.00BM1-136[»]
4V77electron microscopy17.00BM1-136[»]
4V78electron microscopy20.00BM1-136[»]
4V79electron microscopy15.00BM1-136[»]
4V7Aelectron microscopy9.00BM1-136[»]
4V7Belectron microscopy6.80BM1-136[»]
4V7Celectron microscopy7.60BO1-136[»]
4V7Delectron microscopy7.60AP1-136[»]
4V7Ielectron microscopy9.60AM1-136[»]
4V7SX-ray3.25BM/DM1-136[»]
4V7TX-ray3.19BM/DM1-136[»]
4V7UX-ray3.10BM/DM1-136[»]
4V7VX-ray3.29BM/DM1-136[»]
4V85X-ray3.20Q1-136[»]
4V89X-ray3.70BQ1-136[»]
4V9CX-ray3.30BM/DM1-136[»]
4V9DX-ray3.00CM/DM1-136[»]
4V9OX-ray2.90AM/CM/EM/GM1-136[»]
4V9PX-ray2.90AM/CM/EM/GM1-136[»]
4WF1X-ray3.09BM/DM1-136[»]
4WWWX-ray3.10RM/YM1-136[»]
5AFIelectron microscopy2.90M1-136[»]
ProteinModelPortaliP0ADY7.
SMRiP0ADY7. Positions 1-136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADY7.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L16P family.Curated

Phylogenomic databases

eggNOGiCOG0197.
HOGENOMiHOG000164573.
InParanoidiP0ADY7.
KOiK02878.
OMAiPVKTKFI.
OrthoDBiEOG6WHNWS.
PhylomeDBiP0ADY7.

Family and domain databases

Gene3Di3.90.1170.10. 1 hit.
HAMAPiMF_01342. Ribosomal_L16.
InterProiIPR016180. Ribosomal_L10e/L16.
IPR000114. Ribosomal_L16.
IPR020798. Ribosomal_L16_CS.
[Graphical view]
PANTHERiPTHR12220. PTHR12220. 1 hit.
PfamiPF00252. Ribosomal_L16. 1 hit.
[Graphical view]
PRINTSiPR00060. RIBOSOMALL16.
SUPFAMiSSF54686. SSF54686. 1 hit.
TIGRFAMsiTIGR01164. rplP_bact. 1 hit.
PROSITEiPS00586. RIBOSOMAL_L16_1. 1 hit.
PS00701. RIBOSOMAL_L16_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ADY7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQPKRTKFR KMHKGRNRGL AQGTDVSFGS FGLKAVGRGR LTARQIEAAR
60 70 80 90 100
RAMTRAVKRQ GKIWIRVFPD KPITEKPLAV RMGKGKGNVE YWVALIQPGK
110 120 130
VLYEMDGVPE ELAREAFKLA AAKLPIKTTF VTKTVM
Length:136
Mass (Da):15,281
Last modified:July 21, 1986 - v1
Checksum:i445A9B167F7564D1
GO

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI23129. R5EC16.
RefSeqiNP_417772.1. NC_000913.3.
YP_492119.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76338; AAC76338; b3313.
BAE77978; BAE77978; BAE77978.
GeneIDi12934115.
947806.
KEGGiecj:Y75_p3863.
eco:b3313.
PATRICi32122058. VBIEscCol129921_3406.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI23129. R5EC16.
RefSeqiNP_417772.1. NC_000913.3.
YP_492119.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00M1-136[»]
2RDOelectron microscopy9.10M1-136[»]
3BBXelectron microscopy10.00M1-136[»]
3J5Lelectron microscopy6.60M1-136[»]
3J7Zelectron microscopy3.90M1-136[»]
4CSUelectron microscopy5.50M1-136[»]
4U1UX-ray2.95BM/DM1-136[»]
4U1VX-ray3.00BM/DM1-136[»]
4U20X-ray2.90BM/DM1-136[»]
4U24X-ray2.90BM/DM1-136[»]
4U25X-ray2.90BM/DM1-136[»]
4U26X-ray2.80BM/DM1-136[»]
4U27X-ray2.80BM/DM1-136[»]
4V47electron microscopy12.30AK1-136[»]
4V48electron microscopy11.50AK1-136[»]
4V4HX-ray3.46BM/DM1-136[»]
4V4QX-ray3.46BM/DM1-136[»]
4V4Velectron microscopy15.00BK3-133[»]
4V4Welectron microscopy15.00BK3-133[»]
4V50X-ray3.22BM/DM1-136[»]
4V52X-ray3.21BM/DM1-136[»]
4V53X-ray3.54BM/DM1-136[»]
4V54X-ray3.30BM/DM1-136[»]
4V55X-ray4.00BM/DM1-136[»]
4V56X-ray3.93BM/DM1-136[»]
4V57X-ray3.50BM/DM1-136[»]
4V5BX-ray3.74AM/CM1-136[»]
4V5Helectron microscopy5.80BM1-136[»]
4V5YX-ray4.45BM/DM1-136[»]
4V64X-ray3.50BM/DM1-136[»]
4V65electron microscopy9.00BF1-136[»]
4V66electron microscopy9.00BF1-136[»]
4V69electron microscopy6.70BM1-136[»]
4V6CX-ray3.19BM/DM1-136[»]
4V6DX-ray3.81BM/DM1-136[»]
4V6EX-ray3.71BM/DM1-136[»]
4V6Kelectron microscopy8.25AN1-136[»]
4V6Lelectron microscopy13.20BN1-136[»]
4V6Melectron microscopy7.10BM1-136[»]
4V6Nelectron microscopy12.10AO1-136[»]
4V6Oelectron microscopy14.70BO1-136[»]
4V6Pelectron microscopy13.50BO1-136[»]
4V6Qelectron microscopy11.50BO1-136[»]
4V6Relectron microscopy11.50BO1-136[»]
4V6Selectron microscopy13.10AO1-136[»]
4V6Telectron microscopy8.30BM1-136[»]
4V6Velectron microscopy9.80BQ1-136[»]
4V6Yelectron microscopy12.00BM1-136[»]
4V6Zelectron microscopy12.00BM1-136[»]
4V70electron microscopy17.00BM1-136[»]
4V71electron microscopy20.00BM1-136[»]
4V72electron microscopy13.00BM1-136[»]
4V73electron microscopy15.00BM1-136[»]
4V74electron microscopy17.00BM1-136[»]
4V75electron microscopy12.00BM1-136[»]
4V76electron microscopy17.00BM1-136[»]
4V77electron microscopy17.00BM1-136[»]
4V78electron microscopy20.00BM1-136[»]
4V79electron microscopy15.00BM1-136[»]
4V7Aelectron microscopy9.00BM1-136[»]
4V7Belectron microscopy6.80BM1-136[»]
4V7Celectron microscopy7.60BO1-136[»]
4V7Delectron microscopy7.60AP1-136[»]
4V7Ielectron microscopy9.60AM1-136[»]
4V7SX-ray3.25BM/DM1-136[»]
4V7TX-ray3.19BM/DM1-136[»]
4V7UX-ray3.10BM/DM1-136[»]
4V7VX-ray3.29BM/DM1-136[»]
4V85X-ray3.20Q1-136[»]
4V89X-ray3.70BQ1-136[»]
4V9CX-ray3.30BM/DM1-136[»]
4V9DX-ray3.00CM/DM1-136[»]
4V9OX-ray2.90AM/CM/EM/GM1-136[»]
4V9PX-ray2.90AM/CM/EM/GM1-136[»]
4WF1X-ray3.09BM/DM1-136[»]
4WWWX-ray3.10RM/YM1-136[»]
5AFIelectron microscopy2.90M1-136[»]
ProteinModelPortaliP0ADY7.
SMRiP0ADY7. Positions 1-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35976N.
IntActiP0ADY7. 34 interactions.
MINTiMINT-1302401.
STRINGi511145.b3313.

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB00446. Chloramphenicol.

Proteomic databases

PaxDbiP0ADY7.
PRIDEiP0ADY7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76338; AAC76338; b3313.
BAE77978; BAE77978; BAE77978.
GeneIDi12934115.
947806.
KEGGiecj:Y75_p3863.
eco:b3313.
PATRICi32122058. VBIEscCol129921_3406.

Organism-specific databases

EchoBASEiEB0870.
EcoGeneiEG10877. rplP.

Phylogenomic databases

eggNOGiCOG0197.
HOGENOMiHOG000164573.
InParanoidiP0ADY7.
KOiK02878.
OMAiPVKTKFI.
OrthoDBiEOG6WHNWS.
PhylomeDBiP0ADY7.

Enzyme and pathway databases

BioCyciEcoCyc:EG10877-MONOMER.
ECOL316407:JW3275-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ADY7.
PROiP0ADY7.

Gene expression databases

GenevestigatoriP0ADY7.

Family and domain databases

Gene3Di3.90.1170.10. 1 hit.
HAMAPiMF_01342. Ribosomal_L16.
InterProiIPR016180. Ribosomal_L10e/L16.
IPR000114. Ribosomal_L16.
IPR020798. Ribosomal_L16_CS.
[Graphical view]
PANTHERiPTHR12220. PTHR12220. 1 hit.
PfamiPF00252. Ribosomal_L16. 1 hit.
[Graphical view]
PRINTSiPR00060. RIBOSOMALL16.
SUPFAMiSSF54686. SSF54686. 1 hit.
TIGRFAMsiTIGR01164. rplP_bact. 1 hit.
PROSITEiPS00586. RIBOSOMAL_L16_1. 1 hit.
PS00701. RIBOSOMAL_L16_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, METHYLATION AT MET-1.
    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. 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. Cited for: HYDROXYLATION AT ARG-81 BY ROXA.
    Strain: K12.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL16_ECOLI
AccessioniPrimary (citable) accession number: P0ADY7
Secondary accession number(s): P02414, Q2M6X8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 29, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.