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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.2 Publications

GO - Molecular functioni

  • rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: GO_Central
  • tRNA binding Source: EcoCyc

GO - Biological processi

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.
MetaCyc:EG10877-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10877. rplP.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

DrugBankiDB00446. Chloramphenicol.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000621011 – 13650S ribosomal protein L16Add BLAST136

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-methylmethionine1 Publication1
Modified residuei81(3R)-3-hydroxyarginine1 Publication1

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

EPDiP0ADY7.
PaxDbiP0ADY7.
PRIDEiP0ADY7.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Cross-links to the A and P site tRNAs.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

1136
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 10Combined sources3
Beta strandi28 – 35Combined sources8
Beta strandi39 – 42Combined sources4
Helixi43 – 57Combined sources15
Beta strandi61 – 65Combined sources5
Beta strandi71 – 75Combined sources5
Beta strandi82 – 85Combined sources4
Beta strandi88 – 96Combined sources9
Beta strandi101 – 108Combined sources8
Helixi110 – 121Combined sources12
Beta strandi124 – 126Combined sources3
Beta strandi128 – 132Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00M1-136[»]
2RDOelectron microscopy9.10M1-136[»]
3BBXelectron microscopy10.00M1-136[»]
3J5Lelectron microscopy6.60M1-136[»]
3J7Zelectron microscopy3.90M1-136[»]
3J8Gelectron microscopy5.00M1-136[»]
3J9Yelectron microscopy3.90M1-136[»]
3J9Zelectron microscopy3.60LI1-136[»]
3JA1electron microscopy3.60LO1-136[»]
3JBUelectron microscopy3.64m1-136[»]
3JBVelectron microscopy3.32m1-136[»]
3JCDelectron microscopy3.70M1-136[»]
3JCEelectron microscopy3.20M1-136[»]
3JCJelectron microscopy3.70L1-136[»]
3JCNelectron microscopy4.60M1-136[»]
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[»]
4UY8electron microscopy3.80M1-136[»]
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[»]
4WOIX-ray3.00BM/CM1-136[»]
4WWWX-ray3.10RM/YM1-136[»]
4YBBX-ray2.10CN/DN1-136[»]
5ADYelectron microscopy4.50M1-136[»]
5AFIelectron microscopy2.90M1-136[»]
5AKAelectron microscopy5.70M1-136[»]
5GADelectron microscopy3.70N1-136[»]
5GAEelectron microscopy3.33N1-136[»]
5GAFelectron microscopy4.30N1-136[»]
5GAGelectron microscopy3.80N1-136[»]
5GAHelectron microscopy3.80N1-136[»]
5IQRelectron microscopy3.00M1-136[»]
5IT8X-ray3.12CN/DN1-136[»]
5J5BX-ray2.80CN/DN1-136[»]
5J7LX-ray3.00CN/DN1-136[»]
5J88X-ray3.32CN/DN1-136[»]
5J8AX-ray3.10CN/DN1-136[»]
5J91X-ray2.96CN/DN1-136[»]
5JC9X-ray3.03CN/DN1-136[»]
5JTEelectron microscopy3.60BM1-136[»]
5JU8electron microscopy3.60BM1-136[»]
5KCRelectron microscopy3.601Q1-136[»]
5KCSelectron microscopy3.901Q1-136[»]
5KPSelectron microscopy3.90M1-136[»]
5KPVelectron microscopy4.10L1-136[»]
5KPWelectron microscopy3.90L1-136[»]
5KPXelectron microscopy3.90L1-136[»]
5L3Pelectron microscopy3.70Q1-136[»]
ProteinModelPortaliP0ADY7.
SMRiP0ADY7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADY7.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L16P family.Curated

Phylogenomic databases

eggNOGiENOG4108R70. Bacteria.
COG0197. LUCA.
HOGENOMiHOG000164573.
InParanoidiP0ADY7.
KOiK02878.
OMAiKGAVEYW.
PhylomeDBiP0ADY7.

Family and domain databases

CDDicd01433. Ribosomal_L16_L10e. 1 hit.
Gene3Di3.90.1170.10. 1 hit.
HAMAPiMF_01342. Ribosomal_L16. 1 hit.
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.
WP_000941212.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76338; AAC76338; b3313.
BAE77978; BAE77978; BAE77978.
GeneIDi947806.
KEGGiecj:JW3275.
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.
WP_000941212.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00M1-136[»]
2RDOelectron microscopy9.10M1-136[»]
3BBXelectron microscopy10.00M1-136[»]
3J5Lelectron microscopy6.60M1-136[»]
3J7Zelectron microscopy3.90M1-136[»]
3J8Gelectron microscopy5.00M1-136[»]
3J9Yelectron microscopy3.90M1-136[»]
3J9Zelectron microscopy3.60LI1-136[»]
3JA1electron microscopy3.60LO1-136[»]
3JBUelectron microscopy3.64m1-136[»]
3JBVelectron microscopy3.32m1-136[»]
3JCDelectron microscopy3.70M1-136[»]
3JCEelectron microscopy3.20M1-136[»]
3JCJelectron microscopy3.70L1-136[»]
3JCNelectron microscopy4.60M1-136[»]
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[»]
4UY8electron microscopy3.80M1-136[»]
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[»]
4WOIX-ray3.00BM/CM1-136[»]
4WWWX-ray3.10RM/YM1-136[»]
4YBBX-ray2.10CN/DN1-136[»]
5ADYelectron microscopy4.50M1-136[»]
5AFIelectron microscopy2.90M1-136[»]
5AKAelectron microscopy5.70M1-136[»]
5GADelectron microscopy3.70N1-136[»]
5GAEelectron microscopy3.33N1-136[»]
5GAFelectron microscopy4.30N1-136[»]
5GAGelectron microscopy3.80N1-136[»]
5GAHelectron microscopy3.80N1-136[»]
5IQRelectron microscopy3.00M1-136[»]
5IT8X-ray3.12CN/DN1-136[»]
5J5BX-ray2.80CN/DN1-136[»]
5J7LX-ray3.00CN/DN1-136[»]
5J88X-ray3.32CN/DN1-136[»]
5J8AX-ray3.10CN/DN1-136[»]
5J91X-ray2.96CN/DN1-136[»]
5JC9X-ray3.03CN/DN1-136[»]
5JTEelectron microscopy3.60BM1-136[»]
5JU8electron microscopy3.60BM1-136[»]
5KCRelectron microscopy3.601Q1-136[»]
5KCSelectron microscopy3.901Q1-136[»]
5KPSelectron microscopy3.90M1-136[»]
5KPVelectron microscopy4.10L1-136[»]
5KPWelectron microscopy3.90L1-136[»]
5KPXelectron microscopy3.90L1-136[»]
5L3Pelectron microscopy3.70Q1-136[»]
ProteinModelPortaliP0ADY7.
SMRiP0ADY7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

DrugBankiDB00446. Chloramphenicol.

Proteomic databases

EPDiP0ADY7.
PaxDbiP0ADY7.
PRIDEiP0ADY7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76338; AAC76338; b3313.
BAE77978; BAE77978; BAE77978.
GeneIDi947806.
KEGGiecj:JW3275.
eco:b3313.
PATRICi32122058. VBIEscCol129921_3406.

Organism-specific databases

EchoBASEiEB0870.
EcoGeneiEG10877. rplP.

Phylogenomic databases

eggNOGiENOG4108R70. Bacteria.
COG0197. LUCA.
HOGENOMiHOG000164573.
InParanoidiP0ADY7.
KOiK02878.
OMAiKGAVEYW.
PhylomeDBiP0ADY7.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0ADY7.
PROiP0ADY7.

Family and domain databases

CDDicd01433. Ribosomal_L16_L10e. 1 hit.
Gene3Di3.90.1170.10. 1 hit.
HAMAPiMF_01342. Ribosomal_L16. 1 hit.
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...

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: November 30, 2016
This is version 111 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

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 one 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.