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Protein

50S ribosomal protein L20

Gene

rplT

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

Functioni

One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.1 Publication

GO - Molecular functioni

  • rRNA binding Source: UniProtKB-HAMAP
  • structural constituent of ribosome Source: EcoCyc
  • translation repressor activity, nucleic acid binding Source: EcoCyc

GO - Biological processi

  • negative regulation of translation Source: GOC
  • ribosomal large subunit assembly Source: EcoCyc
  • translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10881-MONOMER.
ECOL316407:JW1706-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L20
Gene namesi
Name:rplT
Synonyms:pdzA
Ordered Locus Names:b1716, JW1706
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10881. rplT.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11811750S ribosomal protein L20PRO_0000177156Add
BLAST

Proteomic databases

PaxDbiP0A7L3.
PRIDEiP0A7L3.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts L21 (PubMed:2665813).1 Publication

Protein-protein interaction databases

DIPiDIP-47941N.
IntActiP0A7L3. 35 interactions.
MINTiMINT-1321645.
STRINGi511145.b1716.

Structurei

Secondary structure

1
118
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2014Combined sources
Turni21 – 233Combined sources
Helixi27 – 304Combined sources
Helixi32 – 7140Combined sources
Beta strandi72 – 743Combined sources
Helixi76 – 8510Combined sources
Beta strandi86 – 883Combined sources
Helixi92 – 10110Combined sources
Helixi103 – 11715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00Q2-118[»]
2RDOelectron microscopy9.10Q2-118[»]
3BBXelectron microscopy10.00Q2-118[»]
3J5Lelectron microscopy6.60Q2-118[»]
3J7Zelectron microscopy3.90Q1-118[»]
3J9Yelectron microscopy3.90Q1-118[»]
4CSUelectron microscopy5.50Q2-118[»]
4U1UX-ray2.95BQ/DQ2-118[»]
4U1VX-ray3.00BQ/DQ2-118[»]
4U20X-ray2.90BQ/DQ2-118[»]
4U24X-ray2.90BQ/DQ2-118[»]
4U25X-ray2.90BQ/DQ2-118[»]
4U26X-ray2.80BQ/DQ2-118[»]
4U27X-ray2.80BQ/DQ2-118[»]
4UY8electron microscopy3.80Q2-118[»]
4V47electron microscopy12.30AO2-118[»]
4V48electron microscopy11.50AO2-118[»]
4V4HX-ray3.46BQ/DQ1-118[»]
4V4QX-ray3.46BQ/DQ2-118[»]
4V4Velectron microscopy15.00BO3-117[»]
4V4Welectron microscopy15.00BO3-117[»]
4V50X-ray3.22BQ/DQ2-118[»]
4V52X-ray3.21BQ/DQ2-118[»]
4V53X-ray3.54BQ/DQ2-118[»]
4V54X-ray3.30BQ/DQ2-118[»]
4V55X-ray4.00BQ/DQ2-118[»]
4V56X-ray3.93BQ/DQ2-118[»]
4V57X-ray3.50BQ/DQ2-118[»]
4V5BX-ray3.74AQ/CQ2-118[»]
4V5Helectron microscopy5.80BQ2-118[»]
4V5YX-ray4.45BQ/DQ2-118[»]
4V64X-ray3.50BQ/DQ2-118[»]
4V65electron microscopy9.00BJ1-118[»]
4V66electron microscopy9.00BJ1-118[»]
4V69electron microscopy6.70BQ2-118[»]
4V6CX-ray3.19BQ/DQ1-118[»]
4V6DX-ray3.81BQ/DQ1-118[»]
4V6EX-ray3.71BQ/DQ1-118[»]
4V6Kelectron microscopy8.25AR1-118[»]
4V6Lelectron microscopy13.20BR1-118[»]
4V6Melectron microscopy7.10BQ2-118[»]
4V6Nelectron microscopy12.10AS2-118[»]
4V6Oelectron microscopy14.70BS2-118[»]
4V6Pelectron microscopy13.50BS2-118[»]
4V6Qelectron microscopy11.50BS2-118[»]
4V6Relectron microscopy11.50BS2-118[»]
4V6Selectron microscopy13.10AS2-118[»]
4V6Telectron microscopy8.30BQ2-118[»]
4V6Velectron microscopy9.80U2-118[»]
4V6Yelectron microscopy12.00BQ1-118[»]
4V6Zelectron microscopy12.00BQ1-118[»]
4V70electron microscopy17.00BQ1-118[»]
4V71electron microscopy20.00BQ1-118[»]
4V72electron microscopy13.00BQ1-118[»]
4V73electron microscopy15.00BQ1-118[»]
4V74electron microscopy17.00BQ1-118[»]
4V75electron microscopy12.00BQ1-118[»]
4V76electron microscopy17.00BQ1-118[»]
4V77electron microscopy17.00BQ1-118[»]
4V78electron microscopy20.00BQ1-118[»]
4V79electron microscopy15.00BQ1-118[»]
4V7Aelectron microscopy9.00BQ1-118[»]
4V7Belectron microscopy6.80BQ1-118[»]
4V7Celectron microscopy7.60BS2-118[»]
4V7Delectron microscopy7.60AT2-118[»]
4V7Ielectron microscopy9.60AQ1-118[»]
4V7SX-ray3.25BQ/DQ2-118[»]
4V7TX-ray3.19BQ/DQ2-118[»]
4V7UX-ray3.10BQ/DQ2-118[»]
4V7VX-ray3.29BQ/DQ2-118[»]
4V85X-ray3.20U1-118[»]
4V89X-ray3.70BU1-118[»]
4V9CX-ray3.30BQ/DQ1-118[»]
4V9DX-ray3.00CQ/DQ2-118[»]
4V9OX-ray2.90AQ/CQ/EQ/GQ1-118[»]
4V9PX-ray2.90AQ/CQ/EQ/GQ1-118[»]
4WF1X-ray3.09BQ/DQ2-118[»]
4WWWX-ray3.10RQ/YQ2-118[»]
4YBBX-ray2.10CR/DR2-118[»]
5AFIelectron microscopy2.90Q1-118[»]
5AKAelectron microscopy5.70Q2-118[»]
ProteinModelPortaliP0A7L3.
SMRiP0A7L3. Positions 2-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7L3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L20P family.Curated

Phylogenomic databases

eggNOGiCOG0292.
HOGENOMiHOG000035046.
InParanoidiP0A7L3.
KOiK02887.
OMAiGRRKNVW.
OrthoDBiEOG6CGCMB.
PhylomeDBiP0A7L3.

Family and domain databases

HAMAPiMF_00382. Ribosomal_L20.
InterProiIPR005813. Ribosomal_L20.
[Graphical view]
PANTHERiPTHR10986. PTHR10986. 1 hit.
PfamiPF00453. Ribosomal_L20. 1 hit.
[Graphical view]
PRINTSiPR00062. RIBOSOMALL20.
TIGRFAMsiTIGR01032. rplT_bact. 1 hit.
PROSITEiPS00937. RIBOSOMAL_L20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7L3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARVKRGVIA RARHKKILKQ AKGYYGARSR VYRVAFQAVI KAGQYAYRDR
60 70 80 90 100
RQRKRQFRQL WIARINAAAR QNGISYSKFI NGLKKASVEI DRKILADIAV
110
FDKVAFTALV EKAKAALA
Length:118
Mass (Da):13,497
Last modified:January 23, 2007 - v2
Checksum:iE60AFDBB6F05DFB3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331R → A in CAA23562 (PubMed:6317865).Curated
Sequence conflicti33 – 331R → A in AAA51468 (PubMed:6317865).Curated

Mass spectrometryi

Molecular mass is 13366.9 Da from positions 2 - 118. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00291 Genomic DNA. Translation: CAA23562.1.
K02844 Genomic DNA. Translation: AAA51468.1.
U00096 Genomic DNA. Translation: AAC74786.1.
AP009048 Genomic DNA. Translation: BAA15483.1.
M10423 Genomic DNA. Translation: AAA23960.1.
PIRiD64930. R5EC20.
RefSeqiNP_416231.1. NC_000913.3.
WP_000124850.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC74786; AAC74786; b1716.
BAA15483; BAA15483; BAA15483.
GeneIDi945152.
KEGGieco:b1716.
PATRICi32118736. VBIEscCol129921_1786.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00291 Genomic DNA. Translation: CAA23562.1.
K02844 Genomic DNA. Translation: AAA51468.1.
U00096 Genomic DNA. Translation: AAC74786.1.
AP009048 Genomic DNA. Translation: BAA15483.1.
M10423 Genomic DNA. Translation: AAA23960.1.
PIRiD64930. R5EC20.
RefSeqiNP_416231.1. NC_000913.3.
WP_000124850.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00Q2-118[»]
2RDOelectron microscopy9.10Q2-118[»]
3BBXelectron microscopy10.00Q2-118[»]
3J5Lelectron microscopy6.60Q2-118[»]
3J7Zelectron microscopy3.90Q1-118[»]
3J9Yelectron microscopy3.90Q1-118[»]
4CSUelectron microscopy5.50Q2-118[»]
4U1UX-ray2.95BQ/DQ2-118[»]
4U1VX-ray3.00BQ/DQ2-118[»]
4U20X-ray2.90BQ/DQ2-118[»]
4U24X-ray2.90BQ/DQ2-118[»]
4U25X-ray2.90BQ/DQ2-118[»]
4U26X-ray2.80BQ/DQ2-118[»]
4U27X-ray2.80BQ/DQ2-118[»]
4UY8electron microscopy3.80Q2-118[»]
4V47electron microscopy12.30AO2-118[»]
4V48electron microscopy11.50AO2-118[»]
4V4HX-ray3.46BQ/DQ1-118[»]
4V4QX-ray3.46BQ/DQ2-118[»]
4V4Velectron microscopy15.00BO3-117[»]
4V4Welectron microscopy15.00BO3-117[»]
4V50X-ray3.22BQ/DQ2-118[»]
4V52X-ray3.21BQ/DQ2-118[»]
4V53X-ray3.54BQ/DQ2-118[»]
4V54X-ray3.30BQ/DQ2-118[»]
4V55X-ray4.00BQ/DQ2-118[»]
4V56X-ray3.93BQ/DQ2-118[»]
4V57X-ray3.50BQ/DQ2-118[»]
4V5BX-ray3.74AQ/CQ2-118[»]
4V5Helectron microscopy5.80BQ2-118[»]
4V5YX-ray4.45BQ/DQ2-118[»]
4V64X-ray3.50BQ/DQ2-118[»]
4V65electron microscopy9.00BJ1-118[»]
4V66electron microscopy9.00BJ1-118[»]
4V69electron microscopy6.70BQ2-118[»]
4V6CX-ray3.19BQ/DQ1-118[»]
4V6DX-ray3.81BQ/DQ1-118[»]
4V6EX-ray3.71BQ/DQ1-118[»]
4V6Kelectron microscopy8.25AR1-118[»]
4V6Lelectron microscopy13.20BR1-118[»]
4V6Melectron microscopy7.10BQ2-118[»]
4V6Nelectron microscopy12.10AS2-118[»]
4V6Oelectron microscopy14.70BS2-118[»]
4V6Pelectron microscopy13.50BS2-118[»]
4V6Qelectron microscopy11.50BS2-118[»]
4V6Relectron microscopy11.50BS2-118[»]
4V6Selectron microscopy13.10AS2-118[»]
4V6Telectron microscopy8.30BQ2-118[»]
4V6Velectron microscopy9.80U2-118[»]
4V6Yelectron microscopy12.00BQ1-118[»]
4V6Zelectron microscopy12.00BQ1-118[»]
4V70electron microscopy17.00BQ1-118[»]
4V71electron microscopy20.00BQ1-118[»]
4V72electron microscopy13.00BQ1-118[»]
4V73electron microscopy15.00BQ1-118[»]
4V74electron microscopy17.00BQ1-118[»]
4V75electron microscopy12.00BQ1-118[»]
4V76electron microscopy17.00BQ1-118[»]
4V77electron microscopy17.00BQ1-118[»]
4V78electron microscopy20.00BQ1-118[»]
4V79electron microscopy15.00BQ1-118[»]
4V7Aelectron microscopy9.00BQ1-118[»]
4V7Belectron microscopy6.80BQ1-118[»]
4V7Celectron microscopy7.60BS2-118[»]
4V7Delectron microscopy7.60AT2-118[»]
4V7Ielectron microscopy9.60AQ1-118[»]
4V7SX-ray3.25BQ/DQ2-118[»]
4V7TX-ray3.19BQ/DQ2-118[»]
4V7UX-ray3.10BQ/DQ2-118[»]
4V7VX-ray3.29BQ/DQ2-118[»]
4V85X-ray3.20U1-118[»]
4V89X-ray3.70BU1-118[»]
4V9CX-ray3.30BQ/DQ1-118[»]
4V9DX-ray3.00CQ/DQ2-118[»]
4V9OX-ray2.90AQ/CQ/EQ/GQ1-118[»]
4V9PX-ray2.90AQ/CQ/EQ/GQ1-118[»]
4WF1X-ray3.09BQ/DQ2-118[»]
4WWWX-ray3.10RQ/YQ2-118[»]
4YBBX-ray2.10CR/DR2-118[»]
5AFIelectron microscopy2.90Q1-118[»]
5AKAelectron microscopy5.70Q2-118[»]
ProteinModelPortaliP0A7L3.
SMRiP0A7L3. Positions 2-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47941N.
IntActiP0A7L3. 35 interactions.
MINTiMINT-1321645.
STRINGi511145.b1716.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0A7L3.
PRIDEiP0A7L3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74786; AAC74786; b1716.
BAA15483; BAA15483; BAA15483.
GeneIDi945152.
KEGGieco:b1716.
PATRICi32118736. VBIEscCol129921_1786.

Organism-specific databases

EchoBASEiEB0874.
EcoGeneiEG10881. rplT.

Phylogenomic databases

eggNOGiCOG0292.
HOGENOMiHOG000035046.
InParanoidiP0A7L3.
KOiK02887.
OMAiGRRKNVW.
OrthoDBiEOG6CGCMB.
PhylomeDBiP0A7L3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10881-MONOMER.
ECOL316407:JW1706-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7L3.
PROiP0A7L3.

Family and domain databases

HAMAPiMF_00382. Ribosomal_L20.
InterProiIPR005813. Ribosomal_L20.
[Graphical view]
PANTHERiPTHR10986. PTHR10986. 1 hit.
PfamiPF00453. Ribosomal_L20. 1 hit.
[Graphical view]
PRINTSiPR00062. RIBOSOMALL20.
TIGRFAMsiTIGR01032. rplT_bact. 1 hit.
PROSITEiPS00937. RIBOSOMAL_L20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20."
    Fayat G., Mayaux J.-F., Sacerdot C., Fromant M., Springer M., Grunberg-Manago M., Blanquet S.
    J. Mol. Biol. 171:239-261(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Primary structure of the himA gene of Escherichia coli: homology with DNA-binding protein HU and association with the phenylalanyl-tRNA synthetase operon."
    Miller H.I.
    Cold Spring Harb. Symp. Quant. Biol. 49:691-698(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "The primary structure of protein L20 from the large subunit of the Escherichia coli ribosome."
    Wittmann-Liebold B., Seib C.
    FEBS Lett. 103:61-65(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-118.
    Strain: K12.
  7. "Attenuation control of the Escherichia coli phenylalanyl-tRNA synthetase operon."
    Springer M., Mayaux J.-F., Fayat G., Plumbridge J.A., Graffe M., Blanquet S., Grunberg-Manago M.
    J. Mol. Biol. 181:467-478(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-118.
  8. "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.
  9. "Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli."
    Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.
    Biochemistry 28:4099-4105(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO L21.
  10. "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.
  11. "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.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  13. "Molecular basis for the ribosome functioning as an L-tryptophan sensor."
    Bischoff L., Berninghausen O., Beckmann R.
    Cell Rep. 9:469-475(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 2-118 IN TNAC-STALLED 50S RIBOSOMAL SUBUNIT.
    Strain: K12 / A19 / KC6.

Entry informationi

Entry nameiRL20_ECOLI
AccessioniPrimary (citable) accession number: P0A7L3
Secondary accession number(s): P02421, Q47253
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 108 of the entry and version 2 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.