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Protein

50S ribosomal protein L19

Gene

rplS

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

Functioni

This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8 (PubMed:12809609). In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA (PubMed:16272117). The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10880-MONOMER.
ECOL316407:JW2587-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L19
Gene namesi
Name:rplS
Ordered Locus Names:b2606, JW2587
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10880. rplS.

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 – 11511450S ribosomal protein L19PRO_0000163451Add
BLAST

Proteomic databases

PaxDbiP0A7K6.
PRIDEiP0A7K6.

Expressioni

Inductioni

Part of the rpsP-rimM-trmD-rplS operon.1 Publication

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts L14 (PubMed:2665813, PubMed:16272117). Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
nanEP0A7611EBI-543891,EBI-561432

Protein-protein interaction databases

DIPiDIP-35793N.
IntActiP0A7K6. 101 interactions.
MINTiMINT-1245288.
STRINGi511145.b2606.

Structurei

Secondary structure

1
115
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 107Combined sources
Beta strandi25 – 3410Combined sources
Beta strandi37 – 5115Combined sources
Helixi54 – 563Combined sources
Beta strandi58 – 658Combined sources
Beta strandi68 – 758Combined sources
Beta strandi76 – 783Combined sources
Beta strandi81 – 888Combined sources
Beta strandi93 – 953Combined sources
Helixi98 – 1025Combined sources
Turni105 – 1084Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00P2-115[»]
2RDOelectron microscopy9.10P2-115[»]
3BBXelectron microscopy10.00P2-115[»]
3J5Lelectron microscopy6.60P2-115[»]
3J7Zelectron microscopy3.90P1-115[»]
3J9Yelectron microscopy3.90P1-115[»]
4CSUelectron microscopy5.50P2-115[»]
4U1UX-ray2.95BP/DP2-115[»]
4U1VX-ray3.00BP/DP2-115[»]
4U20X-ray2.90BP/DP2-115[»]
4U24X-ray2.90BP/DP2-115[»]
4U25X-ray2.90BP/DP2-115[»]
4U26X-ray2.80BP/DP2-115[»]
4U27X-ray2.80BP/DP2-115[»]
4UY8electron microscopy3.80P2-115[»]
4V47electron microscopy12.30AN2-115[»]
4V48electron microscopy11.50AN2-115[»]
4V4HX-ray3.46BP/DP1-115[»]
4V4QX-ray3.46BP/DP2-115[»]
4V4Velectron microscopy15.00BN2-115[»]
4V4Welectron microscopy15.00BN2-115[»]
4V50X-ray3.22BP/DP2-115[»]
4V52X-ray3.21BP/DP2-115[»]
4V53X-ray3.54BP/DP2-115[»]
4V54X-ray3.30BP/DP2-115[»]
4V55X-ray4.00BP/DP2-115[»]
4V56X-ray3.93BP/DP2-115[»]
4V57X-ray3.50BP/DP2-115[»]
4V5BX-ray3.74AP/CP2-115[»]
4V5Helectron microscopy5.80BP2-115[»]
4V5YX-ray4.45BP/DP2-115[»]
4V64X-ray3.50BP/DP2-115[»]
4V65electron microscopy9.00BI1-115[»]
4V66electron microscopy9.00BI1-115[»]
4V69electron microscopy6.70BP2-115[»]
4V6CX-ray3.19BP/DP1-115[»]
4V6DX-ray3.81BP/DP1-115[»]
4V6EX-ray3.71BP/DP1-115[»]
4V6Kelectron microscopy8.25AQ1-115[»]
4V6Lelectron microscopy13.20BQ1-115[»]
4V6Melectron microscopy7.10BP2-115[»]
4V6Nelectron microscopy12.10AR2-115[»]
4V6Oelectron microscopy14.70BR2-115[»]
4V6Pelectron microscopy13.50BR2-115[»]
4V6Qelectron microscopy11.50BR2-115[»]
4V6Relectron microscopy11.50BR2-115[»]
4V6Selectron microscopy13.10AR2-115[»]
4V6Telectron microscopy8.30BP2-115[»]
4V6Velectron microscopy9.80BT2-115[»]
4V6Yelectron microscopy12.00BP1-115[»]
4V6Zelectron microscopy12.00BP1-115[»]
4V70electron microscopy17.00BP1-115[»]
4V71electron microscopy20.00BP1-115[»]
4V72electron microscopy13.00BP1-115[»]
4V73electron microscopy15.00BP1-115[»]
4V74electron microscopy17.00BP1-115[»]
4V75electron microscopy12.00BP1-115[»]
4V76electron microscopy17.00BP1-115[»]
4V77electron microscopy17.00BP1-115[»]
4V78electron microscopy20.00BP1-115[»]
4V79electron microscopy15.00BP1-115[»]
4V7Aelectron microscopy9.00BP1-115[»]
4V7Belectron microscopy6.80BP1-115[»]
4V7Celectron microscopy7.60BR2-115[»]
4V7Delectron microscopy7.60AS2-115[»]
4V7Ielectron microscopy9.60AP1-115[»]
4V7SX-ray3.25BP/DP2-115[»]
4V7TX-ray3.19BP/DP2-115[»]
4V7UX-ray3.10BP/DP2-115[»]
4V7VX-ray3.29BP/DP2-115[»]
4V85X-ray3.20T1-115[»]
4V89X-ray3.70BT1-115[»]
4V9CX-ray3.30BP/DP1-115[»]
4V9DX-ray3.00CP/DP2-115[»]
4V9OX-ray2.90AP/CP/EP/GP1-115[»]
4V9PX-ray2.90AP/CP/EP/GP1-115[»]
4WF1X-ray3.09BP/DP2-115[»]
4WWWX-ray3.10RP/YP2-115[»]
4YBBX-ray2.10CQ/DQ2-115[»]
5AFIelectron microscopy2.90P1-115[»]
5AKAelectron microscopy5.70P2-115[»]
ProteinModelPortaliP0A7K6.
SMRiP0A7K6. Positions 2-115.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7K6.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L19P family.Curated

Phylogenomic databases

eggNOGiCOG0335.
HOGENOMiHOG000016264.
InParanoidiP0A7K6.
KOiK02884.
OMAiMLNEEQM.
OrthoDBiEOG6DZF5W.
PhylomeDBiP0A7K6.

Family and domain databases

HAMAPiMF_00402. Ribosomal_L19.
InterProiIPR001857. Ribosomal_L19.
IPR018257. Ribosomal_L19_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR15680. PTHR15680. 1 hit.
PfamiPF01245. Ribosomal_L19. 1 hit.
[Graphical view]
PIRSFiPIRSF002191. Ribosomal_L19. 1 hit.
PRINTSiPR00061. RIBOSOMALL19.
SUPFAMiSSF50104. SSF50104. 1 hit.
TIGRFAMsiTIGR01024. rplS_bact. 1 hit.
PROSITEiPS01015. RIBOSOMAL_L19. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7K6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNIIKQLEQ EQMKQDVPSF RPGDTVEVKV WVVEGSKKRL QAFEGVVIAI
60 70 80 90 100
RNRGLHSAFT VRKISNGEGV ERVFQTHSPV VDSISVKRRG AVRKAKLYYL
110
RERTGKAARI KERLN
Length:115
Mass (Da):13,133
Last modified:January 23, 2007 - v2
Checksum:i7BD9F2EFB9DDB06B
GO

Mass spectrometryi

Molecular mass is 13001.7 Da from positions 2 - 115. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01818 Genomic DNA. Translation: CAA25960.1.
U00096 Genomic DNA. Translation: AAC75655.1.
AP009048 Genomic DNA. Translation: BAA16491.1.
PIRiS07951. R5EC19.
RefSeqiNP_417097.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC75655; AAC75655; b2606.
BAA16491; BAA16491; BAA16491.
GeneIDi947096.
KEGGiecj:Y75_p2554.
eco:b2606.
PATRICi32120611. VBIEscCol129921_2704.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01818 Genomic DNA. Translation: CAA25960.1.
U00096 Genomic DNA. Translation: AAC75655.1.
AP009048 Genomic DNA. Translation: BAA16491.1.
PIRiS07951. R5EC19.
RefSeqiNP_417097.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00P2-115[»]
2RDOelectron microscopy9.10P2-115[»]
3BBXelectron microscopy10.00P2-115[»]
3J5Lelectron microscopy6.60P2-115[»]
3J7Zelectron microscopy3.90P1-115[»]
3J9Yelectron microscopy3.90P1-115[»]
4CSUelectron microscopy5.50P2-115[»]
4U1UX-ray2.95BP/DP2-115[»]
4U1VX-ray3.00BP/DP2-115[»]
4U20X-ray2.90BP/DP2-115[»]
4U24X-ray2.90BP/DP2-115[»]
4U25X-ray2.90BP/DP2-115[»]
4U26X-ray2.80BP/DP2-115[»]
4U27X-ray2.80BP/DP2-115[»]
4UY8electron microscopy3.80P2-115[»]
4V47electron microscopy12.30AN2-115[»]
4V48electron microscopy11.50AN2-115[»]
4V4HX-ray3.46BP/DP1-115[»]
4V4QX-ray3.46BP/DP2-115[»]
4V4Velectron microscopy15.00BN2-115[»]
4V4Welectron microscopy15.00BN2-115[»]
4V50X-ray3.22BP/DP2-115[»]
4V52X-ray3.21BP/DP2-115[»]
4V53X-ray3.54BP/DP2-115[»]
4V54X-ray3.30BP/DP2-115[»]
4V55X-ray4.00BP/DP2-115[»]
4V56X-ray3.93BP/DP2-115[»]
4V57X-ray3.50BP/DP2-115[»]
4V5BX-ray3.74AP/CP2-115[»]
4V5Helectron microscopy5.80BP2-115[»]
4V5YX-ray4.45BP/DP2-115[»]
4V64X-ray3.50BP/DP2-115[»]
4V65electron microscopy9.00BI1-115[»]
4V66electron microscopy9.00BI1-115[»]
4V69electron microscopy6.70BP2-115[»]
4V6CX-ray3.19BP/DP1-115[»]
4V6DX-ray3.81BP/DP1-115[»]
4V6EX-ray3.71BP/DP1-115[»]
4V6Kelectron microscopy8.25AQ1-115[»]
4V6Lelectron microscopy13.20BQ1-115[»]
4V6Melectron microscopy7.10BP2-115[»]
4V6Nelectron microscopy12.10AR2-115[»]
4V6Oelectron microscopy14.70BR2-115[»]
4V6Pelectron microscopy13.50BR2-115[»]
4V6Qelectron microscopy11.50BR2-115[»]
4V6Relectron microscopy11.50BR2-115[»]
4V6Selectron microscopy13.10AR2-115[»]
4V6Telectron microscopy8.30BP2-115[»]
4V6Velectron microscopy9.80BT2-115[»]
4V6Yelectron microscopy12.00BP1-115[»]
4V6Zelectron microscopy12.00BP1-115[»]
4V70electron microscopy17.00BP1-115[»]
4V71electron microscopy20.00BP1-115[»]
4V72electron microscopy13.00BP1-115[»]
4V73electron microscopy15.00BP1-115[»]
4V74electron microscopy17.00BP1-115[»]
4V75electron microscopy12.00BP1-115[»]
4V76electron microscopy17.00BP1-115[»]
4V77electron microscopy17.00BP1-115[»]
4V78electron microscopy20.00BP1-115[»]
4V79electron microscopy15.00BP1-115[»]
4V7Aelectron microscopy9.00BP1-115[»]
4V7Belectron microscopy6.80BP1-115[»]
4V7Celectron microscopy7.60BR2-115[»]
4V7Delectron microscopy7.60AS2-115[»]
4V7Ielectron microscopy9.60AP1-115[»]
4V7SX-ray3.25BP/DP2-115[»]
4V7TX-ray3.19BP/DP2-115[»]
4V7UX-ray3.10BP/DP2-115[»]
4V7VX-ray3.29BP/DP2-115[»]
4V85X-ray3.20T1-115[»]
4V89X-ray3.70BT1-115[»]
4V9CX-ray3.30BP/DP1-115[»]
4V9DX-ray3.00CP/DP2-115[»]
4V9OX-ray2.90AP/CP/EP/GP1-115[»]
4V9PX-ray2.90AP/CP/EP/GP1-115[»]
4WF1X-ray3.09BP/DP2-115[»]
4WWWX-ray3.10RP/YP2-115[»]
4YBBX-ray2.10CQ/DQ2-115[»]
5AFIelectron microscopy2.90P1-115[»]
5AKAelectron microscopy5.70P2-115[»]
ProteinModelPortaliP0A7K6.
SMRiP0A7K6. Positions 2-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35793N.
IntActiP0A7K6. 101 interactions.
MINTiMINT-1245288.
STRINGi511145.b2606.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0A7K6.
PRIDEiP0A7K6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75655; AAC75655; b2606.
BAA16491; BAA16491; BAA16491.
GeneIDi947096.
KEGGiecj:Y75_p2554.
eco:b2606.
PATRICi32120611. VBIEscCol129921_2704.

Organism-specific databases

EchoBASEiEB0873.
EcoGeneiEG10880. rplS.

Phylogenomic databases

eggNOGiCOG0335.
HOGENOMiHOG000016264.
InParanoidiP0A7K6.
KOiK02884.
OMAiMLNEEQM.
OrthoDBiEOG6DZF5W.
PhylomeDBiP0A7K6.

Enzyme and pathway databases

BioCyciEcoCyc:EG10880-MONOMER.
ECOL316407:JW2587-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7K6.
PROiP0A7K6.

Family and domain databases

HAMAPiMF_00402. Ribosomal_L19.
InterProiIPR001857. Ribosomal_L19.
IPR018257. Ribosomal_L19_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR15680. PTHR15680. 1 hit.
PfamiPF01245. Ribosomal_L19. 1 hit.
[Graphical view]
PIRSFiPIRSF002191. Ribosomal_L19. 1 hit.
PRINTSiPR00061. RIBOSOMALL19.
SUPFAMiSSF50104. SSF50104. 1 hit.
TIGRFAMsiTIGR01024. rplS_bact. 1 hit.
PROSITEiPS01015. RIBOSOMAL_L19. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21-K polypeptide."
    Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.
    EMBO J. 2:899-905(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE.
    Strain: K12.
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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. "Primary structure of protein L19 from the large subunit of Escherichia coli ribosomes."
    Brosius J., Arfsten U.
    Biochemistry 17:508-516(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-115.
  6. "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 L14.
  7. "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.
  8. "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), INTERSUBUNIT BRIDGE FORMATION.
    Strain: MRE-600.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  10. "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 2-115 IN TNAC-STALLED 50S RIBOSOMAL SUBUNIT.
    Strain: K12 / A19 / KC6.

Entry informationi

Entry nameiRL19_ECOLI
AccessioniPrimary (citable) accession number: P0A7K6
Secondary accession number(s): P02420
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 105 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.