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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.
MetaCyc:EG10880-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10880. rplS.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001634512 – 11550S ribosomal protein L19Add BLAST114

Proteomic databases

EPDiP0A7K6.
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

Protein-protein interaction databases

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

Structurei

Secondary structure

1115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 10Combined sources7
Beta strandi25 – 34Combined sources10
Beta strandi37 – 51Combined sources15
Helixi54 – 56Combined sources3
Beta strandi58 – 65Combined sources8
Beta strandi68 – 75Combined sources8
Beta strandi76 – 78Combined sources3
Beta strandi81 – 88Combined sources8
Beta strandi93 – 95Combined sources3
Helixi98 – 102Combined sources5
Turni105 – 108Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00P2-115[»]
2RDOelectron microscopy9.10P2-115[»]
3BBXelectron microscopy10.00P2-115[»]
3J5Lelectron microscopy6.60P2-115[»]
3J7Zelectron microscopy3.90P1-115[»]
3J8Gelectron microscopy5.00P1-115[»]
3J9Yelectron microscopy3.90P1-115[»]
3J9Zelectron microscopy3.60LM2-115[»]
3JA1electron microscopy3.60LR2-115[»]
3JBUelectron microscopy3.64p1-115[»]
3JBVelectron microscopy3.32p1-115[»]
3JCDelectron microscopy3.70P1-115[»]
3JCEelectron microscopy3.20P1-115[»]
3JCJelectron microscopy3.70O1-115[»]
3JCNelectron microscopy4.60P1-115[»]
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[»]
4WOIX-ray3.00BP/CP1-115[»]
4WWWX-ray3.10RP/YP2-115[»]
4YBBX-ray2.10CQ/DQ2-115[»]
5ADYelectron microscopy4.50P1-115[»]
5AFIelectron microscopy2.90P1-115[»]
5AKAelectron microscopy5.70P2-115[»]
5GADelectron microscopy3.70Q1-115[»]
5GAEelectron microscopy3.33Q1-115[»]
5GAFelectron microscopy4.30Q2-115[»]
5GAGelectron microscopy3.80Q1-115[»]
5GAHelectron microscopy3.80Q1-115[»]
5IQRelectron microscopy3.00P1-115[»]
5IT8X-ray3.12CQ/DQ2-115[»]
5J5BX-ray2.80CQ/DQ2-115[»]
5J7LX-ray3.00CQ/DQ2-115[»]
5J88X-ray3.32CQ/DQ2-115[»]
5J8AX-ray3.10CQ/DQ2-115[»]
5J91X-ray2.96CQ/DQ2-115[»]
5JC9X-ray3.03CQ/DQ2-115[»]
5JTEelectron microscopy3.60BP1-115[»]
5JU8electron microscopy3.60BP1-115[»]
5KCRelectron microscopy3.601T1-115[»]
5KCSelectron microscopy3.901T1-115[»]
5KPSelectron microscopy3.90P1-115[»]
5KPVelectron microscopy4.10O1-115[»]
5KPWelectron microscopy3.90O1-115[»]
5KPXelectron microscopy3.90O1-115[»]
5L3Pelectron microscopy3.70T1-115[»]
ProteinModelPortaliP0A7K6.
SMRiP0A7K6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7K6.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L19P family.Curated

Phylogenomic databases

eggNOGiENOG4108YY1. Bacteria.
COG0335. LUCA.
HOGENOMiHOG000016264.
InParanoidiP0A7K6.
KOiK02884.
OMAiEAEQCAK.
PhylomeDBiP0A7K6.

Family and domain databases

HAMAPiMF_00402. Ribosomal_L19. 1 hit.
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.
WP_000065253.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75655; AAC75655; b2606.
BAA16491; BAA16491; BAA16491.
GeneIDi947096.
KEGGiecj:JW2587.
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.
WP_000065253.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00P2-115[»]
2RDOelectron microscopy9.10P2-115[»]
3BBXelectron microscopy10.00P2-115[»]
3J5Lelectron microscopy6.60P2-115[»]
3J7Zelectron microscopy3.90P1-115[»]
3J8Gelectron microscopy5.00P1-115[»]
3J9Yelectron microscopy3.90P1-115[»]
3J9Zelectron microscopy3.60LM2-115[»]
3JA1electron microscopy3.60LR2-115[»]
3JBUelectron microscopy3.64p1-115[»]
3JBVelectron microscopy3.32p1-115[»]
3JCDelectron microscopy3.70P1-115[»]
3JCEelectron microscopy3.20P1-115[»]
3JCJelectron microscopy3.70O1-115[»]
3JCNelectron microscopy4.60P1-115[»]
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[»]
4WOIX-ray3.00BP/CP1-115[»]
4WWWX-ray3.10RP/YP2-115[»]
4YBBX-ray2.10CQ/DQ2-115[»]
5ADYelectron microscopy4.50P1-115[»]
5AFIelectron microscopy2.90P1-115[»]
5AKAelectron microscopy5.70P2-115[»]
5GADelectron microscopy3.70Q1-115[»]
5GAEelectron microscopy3.33Q1-115[»]
5GAFelectron microscopy4.30Q2-115[»]
5GAGelectron microscopy3.80Q1-115[»]
5GAHelectron microscopy3.80Q1-115[»]
5IQRelectron microscopy3.00P1-115[»]
5IT8X-ray3.12CQ/DQ2-115[»]
5J5BX-ray2.80CQ/DQ2-115[»]
5J7LX-ray3.00CQ/DQ2-115[»]
5J88X-ray3.32CQ/DQ2-115[»]
5J8AX-ray3.10CQ/DQ2-115[»]
5J91X-ray2.96CQ/DQ2-115[»]
5JC9X-ray3.03CQ/DQ2-115[»]
5JTEelectron microscopy3.60BP1-115[»]
5JU8electron microscopy3.60BP1-115[»]
5KCRelectron microscopy3.601T1-115[»]
5KCSelectron microscopy3.901T1-115[»]
5KPSelectron microscopy3.90P1-115[»]
5KPVelectron microscopy4.10O1-115[»]
5KPWelectron microscopy3.90O1-115[»]
5KPXelectron microscopy3.90O1-115[»]
5L3Pelectron microscopy3.70T1-115[»]
ProteinModelPortaliP0A7K6.
SMRiP0A7K6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

EPDiP0A7K6.
PaxDbiP0A7K6.
PRIDEiP0A7K6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75655; AAC75655; b2606.
BAA16491; BAA16491; BAA16491.
GeneIDi947096.
KEGGiecj:JW2587.
eco:b2606.
PATRICi32120611. VBIEscCol129921_2704.

Organism-specific databases

EchoBASEiEB0873.
EcoGeneiEG10880. rplS.

Phylogenomic databases

eggNOGiENOG4108YY1. Bacteria.
COG0335. LUCA.
HOGENOMiHOG000016264.
InParanoidiP0A7K6.
KOiK02884.
OMAiEAEQCAK.
PhylomeDBiP0A7K6.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7K6.
PROiP0A7K6.

Family and domain databases

HAMAPiMF_00402. Ribosomal_L19. 1 hit.
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...

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: November 30, 2016
This is version 118 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

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.