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Protein

50S ribosomal protein L19

Gene

rplS

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Contacts the 16S rRNA of the 30S subunit (part of bridge B6), connecting the 2 subunits.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-KW
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1063-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L19
Gene namesi
Name:rplS
Ordered Locus Names:TTHA1031
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14614650S ribosomal protein L19PRO_0000163558Add
BLAST

Interactioni

Subunit structurei

Part of the 50S risobomal subunit. Contacts protein L14. Forms a bridge to the 30S subunit in the 70S ribosome, contacting the 16S rRNA.

Protein-protein interaction databases

STRINGi300852.TTHA1031.

Structurei

Secondary structure

1
146
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Helixi12 – 143Combined sources
Beta strandi17 – 193Combined sources
Beta strandi23 – 253Combined sources
Beta strandi27 – 359Combined sources
Beta strandi37 – 5317Combined sources
Helixi56 – 583Combined sources
Beta strandi60 – 678Combined sources
Beta strandi70 – 778Combined sources
Beta strandi78 – 814Combined sources
Beta strandi83 – 908Combined sources
Beta strandi95 – 973Combined sources
Helixi100 – 1045Combined sources
Helixi107 – 1137Combined sources
Beta strandi114 – 1163Combined sources
Helixi118 – 1269Combined sources
Turni130 – 1334Combined sources
Turni134 – 1363Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44T1-146[»]
1VY4X-ray2.60T1-146[»]
1VY5X-ray2.55T1-146[»]
1VY6X-ray2.90T1-146[»]
1VY7X-ray2.80T1-146[»]
4L47X-ray3.22T1-146[»]
4L71X-ray3.90T1-146[»]
4LELX-ray3.90T1-146[»]
4LFZX-ray3.92T1-146[»]
4LNTX-ray2.94T1-146[»]
4LSKX-ray3.48T1-146[»]
4LT8X-ray3.14T1-146[»]
4P6FX-ray3.60O1-146[»]
4P70X-ray3.68T1-146[»]
4V42X-ray5.50R1-146[»]
4V4PX-ray5.50R1-146[»]
4V4XX-ray5.00S1-146[»]
4V4YX-ray5.50S1-146[»]
4V4ZX-ray4.51S1-146[»]
4V51X-ray2.80T1-146[»]
4V5AX-ray3.80T1-146[»]
4V5CX-ray3.30T1-146[»]
4V5EX-ray3.45T1-146[»]
4V5FX-ray3.60T1-146[»]
4V5GX-ray3.60T1-146[»]
4V5JX-ray3.10T1-146[»]
4V5KX-ray3.20T1-146[»]
4V5LX-ray3.10T1-146[»]
4V5Melectron microscopy7.80T1-146[»]
4V5Nelectron microscopy7.60T1-146[»]
4V5PX-ray3.10T1-146[»]
4V5QX-ray3.10T1-146[»]
4V5RX-ray3.10T1-146[»]
4V5SX-ray3.10T1-146[»]
4V68electron microscopy6.40T1-138[»]
4V6AX-ray3.10T1-146[»]
4V6FX-ray3.10R1-146[»]
4V6GX-ray3.50R1-146[»]
4V7JX-ray3.30T1-146[»]
4V7KX-ray3.60T1-146[»]
4V7LX-ray3.00T1-146[»]
4V7MX-ray3.45T1-146[»]
4V7WX-ray3.00T1-146[»]
4V7ZX-ray3.10T1-146[»]
4V87X-ray3.10R1-137[»]
4V8AX-ray3.20T1-146[»]
4V8BX-ray3.00R1-146[»]
4V8CX-ray3.30R1-146[»]
4V8DX-ray3.00R1-146[»]
4V8EX-ray3.30R1-146[»]
4V8FX-ray3.30R1-146[»]
4V8GX-ray3.00T1-146[»]
4V8HX-ray3.10T1-146[»]
4V8IX-ray2.70T1-146[»]
4V8JX-ray3.90T1-146[»]
4V8NX-ray3.10T1-146[»]
4V8OX-ray3.80T1-146[»]
4V8QX-ray3.10T1-146[»]
4V8UX-ray3.70T1-146[»]
4V8XX-ray3.35T1-146[»]
4V90X-ray2.95T1-146[»]
4V95X-ray3.20T1-146[»]
4V97X-ray3.52T1-146[»]
4V9AX-ray3.30R1-146[»]
4V9BX-ray3.10R1-146[»]
4V9HX-ray2.86T1-146[»]
4V9IX-ray3.30T1-137[»]
4V9RX-ray3.00T1-146[»]
4V9SX-ray3.10T1-146[»]
4W2EX-ray2.90T1-146[»]
4W2FX-ray2.40T1-146[»]
4W2GX-ray2.55T1-146[»]
4W2HX-ray2.70T1-146[»]
4W2IX-ray2.70T1-146[»]
ProteinModelPortaliP60490.
SMRiP60490. Positions 1-137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60490.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L19P family.Curated

Phylogenomic databases

eggNOGiCOG0335.
HOGENOMiHOG000016265.
KOiK02884.
OMAiLVESRYV.
OrthoDBiEOG6DZF5W.
PhylomeDBiP60490.

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.

P60490-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRGALIKLV ESRYVRTDLP EFRPGDTVRV SYKVKEGNRT RIQDFEGIVI
60 70 80 90 100
RIRRNGFNTT FTVRKVSYGV GVERIFPLHS PLIQKIDIVQ RGRARRAKLY
110 120 130 140
FIRNLSDREI RRKLRADRKR IDQDRAAERA AKEEAQKAQE PKASQE
Length:146
Mass (Da):17,152
Last modified:March 29, 2005 - v2
Checksum:i119CC349889AF6A7
GO

Mass spectrometryi

Molecular mass is 17152 Da from positions 1 - 146. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70854.1.
RefSeqiYP_144297.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70854; BAD70854; BAD70854.
GeneIDi3168297.
KEGGittj:TTHA1031.
PATRICi23957022. VBITheThe93045_1011.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70854.1.
RefSeqiYP_144297.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44T1-146[»]
1VY4X-ray2.60T1-146[»]
1VY5X-ray2.55T1-146[»]
1VY6X-ray2.90T1-146[»]
1VY7X-ray2.80T1-146[»]
4L47X-ray3.22T1-146[»]
4L71X-ray3.90T1-146[»]
4LELX-ray3.90T1-146[»]
4LFZX-ray3.92T1-146[»]
4LNTX-ray2.94T1-146[»]
4LSKX-ray3.48T1-146[»]
4LT8X-ray3.14T1-146[»]
4P6FX-ray3.60O1-146[»]
4P70X-ray3.68T1-146[»]
4V42X-ray5.50R1-146[»]
4V4PX-ray5.50R1-146[»]
4V4XX-ray5.00S1-146[»]
4V4YX-ray5.50S1-146[»]
4V4ZX-ray4.51S1-146[»]
4V51X-ray2.80T1-146[»]
4V5AX-ray3.80T1-146[»]
4V5CX-ray3.30T1-146[»]
4V5EX-ray3.45T1-146[»]
4V5FX-ray3.60T1-146[»]
4V5GX-ray3.60T1-146[»]
4V5JX-ray3.10T1-146[»]
4V5KX-ray3.20T1-146[»]
4V5LX-ray3.10T1-146[»]
4V5Melectron microscopy7.80T1-146[»]
4V5Nelectron microscopy7.60T1-146[»]
4V5PX-ray3.10T1-146[»]
4V5QX-ray3.10T1-146[»]
4V5RX-ray3.10T1-146[»]
4V5SX-ray3.10T1-146[»]
4V68electron microscopy6.40T1-138[»]
4V6AX-ray3.10T1-146[»]
4V6FX-ray3.10R1-146[»]
4V6GX-ray3.50R1-146[»]
4V7JX-ray3.30T1-146[»]
4V7KX-ray3.60T1-146[»]
4V7LX-ray3.00T1-146[»]
4V7MX-ray3.45T1-146[»]
4V7WX-ray3.00T1-146[»]
4V7ZX-ray3.10T1-146[»]
4V87X-ray3.10R1-137[»]
4V8AX-ray3.20T1-146[»]
4V8BX-ray3.00R1-146[»]
4V8CX-ray3.30R1-146[»]
4V8DX-ray3.00R1-146[»]
4V8EX-ray3.30R1-146[»]
4V8FX-ray3.30R1-146[»]
4V8GX-ray3.00T1-146[»]
4V8HX-ray3.10T1-146[»]
4V8IX-ray2.70T1-146[»]
4V8JX-ray3.90T1-146[»]
4V8NX-ray3.10T1-146[»]
4V8OX-ray3.80T1-146[»]
4V8QX-ray3.10T1-146[»]
4V8UX-ray3.70T1-146[»]
4V8XX-ray3.35T1-146[»]
4V90X-ray2.95T1-146[»]
4V95X-ray3.20T1-146[»]
4V97X-ray3.52T1-146[»]
4V9AX-ray3.30R1-146[»]
4V9BX-ray3.10R1-146[»]
4V9HX-ray2.86T1-146[»]
4V9IX-ray3.30T1-137[»]
4V9RX-ray3.00T1-146[»]
4V9SX-ray3.10T1-146[»]
4W2EX-ray2.90T1-146[»]
4W2FX-ray2.40T1-146[»]
4W2GX-ray2.55T1-146[»]
4W2HX-ray2.70T1-146[»]
4W2IX-ray2.70T1-146[»]
ProteinModelPortaliP60490.
SMRiP60490. Positions 1-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1031.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70854; BAD70854; BAD70854.
GeneIDi3168297.
KEGGittj:TTHA1031.
PATRICi23957022. VBITheThe93045_1011.

Phylogenomic databases

eggNOGiCOG0335.
HOGENOMiHOG000016265.
KOiK02884.
OMAiLVESRYV.
OrthoDBiEOG6DZF5W.
PhylomeDBiP60490.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1063-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60490.

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. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Identification of the 50S ribosomal proteins from the eubacterium Thermus thermophilus."
    Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., Choli-Papadopoulou T.
    Biol. Chem. 381:1079-1087(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-29.
  3. "Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry."
    Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.
    Proteomics 5:4818-4831(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
  4. "The path of messenger RNA through the ribosome."
    Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F.
    Cell 106:233-241(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME, INTERSUBUNIT BRIDGE FORMATION.

Entry informationi

Entry nameiRL19_THET8
AccessioniPrimary (citable) accession number: P60490
Secondary accession number(s): Q5SJH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 29, 2005
Last modified: April 1, 2015
This is version 99 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. 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.