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Protein

50S ribosomal protein L17

Gene

rplQ

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1702-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L17UniRule annotation
Gene namesi
Name:rplQUniRule annotation
Synonyms:rpl17UniRule annotation
Ordered Locus Names:TTHA1663
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11811850S ribosomal protein L17PRO_0000175547Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts protein L32.UniRule annotation

Protein-protein interaction databases

STRINGi300852.TTHA1663.

Structurei

Secondary structure

1
118
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 3117Combined sources
Beta strandi32 – 376Combined sources
Helixi38 – 5720Combined sources
Helixi60 – 6910Combined sources
Helixi73 – 819Combined sources
Helixi83 – 864Combined sources
Beta strandi95 – 1039Combined sources
Turni105 – 1073Combined sources
Beta strandi110 – 1167Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GD8X-ray2.30A/B/C/D/E/F/G/H/I1-118[»]
1VVJX-ray3.44RR/YR1-118[»]
1VY4X-ray2.60BR/DR1-118[»]
1VY5X-ray2.55BR/DR1-118[»]
1VY6X-ray2.90BR/DR1-118[»]
1VY7X-ray2.80BR/DR1-118[»]
4L47X-ray3.22RR/YR1-118[»]
4L71X-ray3.90RR/YR1-118[»]
4LELX-ray3.90RR/YR1-118[»]
4LFZX-ray3.92RR/YR1-118[»]
4LNTX-ray2.94RR/YR1-118[»]
4LSKX-ray3.48RR/YR1-118[»]
4LT8X-ray3.14RR/YR1-118[»]
4P6FX-ray3.60RR/YR1-118[»]
4P70X-ray3.68RR/YR1-118[»]
4TUAX-ray3.60RR/YR1-118[»]
4TUBX-ray3.60RR/YR1-118[»]
4TUCX-ray3.60RR/YR1-118[»]
4TUDX-ray3.60RR/YR1-118[»]
4TUEX-ray3.50RR/YR1-118[»]
4V4PX-ray5.50A01-118[»]
4V4RX-ray5.90BR1-118[»]
4V4SX-ray6.76BR1-118[»]
4V4TX-ray6.46BR1-118[»]
4V4XX-ray5.00BQ1-118[»]
4V4YX-ray5.50BQ1-118[»]
4V4ZX-ray4.51BQ1-118[»]
4V51X-ray2.80BR/DR1-118[»]
4V5AX-ray3.50BR/DR1-118[»]
4V5CX-ray3.30BR/DR1-118[»]
4V5DX-ray3.50BR/DR1-118[»]
4V5EX-ray3.45BR/DR1-118[»]
4V5FX-ray3.60BR/DR1-118[»]
4V5GX-ray3.60BR/DR1-118[»]
4V5JX-ray3.10BR/DR1-118[»]
4V5KX-ray3.20BR/DR1-118[»]
4V5LX-ray3.10BR1-118[»]
4V5Melectron microscopy7.80BR1-118[»]
4V5Nelectron microscopy7.60BR1-118[»]
4V5PX-ray3.10BR/DR1-118[»]
4V5QX-ray3.10BR/DR1-118[»]
4V5RX-ray3.10BR/DR1-118[»]
4V5SX-ray3.10BR/DR1-118[»]
4V68electron microscopy6.40BR2-118[»]
4V6AX-ray3.10BR/DR1-118[»]
4V6FX-ray3.10A0/D01-118[»]
4V6GX-ray3.50B0/D01-118[»]
4V7JX-ray3.30AR/BR1-118[»]
4V7KX-ray3.60AR/BR1-118[»]
4V7LX-ray3.00BR/DR1-118[»]
4V7MX-ray3.45BR/DR1-118[»]
4V7WX-ray3.00BR/DR1-118[»]
4V7XX-ray3.00BR/DR1-118[»]
4V7YX-ray3.00BR/DR1-118[»]
4V7ZX-ray3.10BR/DR1-118[»]
4V87X-ray3.10A0/D01-118[»]
4V8AX-ray3.20AR/BR1-118[»]
4V8BX-ray3.00B0/D01-118[»]
4V8CX-ray3.30A0/B01-118[»]
4V8DX-ray3.00B0/D01-118[»]
4V8EX-ray3.30A0/C01-118[»]
4V8FX-ray3.30A0/D01-118[»]
4V8GX-ray3.00BR/DR1-118[»]
4V8HX-ray3.10BR/DR1-118[»]
4V8IX-ray2.70BR/DR1-118[»]
4V8JX-ray3.90BR/DR1-118[»]
4V8NX-ray3.10BR/DR1-118[»]
4V8OX-ray3.80BR1-118[»]
4V8QX-ray3.10AR1-118[»]
4V8UX-ray3.70BR/DR1-118[»]
4V8XX-ray3.35BR/DR1-118[»]
4V90X-ray2.95BR2-118[»]
4V95X-ray3.20BR/DR1-118[»]
4V97X-ray3.52BR/DR1-118[»]
4V9AX-ray3.30B0/D01-118[»]
4V9BX-ray3.10B0/D01-118[»]
4V9HX-ray2.86BR1-118[»]
4V9IX-ray3.30BR/DR2-118[»]
4V9RX-ray3.00BR/DR1-118[»]
4V9SX-ray3.10BR/DR1-118[»]
4W2EX-ray2.90R1-118[»]
4W2FX-ray2.40BR/DR1-118[»]
4W2GX-ray2.55BR/DR1-118[»]
4W2HX-ray2.70BR/DR1-118[»]
4W2IX-ray2.70BR/DR1-118[»]
4WPOX-ray2.80AR/CR1-118[»]
4WQFX-ray2.80AR/CR1-118[»]
4WQUX-ray2.80AR/CR1-118[»]
4WQYX-ray2.80AR/CR1-118[»]
4WWEX-ray3.40Q2-118[»]
4Y4OX-ray2.301R/2R1-118[»]
4Y4PX-ray2.501R/2R1-118[»]
4Z3QX-ray2.601R/2R1-118[»]
4Z3RX-ray3.101R/2R1-118[»]
4Z3SX-ray2.651R/2R1-118[»]
4Z8CX-ray2.901R/2R1-118[»]
4ZERX-ray3.101R/2R1-118[»]
ProteinModelPortaliQ9Z9H5.
SMRiQ9Z9H5. Positions 1-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z9H5.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L17P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0203.
HOGENOMiHOG000019780.
KOiK02879.
OMAiKTVQRRG.
OrthoDBiEOG6GR3GR.
PhylomeDBiQ9Z9H5.

Family and domain databases

Gene3Di3.90.1030.10. 1 hit.
HAMAPiMF_01368. Ribosomal_L17.
InterProiIPR000456. Ribosomal_L17.
[Graphical view]
PANTHERiPTHR14413. PTHR14413. 1 hit.
PfamiPF01196. Ribosomal_L17. 1 hit.
[Graphical view]
SUPFAMiSSF64263. SSF64263. 1 hit.
TIGRFAMsiTIGR00059. L17. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Z9H5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRHLKSGRKL NRHSSHRLAL YRNQAKSLLT HGRITTTVPK AKELRGFVDH
60 70 80 90 100
LIHLAKRGDL HARRLVLRDL QDVKLVRKLF DEIAPRYRDR QGGYTRVLKL
110
AERRRGDGAP LALVELVE
Length:118
Mass (Da):13,715
Last modified:May 1, 1999 - v1
Checksum:iC9B8DD552F6C42AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31H → A AA sequence (PubMed:11154066).Curated
Sequence conflicti13 – 131H → A AA sequence (PubMed:11154066).Curated

Mass spectrometryi

Molecular mass is 13717 Da from positions 1 - 118. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024328 Genomic DNA. Translation: BAA75550.1.
AP008226 Genomic DNA. Translation: BAD71486.1.
RefSeqiWP_008633358.1. NC_006461.1.
YP_144929.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71486; BAD71486; BAD71486.
GeneIDi3168022.
KEGGittj:TTHA1663.
PATRICi23958281. VBITheThe93045_1633.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024328 Genomic DNA. Translation: BAA75550.1.
AP008226 Genomic DNA. Translation: BAD71486.1.
RefSeqiWP_008633358.1. NC_006461.1.
YP_144929.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GD8X-ray2.30A/B/C/D/E/F/G/H/I1-118[»]
1VVJX-ray3.44RR/YR1-118[»]
1VY4X-ray2.60BR/DR1-118[»]
1VY5X-ray2.55BR/DR1-118[»]
1VY6X-ray2.90BR/DR1-118[»]
1VY7X-ray2.80BR/DR1-118[»]
4L47X-ray3.22RR/YR1-118[»]
4L71X-ray3.90RR/YR1-118[»]
4LELX-ray3.90RR/YR1-118[»]
4LFZX-ray3.92RR/YR1-118[»]
4LNTX-ray2.94RR/YR1-118[»]
4LSKX-ray3.48RR/YR1-118[»]
4LT8X-ray3.14RR/YR1-118[»]
4P6FX-ray3.60RR/YR1-118[»]
4P70X-ray3.68RR/YR1-118[»]
4TUAX-ray3.60RR/YR1-118[»]
4TUBX-ray3.60RR/YR1-118[»]
4TUCX-ray3.60RR/YR1-118[»]
4TUDX-ray3.60RR/YR1-118[»]
4TUEX-ray3.50RR/YR1-118[»]
4V4PX-ray5.50A01-118[»]
4V4RX-ray5.90BR1-118[»]
4V4SX-ray6.76BR1-118[»]
4V4TX-ray6.46BR1-118[»]
4V4XX-ray5.00BQ1-118[»]
4V4YX-ray5.50BQ1-118[»]
4V4ZX-ray4.51BQ1-118[»]
4V51X-ray2.80BR/DR1-118[»]
4V5AX-ray3.50BR/DR1-118[»]
4V5CX-ray3.30BR/DR1-118[»]
4V5DX-ray3.50BR/DR1-118[»]
4V5EX-ray3.45BR/DR1-118[»]
4V5FX-ray3.60BR/DR1-118[»]
4V5GX-ray3.60BR/DR1-118[»]
4V5JX-ray3.10BR/DR1-118[»]
4V5KX-ray3.20BR/DR1-118[»]
4V5LX-ray3.10BR1-118[»]
4V5Melectron microscopy7.80BR1-118[»]
4V5Nelectron microscopy7.60BR1-118[»]
4V5PX-ray3.10BR/DR1-118[»]
4V5QX-ray3.10BR/DR1-118[»]
4V5RX-ray3.10BR/DR1-118[»]
4V5SX-ray3.10BR/DR1-118[»]
4V68electron microscopy6.40BR2-118[»]
4V6AX-ray3.10BR/DR1-118[»]
4V6FX-ray3.10A0/D01-118[»]
4V6GX-ray3.50B0/D01-118[»]
4V7JX-ray3.30AR/BR1-118[»]
4V7KX-ray3.60AR/BR1-118[»]
4V7LX-ray3.00BR/DR1-118[»]
4V7MX-ray3.45BR/DR1-118[»]
4V7WX-ray3.00BR/DR1-118[»]
4V7XX-ray3.00BR/DR1-118[»]
4V7YX-ray3.00BR/DR1-118[»]
4V7ZX-ray3.10BR/DR1-118[»]
4V87X-ray3.10A0/D01-118[»]
4V8AX-ray3.20AR/BR1-118[»]
4V8BX-ray3.00B0/D01-118[»]
4V8CX-ray3.30A0/B01-118[»]
4V8DX-ray3.00B0/D01-118[»]
4V8EX-ray3.30A0/C01-118[»]
4V8FX-ray3.30A0/D01-118[»]
4V8GX-ray3.00BR/DR1-118[»]
4V8HX-ray3.10BR/DR1-118[»]
4V8IX-ray2.70BR/DR1-118[»]
4V8JX-ray3.90BR/DR1-118[»]
4V8NX-ray3.10BR/DR1-118[»]
4V8OX-ray3.80BR1-118[»]
4V8QX-ray3.10AR1-118[»]
4V8UX-ray3.70BR/DR1-118[»]
4V8XX-ray3.35BR/DR1-118[»]
4V90X-ray2.95BR2-118[»]
4V95X-ray3.20BR/DR1-118[»]
4V97X-ray3.52BR/DR1-118[»]
4V9AX-ray3.30B0/D01-118[»]
4V9BX-ray3.10B0/D01-118[»]
4V9HX-ray2.86BR1-118[»]
4V9IX-ray3.30BR/DR2-118[»]
4V9RX-ray3.00BR/DR1-118[»]
4V9SX-ray3.10BR/DR1-118[»]
4W2EX-ray2.90R1-118[»]
4W2FX-ray2.40BR/DR1-118[»]
4W2GX-ray2.55BR/DR1-118[»]
4W2HX-ray2.70BR/DR1-118[»]
4W2IX-ray2.70BR/DR1-118[»]
4WPOX-ray2.80AR/CR1-118[»]
4WQFX-ray2.80AR/CR1-118[»]
4WQUX-ray2.80AR/CR1-118[»]
4WQYX-ray2.80AR/CR1-118[»]
4WWEX-ray3.40Q2-118[»]
4Y4OX-ray2.301R/2R1-118[»]
4Y4PX-ray2.501R/2R1-118[»]
4Z3QX-ray2.601R/2R1-118[»]
4Z3RX-ray3.101R/2R1-118[»]
4Z3SX-ray2.651R/2R1-118[»]
4Z8CX-ray2.901R/2R1-118[»]
4ZERX-ray3.101R/2R1-118[»]
ProteinModelPortaliQ9Z9H5.
SMRiQ9Z9H5. Positions 1-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1663.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71486; BAD71486; BAD71486.
GeneIDi3168022.
KEGGittj:TTHA1663.
PATRICi23958281. VBITheThe93045_1633.

Phylogenomic databases

eggNOGiCOG0203.
HOGENOMiHOG000019780.
KOiK02879.
OMAiKTVQRRG.
OrthoDBiEOG6GR3GR.
PhylomeDBiQ9Z9H5.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1702-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9Z9H5.

Family and domain databases

Gene3Di3.90.1030.10. 1 hit.
HAMAPiMF_01368. Ribosomal_L17.
InterProiIPR000456. Ribosomal_L17.
[Graphical view]
PANTHERiPTHR14413. PTHR14413. 1 hit.
PfamiPF01196. Ribosomal_L17. 1 hit.
[Graphical view]
SUPFAMiSSF64263. SSF64263. 1 hit.
TIGRFAMsiTIGR00059. L17. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the RNA polymerase alpha subunit gene from Thermus thermophilus HB8 and characterization of the protein."
    Wada T., Yamazaki T., Kuramitsu S., Kyogoku Y.
    J. Biochem. 125:143-150(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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 (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  3. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-15.
  4. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
  5. "The crystal structure of the bacteria-specific L17 ribosomal protein from Thermus thermophilus."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JAN-2003) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-118.
  6. "Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon."
    Petry S., Brodersen D.E., Murphy F.V. IV, Dunham C.M., Selmer M., Tarry M.J., Kelley A.C., Ramakrishnan V.
    Cell 123:1255-1266(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.9 ANGSTROMS) OF 1-118 OF THE RIBOSOME ALONE OR IN COMPLEX WITH RELEASE FACTOR 1 OR RELEASE FACTOR 2.
  7. "Translational operator of mRNA on the ribosome: how repressor proteins exclude ribosome binding."
    Jenner L., Romby P., Rees B., Schulze-Briese C., Springer M., Ehresmann C., Ehresmann B., Moras D., Yusupova G., Yusupov M.
    Science 308:120-123(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF 14-118.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-118 OF THE RIBOSOME.

Entry informationi

Entry nameiRL17_THET8
AccessioniPrimary (citable) accession number: Q9Z9H5
Secondary accession number(s): Q5SHR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: July 22, 2015
This is version 113 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. 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.