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Protein

50S ribosomal protein L29

Gene

rpmC

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

One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.

GO - Molecular functioni

  1. structural constituent of ribosome Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1723-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L29
Gene namesi
Name:rpmC
Ordered Locus Names:TTHA1684
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: 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 – 727250S ribosomal protein L29PRO_0000130483Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

STRINGi300852.TTHA1684.

Structurei

Secondary structure

1
72
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1513Combined sources
Helixi18 – 4023Combined sources
Turni42 – 443Combined sources
Helixi45 – 473Combined sources
Helixi48 – 6821Combined sources
Turni69 – 713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.4421-72[»]
1VY4X-ray2.6021-72[»]
1VY5X-ray2.5521-72[»]
1VY6X-ray2.9021-72[»]
1VY7X-ray2.8021-72[»]
4L47X-ray3.2221-72[»]
4L71X-ray3.9021-72[»]
4LELX-ray3.9021-72[»]
4LFZX-ray3.9221-72[»]
4LNTX-ray2.9421-72[»]
4LSKX-ray3.4821-72[»]
4LT8X-ray3.1421-72[»]
4P6FX-ray3.60X1-72[»]
4P70X-ray3.6821-72[»]
4V42X-ray5.50W1-72[»]
4V4PX-ray5.50W1-72[»]
4V4XX-ray5.0017-72[»]
4V4YX-ray5.5011-72[»]
4V4ZX-ray4.5111-72[»]
4V51X-ray2.8021-72[»]
4V5AX-ray3.8021-72[»]
4V5CX-ray3.3021-72[»]
4V5DX-ray3.5021-72[»]
4V5EX-ray3.4521-72[»]
4V5FX-ray3.6021-72[»]
4V5GX-ray3.6021-72[»]
4V5JX-ray3.1021-72[»]
4V5KX-ray3.2021-72[»]
4V5LX-ray3.1021-72[»]
4V5Melectron microscopy7.8021-72[»]
4V5Nelectron microscopy7.6021-72[»]
4V5PX-ray3.1021-72[»]
4V5QX-ray3.1021-72[»]
4V5RX-ray3.1021-72[»]
4V5SX-ray3.1021-72[»]
4V68electron microscopy6.40212-62[»]
4V6AX-ray3.1021-72[»]
4V6FX-ray3.10W1-72[»]
4V6GX-ray3.50W1-72[»]
4V7JX-ray3.3021-72[»]
4V7KX-ray3.6021-72[»]
4V7LX-ray3.0021-72[»]
4V7MX-ray3.4521-72[»]
4V7WX-ray3.0021-72[»]
4V7XX-ray3.0021-72[»]
4V7YX-ray3.0021-72[»]
4V7ZX-ray3.1021-72[»]
4V87X-ray3.10W4-72[»]
4V8AX-ray3.2021-72[»]
4V8BX-ray3.00W1-72[»]
4V8CX-ray3.30W1-72[»]
4V8DX-ray3.00W1-72[»]
4V8EX-ray3.30W1-72[»]
4V8FX-ray3.30W1-72[»]
4V8GX-ray3.0021-72[»]
4V8HX-ray3.1021-72[»]
4V8IX-ray2.7021-72[»]
4V8JX-ray3.9021-72[»]
4V8NX-ray3.1021-72[»]
4V8OX-ray3.8021-72[»]
4V8QX-ray3.1021-72[»]
4V8UX-ray3.7021-72[»]
4V8XX-ray3.3521-72[»]
4V90X-ray2.9522-72[»]
4V95X-ray3.2021-72[»]
4V97X-ray3.5221-72[»]
4V9AX-ray3.30W1-72[»]
4V9BX-ray3.10W1-72[»]
4V9HX-ray2.8621-72[»]
4V9IX-ray3.3022-72[»]
4V9RX-ray3.0021-72[»]
4V9SX-ray3.1021-72[»]
4W2EX-ray2.9021-72[»]
4W2FX-ray2.4021-72[»]
4W2GX-ray2.5521-72[»]
4W2HX-ray2.7021-72[»]
4W2IX-ray2.7021-72[»]
ProteinModelPortaliQ5SHP6.
SMRiQ5SHP6. Positions 1-62.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHP6.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L29P family.Curated

Phylogenomic databases

eggNOGideiNOG05431.
HOGENOMiHOG000248755.
KOiK02904.
OMAiGSLDQTH.
OrthoDBiEOG6VTK8Z.

Family and domain databases

Gene3Di1.10.287.310. 1 hit.
HAMAPiMF_00374. Ribosomal_L29.
InterProiIPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view]
PfamiPF00831. Ribosomal_L29. 1 hit.
[Graphical view]
SUPFAMiSSF46561. SSF46561. 1 hit.
TIGRFAMsiTIGR00012. L29. 1 hit.
PROSITEiPS00579. RIBOSOMAL_L29. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SHP6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSEVRKQL EEARKLSPVE LEKLVREKKR ELMELRFQAS IGQLSQNHKI
60 70
RDLKRQIARL LTVLNEKRRQ NA
Length:72
Mass (Da):8,650
Last modified:December 21, 2004 - v1
Checksum:iC113B72000929584
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61V → M AA sequence (PubMed:9825301).Curated
Sequence conflicti19 – 191V → M AA sequence (PubMed:9825301).Curated

Mass spectrometryi

Molecular mass is 8652 Da from positions 1 - 72. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71507.1.
RefSeqiYP_144950.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71507; BAD71507; BAD71507.
GeneIDi3169832.
KEGGittj:TTHA1684.
PATRICi23958323. VBITheThe93045_1654.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71507.1.
RefSeqiYP_144950.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.4421-72[»]
1VY4X-ray2.6021-72[»]
1VY5X-ray2.5521-72[»]
1VY6X-ray2.9021-72[»]
1VY7X-ray2.8021-72[»]
4L47X-ray3.2221-72[»]
4L71X-ray3.9021-72[»]
4LELX-ray3.9021-72[»]
4LFZX-ray3.9221-72[»]
4LNTX-ray2.9421-72[»]
4LSKX-ray3.4821-72[»]
4LT8X-ray3.1421-72[»]
4P6FX-ray3.60X1-72[»]
4P70X-ray3.6821-72[»]
4V42X-ray5.50W1-72[»]
4V4PX-ray5.50W1-72[»]
4V4XX-ray5.0017-72[»]
4V4YX-ray5.5011-72[»]
4V4ZX-ray4.5111-72[»]
4V51X-ray2.8021-72[»]
4V5AX-ray3.8021-72[»]
4V5CX-ray3.3021-72[»]
4V5DX-ray3.5021-72[»]
4V5EX-ray3.4521-72[»]
4V5FX-ray3.6021-72[»]
4V5GX-ray3.6021-72[»]
4V5JX-ray3.1021-72[»]
4V5KX-ray3.2021-72[»]
4V5LX-ray3.1021-72[»]
4V5Melectron microscopy7.8021-72[»]
4V5Nelectron microscopy7.6021-72[»]
4V5PX-ray3.1021-72[»]
4V5QX-ray3.1021-72[»]
4V5RX-ray3.1021-72[»]
4V5SX-ray3.1021-72[»]
4V68electron microscopy6.40212-62[»]
4V6AX-ray3.1021-72[»]
4V6FX-ray3.10W1-72[»]
4V6GX-ray3.50W1-72[»]
4V7JX-ray3.3021-72[»]
4V7KX-ray3.6021-72[»]
4V7LX-ray3.0021-72[»]
4V7MX-ray3.4521-72[»]
4V7WX-ray3.0021-72[»]
4V7XX-ray3.0021-72[»]
4V7YX-ray3.0021-72[»]
4V7ZX-ray3.1021-72[»]
4V87X-ray3.10W4-72[»]
4V8AX-ray3.2021-72[»]
4V8BX-ray3.00W1-72[»]
4V8CX-ray3.30W1-72[»]
4V8DX-ray3.00W1-72[»]
4V8EX-ray3.30W1-72[»]
4V8FX-ray3.30W1-72[»]
4V8GX-ray3.0021-72[»]
4V8HX-ray3.1021-72[»]
4V8IX-ray2.7021-72[»]
4V8JX-ray3.9021-72[»]
4V8NX-ray3.1021-72[»]
4V8OX-ray3.8021-72[»]
4V8QX-ray3.1021-72[»]
4V8UX-ray3.7021-72[»]
4V8XX-ray3.3521-72[»]
4V90X-ray2.9522-72[»]
4V95X-ray3.2021-72[»]
4V97X-ray3.5221-72[»]
4V9AX-ray3.30W1-72[»]
4V9BX-ray3.10W1-72[»]
4V9HX-ray2.8621-72[»]
4V9IX-ray3.3022-72[»]
4V9RX-ray3.0021-72[»]
4V9SX-ray3.1021-72[»]
4W2EX-ray2.9021-72[»]
4W2FX-ray2.4021-72[»]
4W2GX-ray2.5521-72[»]
4W2HX-ray2.7021-72[»]
4W2IX-ray2.7021-72[»]
ProteinModelPortaliQ5SHP6.
SMRiQ5SHP6. Positions 1-62.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1684.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71507; BAD71507; BAD71507.
GeneIDi3169832.
KEGGittj:TTHA1684.
PATRICi23958323. VBITheThe93045_1654.

Phylogenomic databases

eggNOGideiNOG05431.
HOGENOMiHOG000248755.
KOiK02904.
OMAiGSLDQTH.
OrthoDBiEOG6VTK8Z.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1723-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SHP6.

Family and domain databases

Gene3Di1.10.287.310. 1 hit.
HAMAPiMF_00374. Ribosomal_L29.
InterProiIPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view]
PfamiPF00831. Ribosomal_L29. 1 hit.
[Graphical view]
SUPFAMiSSF46561. SSF46561. 1 hit.
TIGRFAMsiTIGR00012. L29. 1 hit.
PROSITEiPS00579. RIBOSOMAL_L29. 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 (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Systematic, computer-assisted optimisation of the isolation of Thermus thermophilus 50S ribosomal proteins by reversed-phase high-performance liquid chromatography."
    Boysen R.I., Erdmann V.A., Hearn M.T.
    J. Biochem. Biophys. Methods 37:69-89(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-59.
  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 1-20.
  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 path of messenger RNA through the ribosome."
    Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F.
    Cell 106:233-241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.

Entry informationi

Entry nameiRL29_THET8
AccessioniPrimary (citable) accession number: Q5SHP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 21, 2004
Last modified: March 4, 2015
This is version 83 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.