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Q5SLP7

- RL1_THET8

UniProt

Q5SLP7 - RL1_THET8

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Protein
50S ribosomal protein L1
Gene
rplA, TTHA0246
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Directly binds to 23S rRNA. Forms what is known as the L1 stalk, which protrudes beyond the 70S ribosome surface. The stalk is preferentially stabilized in 70S versus 50S crystals. Interacts with the E site tRNA, blocking the exit path. This blockage implies that this section of the ribosome must be able to move to release the deacetylated tRNA.UniRule annotation
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA By similarity.UniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. regulation of translation Source: UniProtKB-KW
  2. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-256-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L1
Gene namesi
Name:rplA
Ordered Locus Names:TTHA0246
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. large ribosomal subunit Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 22922850S ribosomal protein L1UniRule annotation
PRO_0000125764Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

STRINGi300852.TTHA0246.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 127
Turni13 – 153
Beta strandi17 – 193
Turni20 – 223
Helixi23 – 3210
Beta strandi36 – 383
Beta strandi41 – 5010
Beta strandi52 – 543
Helixi55 – 573
Beta strandi60 – 645
Helixi70 – 723
Beta strandi75 – 784
Beta strandi79 – 813
Helixi82 – 898
Beta strandi93 – 964
Helixi98 – 1003
Helixi101 – 1055
Turni108 – 1103
Beta strandi112 – 1165
Helixi118 – 1203
Helixi121 – 13212
Turni133 – 1364
Helixi141 – 1433
Beta strandi146 – 1483
Helixi150 – 1578
Beta strandi161 – 1655
Beta strandi170 – 1789
Beta strandi179 – 1813
Helixi183 – 19917
Beta strandi204 – 2063
Beta strandi209 – 2179
Beta strandi218 – 2203
Beta strandi222 – 2254

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GIYX-ray5.50C2-229[»]
1YL3X-ray5.50C2-229[»]
2HGJX-ray5.00C1-229[»]
2HGQX-ray5.50C1-229[»]
2HGUX-ray4.51C1-229[»]
2J01X-ray2.80C2-229[»]
2J03X-ray2.80C2-229[»]
2OM7electron microscopy7.30K1-229[»]
2V47X-ray3.50C2-229[»]
2V49X-ray3.50C2-229[»]
2WDIX-ray3.30C1-229[»]
2WDJX-ray3.30C1-229[»]
2WDLX-ray3.50C1-229[»]
2WDNX-ray3.50C1-229[»]
2WH2X-ray3.45C1-229[»]
2WH4X-ray3.45C1-229[»]
2WRJX-ray3.60C1-229[»]
2WRLX-ray3.60C1-229[»]
2WROX-ray3.60C1-229[»]
2WRRX-ray3.60C1-229[»]
2X9SX-ray3.10C1-229[»]
2X9UX-ray3.10C1-229[»]
2XG0X-ray3.20C1-229[»]
2XG2X-ray3.20C1-229[»]
2XQEX-ray3.10C1-229[»]
2XTGelectron microscopy7.80C1-229[»]
2XUXelectron microscopy7.60C1-229[»]
2Y0VX-ray3.10C1-229[»]
2Y0XX-ray3.10C1-229[»]
2Y0ZX-ray3.10C1-229[»]
2Y11X-ray3.10C1-229[»]
2Y13X-ray3.10C1-229[»]
2Y15X-ray3.10C1-229[»]
2Y17X-ray3.10C1-229[»]
2Y19X-ray3.10C1-229[»]
3FINelectron microscopy6.40C19-225[»]
3HUXX-ray3.10C1-229[»]
3HUZX-ray3.10C1-229[»]
3KIRX-ray3.30C1-229[»]
3KITX-ray3.30C1-229[»]
3KIWX-ray3.60C1-229[»]
3KIYX-ray3.60C1-229[»]
3KNIX-ray3.00C1-229[»]
3KNKX-ray3.00C1-229[»]
3KNMX-ray3.45C1-229[»]
3KNOX-ray3.45C1-229[»]
3TG8X-ray1.95A1-229[»]
3V6WX-ray3.90C1-229[»]
3V6XX-ray3.90C1-229[»]
3ZN9X-ray3.10C1-229[»]
3ZNEX-ray3.10C1-229[»]
3ZVPX-ray3.80C1-229[»]
4ABSX-ray3.10C1-229[»]
4B8GX-ray3.70C1-229[»]
4B8IX-ray3.70C1-229[»]
4BTDX-ray2.95C2-229[»]
4BYCX-ray3.35C1-229[»]
4BYEX-ray3.35C1-229[»]
4EJBX-ray3.52C1-229[»]
4EJCX-ray3.52C1-229[»]
4JUXX-ray2.86C1-229[»]
4K0MX-ray3.30C19-102[»]
4K0QX-ray3.30C19-102[»]
ProteinModelPortaliQ5SLP7.
SMRiQ5SLP7. Positions 2-229.

Miscellaneous databases

EvolutionaryTraceiQ5SLP7.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0081.
HOGENOMiHOG000207015.
KOiK02863.
OMAiNEGWTDF.
OrthoDBiEOG6FBX2G.
PhylomeDBiQ5SLP7.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPiMF_01318_B. Ribosomal_L1_B.
InterProiIPR005878. Ribosom_L1_bac-type.
IPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
[Graphical view]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
TIGRFAMsiTIGR01169. rplA_bact. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5SLP7-1 [UniParc]FASTAAdd to Basket

« Hide

MPKHGKRYRA LLEKVDPNKV YTIDEAARLV KELATAKFDE TVEVHAKLGI    50
DPRRSDQNVR GTVSLPHGLG KQVRVLAIAK GEKIKEAEEA GADYVGGEEI 100
IQKILDGWMD FDAVVATPDV MGAVGSKLGR ILGPRGLLPN PKAGTVGFNI 150
GEIIREIKAG RIEFRNDKTG AIHAPVGKAS FPPEKLADNI RAFIRALEAH 200
KPEGAKGTFL RSVYVTTTMG PSVRINPHS 229
Length:229
Mass (Da):24,831
Last modified:January 23, 2007 - v3
Checksum:i99EE7BE00801B1B4
GO

Mass spectrometryi

Molecular mass is 24698 Da from positions 2 - 229. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD70069.1.
RefSeqiWP_011227804.1. NC_006461.1.
YP_143512.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70069; BAD70069; BAD70069.
GeneIDi3168861.
KEGGittj:TTHA0246.
PATRICi23955439. VBITheThe93045_0246.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008226 Genomic DNA. Translation: BAD70069.1 .
RefSeqi WP_011227804.1. NC_006461.1.
YP_143512.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GIY X-ray 5.50 C 2-229 [» ]
1YL3 X-ray 5.50 C 2-229 [» ]
2HGJ X-ray 5.00 C 1-229 [» ]
2HGQ X-ray 5.50 C 1-229 [» ]
2HGU X-ray 4.51 C 1-229 [» ]
2J01 X-ray 2.80 C 2-229 [» ]
2J03 X-ray 2.80 C 2-229 [» ]
2OM7 electron microscopy 7.30 K 1-229 [» ]
2V47 X-ray 3.50 C 2-229 [» ]
2V49 X-ray 3.50 C 2-229 [» ]
2WDI X-ray 3.30 C 1-229 [» ]
2WDJ X-ray 3.30 C 1-229 [» ]
2WDL X-ray 3.50 C 1-229 [» ]
2WDN X-ray 3.50 C 1-229 [» ]
2WH2 X-ray 3.45 C 1-229 [» ]
2WH4 X-ray 3.45 C 1-229 [» ]
2WRJ X-ray 3.60 C 1-229 [» ]
2WRL X-ray 3.60 C 1-229 [» ]
2WRO X-ray 3.60 C 1-229 [» ]
2WRR X-ray 3.60 C 1-229 [» ]
2X9S X-ray 3.10 C 1-229 [» ]
2X9U X-ray 3.10 C 1-229 [» ]
2XG0 X-ray 3.20 C 1-229 [» ]
2XG2 X-ray 3.20 C 1-229 [» ]
2XQE X-ray 3.10 C 1-229 [» ]
2XTG electron microscopy 7.80 C 1-229 [» ]
2XUX electron microscopy 7.60 C 1-229 [» ]
2Y0V X-ray 3.10 C 1-229 [» ]
2Y0X X-ray 3.10 C 1-229 [» ]
2Y0Z X-ray 3.10 C 1-229 [» ]
2Y11 X-ray 3.10 C 1-229 [» ]
2Y13 X-ray 3.10 C 1-229 [» ]
2Y15 X-ray 3.10 C 1-229 [» ]
2Y17 X-ray 3.10 C 1-229 [» ]
2Y19 X-ray 3.10 C 1-229 [» ]
3FIN electron microscopy 6.40 C 19-225 [» ]
3HUX X-ray 3.10 C 1-229 [» ]
3HUZ X-ray 3.10 C 1-229 [» ]
3KIR X-ray 3.30 C 1-229 [» ]
3KIT X-ray 3.30 C 1-229 [» ]
3KIW X-ray 3.60 C 1-229 [» ]
3KIY X-ray 3.60 C 1-229 [» ]
3KNI X-ray 3.00 C 1-229 [» ]
3KNK X-ray 3.00 C 1-229 [» ]
3KNM X-ray 3.45 C 1-229 [» ]
3KNO X-ray 3.45 C 1-229 [» ]
3TG8 X-ray 1.95 A 1-229 [» ]
3V6W X-ray 3.90 C 1-229 [» ]
3V6X X-ray 3.90 C 1-229 [» ]
3ZN9 X-ray 3.10 C 1-229 [» ]
3ZNE X-ray 3.10 C 1-229 [» ]
3ZVP X-ray 3.80 C 1-229 [» ]
4ABS X-ray 3.10 C 1-229 [» ]
4B8G X-ray 3.70 C 1-229 [» ]
4B8I X-ray 3.70 C 1-229 [» ]
4BTD X-ray 2.95 C 2-229 [» ]
4BYC X-ray 3.35 C 1-229 [» ]
4BYE X-ray 3.35 C 1-229 [» ]
4EJB X-ray 3.52 C 1-229 [» ]
4EJC X-ray 3.52 C 1-229 [» ]
4JUX X-ray 2.86 C 1-229 [» ]
4K0M X-ray 3.30 C 19-102 [» ]
4K0Q X-ray 3.30 C 19-102 [» ]
ProteinModelPortali Q5SLP7.
SMRi Q5SLP7. Positions 2-229.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA0246.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD70069 ; BAD70069 ; BAD70069 .
GeneIDi 3168861.
KEGGi ttj:TTHA0246.
PATRICi 23955439. VBITheThe93045_0246.

Phylogenomic databases

eggNOGi COG0081.
HOGENOMi HOG000207015.
KOi K02863.
OMAi NEGWTDF.
OrthoDBi EOG6FBX2G.
PhylomeDBi Q5SLP7.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-256-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q5SLP7.

Family and domain databases

Gene3Di 3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPi MF_01318_B. Ribosomal_L1_B.
InterProi IPR005878. Ribosom_L1_bac-type.
IPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
[Graphical view ]
Pfami PF00687. Ribosomal_L1. 1 hit.
[Graphical view ]
PIRSFi PIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMi SSF56808. SSF56808. 1 hit.
TIGRFAMsi TIGR01169. rplA_bact. 1 hit.
PROSITEi PS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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 2-26.
  3. "Identification of the gene encoding transcription factor NusG of Thermus thermophilus."
    Heinrich T., Schroeder W., Erdmann V.A., Hartmann R.K.
    J. Bacteriol. 174:7859-7863(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-181.
    Strain: HB8 / ATCC 27634 / DSM 579.
  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 nameiRL1_THET8
AccessioniPrimary (citable) accession number: Q5SLP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 89 of the entry and version 3 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

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