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Protein

50S ribosomal protein L2

Gene

rplB

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial (By similarity). Makes several contacts with the 16S rRNA (forming bridge B7b) in the 70S ribosome.By similarity

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro
  3. transferase activity 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-1728-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L2
Gene namesi
Name:rplB
Ordered Locus Names:TTHA1689
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: 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 – 27627550S ribosomal protein L2PRO_0000129641Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. May also make transient contacts with protein S6 during translation in the 70S ribosome.

Protein-protein interaction databases

STRINGi300852.TTHA1689.

Structurei

Secondary structure

1
276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi8 – 103Combined sources
Turni11 – 155Combined sources
Beta strandi17 – 193Combined sources
Turni22 – 243Combined sources
Beta strandi26 – 283Combined sources
Helixi31 – 333Combined sources
Beta strandi34 – 363Combined sources
Beta strandi41 – 433Combined sources
Beta strandi45 – 484Combined sources
Beta strandi49 – 546Combined sources
Beta strandi61 – 633Combined sources
Helixi70 – 723Combined sources
Beta strandi77 – 837Combined sources
Beta strandi88 – 903Combined sources
Beta strandi92 – 976Combined sources
Beta strandi102 – 1065Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi119 – 1235Combined sources
Beta strandi125 – 1284Combined sources
Beta strandi130 – 1323Combined sources
Helixi133 – 1353Combined sources
Beta strandi141 – 1488Combined sources
Turni149 – 1513Combined sources
Beta strandi153 – 1564Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi163 – 1697Combined sources
Beta strandi172 – 1765Combined sources
Turni178 – 1803Combined sources
Beta strandi182 – 1865Combined sources
Beta strandi189 – 1946Combined sources
Helixi199 – 2035Combined sources
Helixi209 – 2146Combined sources
Helixi223 – 2253Combined sources
Turni228 – 2303Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi253 – 2564Combined sources
Helixi265 – 2684Combined sources
Beta strandi270 – 2723Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RD/YD1-276[»]
1VY4X-ray2.60BD/DD1-276[»]
1VY5X-ray2.55BD/DD1-276[»]
1VY6X-ray2.90BD/DD1-276[»]
1VY7X-ray2.80BD/DD1-276[»]
4L47X-ray3.22RD/YD1-276[»]
4L71X-ray3.90RD/YD1-276[»]
4LELX-ray3.90RD/YD1-276[»]
4LFZX-ray3.92RD/YD1-276[»]
4LNTX-ray2.94RD/YD1-276[»]
4LSKX-ray3.48RD/YD1-276[»]
4LT8X-ray3.14RD/YD1-276[»]
4P6FX-ray3.60RD/YD1-276[»]
4P70X-ray3.68RD/YD1-276[»]
4V42X-ray5.50BD61-197[»]
4V4PX-ray5.50AD62-234[»]
4V4XX-ray5.00BD1-276[»]
4V4YX-ray5.50BD1-276[»]
4V4ZX-ray4.51BD1-276[»]
4V51X-ray2.80BD/DD2-276[»]
4V5AX-ray3.50BD/DD2-276[»]
4V5CX-ray3.30BD/DD1-276[»]
4V5DX-ray3.50BD/DD1-276[»]
4V5EX-ray3.45BD/DD1-276[»]
4V5FX-ray3.60BD/DD1-276[»]
4V5GX-ray3.60BD/DD1-276[»]
4V5JX-ray3.10BD/DD1-276[»]
4V5KX-ray3.20BD/DD1-276[»]
4V5LX-ray3.10BD1-276[»]
4V5Melectron microscopy7.80BD1-276[»]
4V5Nelectron microscopy7.60BD1-276[»]
4V5PX-ray3.10BD/DD1-276[»]
4V5QX-ray3.10BD/DD1-276[»]
4V5RX-ray3.10BD/DD1-276[»]
4V5SX-ray3.10BD/DD1-276[»]
4V68electron microscopy6.40BD2-273[»]
4V6AX-ray3.10BD/DD1-276[»]
4V6FX-ray3.10AD/DD1-276[»]
4V6GX-ray3.50BD/DD1-276[»]
4V7JX-ray3.30AD/BD1-276[»]
4V7KX-ray3.60AD/BD1-276[»]
4V7LX-ray3.00BD/DD1-276[»]
4V7MX-ray3.45BD/DD1-276[»]
4V7WX-ray3.00BD/DD1-276[»]
4V7XX-ray3.00BD/DD1-276[»]
4V7YX-ray3.00BD/DD1-276[»]
4V7ZX-ray3.10BD/DD1-276[»]
4V87X-ray3.10AD/DD2-273[»]
4V8AX-ray3.20AD/BD1-276[»]
4V8BX-ray3.00BD/DD1-276[»]
4V8CX-ray3.30AD/BD1-276[»]
4V8DX-ray3.00BD/DD1-276[»]
4V8EX-ray3.30AD/CD1-276[»]
4V8FX-ray3.30AD/DD1-276[»]
4V8GX-ray3.00BD/DD1-276[»]
4V8HX-ray3.10BD/DD1-276[»]
4V8IX-ray2.70BD/DD1-276[»]
4V8JX-ray3.90BD/DD1-276[»]
4V8NX-ray3.10BD/DD1-276[»]
4V8OX-ray3.80BD1-276[»]
4V8QX-ray3.10AD1-276[»]
4V8UX-ray3.70BD/DD1-276[»]
4V8XX-ray3.35BD/DD1-276[»]
4V90X-ray2.95BD2-276[»]
4V95X-ray3.20BD/DD1-276[»]
4V97X-ray3.52BD/DD1-276[»]
4V9AX-ray3.30BD/DD1-276[»]
4V9BX-ray3.10BD/DD1-276[»]
4V9HX-ray2.86BD1-276[»]
4V9IX-ray3.30BD/DD2-272[»]
4V9RX-ray3.00BD/DD1-276[»]
4V9SX-ray3.10BD/DD1-276[»]
4W2EX-ray2.90D1-276[»]
4W2FX-ray2.40BD/DD1-276[»]
4W2GX-ray2.55BD/DD1-276[»]
4W2HX-ray2.70BD/DD1-276[»]
4W2IX-ray2.70BD/DD1-276[»]
ProteinModelPortaliP60405.
SMRiP60405. Positions 2-273.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60405.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L2P family.Curated

Phylogenomic databases

eggNOGiCOG0090.
HOGENOMiHOG000232982.
KOiK02886.
OMAiNNLPIRN.
OrthoDBiEOG6TR0J1.
PhylomeDBiP60405.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPiMF_01320_B. Ribosomal_L2_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR005880. Ribosomal_L2_bac/org-type.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PTHR13691:SF5. PTHR13691:SF5. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR01171. rplB_bact. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P60405-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVKKFKPYT PSRRFMTVAD FSEITKTEPE KSLVKPLKKT GGRNNQGRIT
60 70 80 90 100
VRFRGGGHKR LYRIIDFKRW DKVGIPAKVA AIEYDPNRSA RIALLHYVDG
110 120 130 140 150
EKRYIIAPDG LQVGQQVVAG PDAPIQVGNA LPLRFIPVGT VVHAVELEPK
160 170 180 190 200
KGAKLARAAG TSAQIQGREG DYVILRLPSG ELRKVHGECY ATVGAVGNAD
210 220 230 240 250
HKNIVLGKAG RSRWLGRRPH VRGAAMNPVD HPHGGGEGRA PRGRPPASPW
260 270
GWQTKGLKTR KRRKPSSRFI IARRKK
Length:276
Mass (Da):30,468
Last modified:January 22, 2007 - v3
Checksum:i7CF40C2BD586349B
GO

Mass spectrometryi

Molecular mass is 30337 Da from positions 2 - 276. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71512.1.
RefSeqiWP_011173712.1. NC_006461.1.
YP_144955.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71512; BAD71512; BAD71512.
GeneIDi3168720.
KEGGittj:TTHA1689.
PATRICi23958333. VBITheThe93045_1659.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71512.1.
RefSeqiWP_011173712.1. NC_006461.1.
YP_144955.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VVJX-ray3.44RD/YD1-276[»]
1VY4X-ray2.60BD/DD1-276[»]
1VY5X-ray2.55BD/DD1-276[»]
1VY6X-ray2.90BD/DD1-276[»]
1VY7X-ray2.80BD/DD1-276[»]
4L47X-ray3.22RD/YD1-276[»]
4L71X-ray3.90RD/YD1-276[»]
4LELX-ray3.90RD/YD1-276[»]
4LFZX-ray3.92RD/YD1-276[»]
4LNTX-ray2.94RD/YD1-276[»]
4LSKX-ray3.48RD/YD1-276[»]
4LT8X-ray3.14RD/YD1-276[»]
4P6FX-ray3.60RD/YD1-276[»]
4P70X-ray3.68RD/YD1-276[»]
4V42X-ray5.50BD61-197[»]
4V4PX-ray5.50AD62-234[»]
4V4XX-ray5.00BD1-276[»]
4V4YX-ray5.50BD1-276[»]
4V4ZX-ray4.51BD1-276[»]
4V51X-ray2.80BD/DD2-276[»]
4V5AX-ray3.50BD/DD2-276[»]
4V5CX-ray3.30BD/DD1-276[»]
4V5DX-ray3.50BD/DD1-276[»]
4V5EX-ray3.45BD/DD1-276[»]
4V5FX-ray3.60BD/DD1-276[»]
4V5GX-ray3.60BD/DD1-276[»]
4V5JX-ray3.10BD/DD1-276[»]
4V5KX-ray3.20BD/DD1-276[»]
4V5LX-ray3.10BD1-276[»]
4V5Melectron microscopy7.80BD1-276[»]
4V5Nelectron microscopy7.60BD1-276[»]
4V5PX-ray3.10BD/DD1-276[»]
4V5QX-ray3.10BD/DD1-276[»]
4V5RX-ray3.10BD/DD1-276[»]
4V5SX-ray3.10BD/DD1-276[»]
4V68electron microscopy6.40BD2-273[»]
4V6AX-ray3.10BD/DD1-276[»]
4V6FX-ray3.10AD/DD1-276[»]
4V6GX-ray3.50BD/DD1-276[»]
4V7JX-ray3.30AD/BD1-276[»]
4V7KX-ray3.60AD/BD1-276[»]
4V7LX-ray3.00BD/DD1-276[»]
4V7MX-ray3.45BD/DD1-276[»]
4V7WX-ray3.00BD/DD1-276[»]
4V7XX-ray3.00BD/DD1-276[»]
4V7YX-ray3.00BD/DD1-276[»]
4V7ZX-ray3.10BD/DD1-276[»]
4V87X-ray3.10AD/DD2-273[»]
4V8AX-ray3.20AD/BD1-276[»]
4V8BX-ray3.00BD/DD1-276[»]
4V8CX-ray3.30AD/BD1-276[»]
4V8DX-ray3.00BD/DD1-276[»]
4V8EX-ray3.30AD/CD1-276[»]
4V8FX-ray3.30AD/DD1-276[»]
4V8GX-ray3.00BD/DD1-276[»]
4V8HX-ray3.10BD/DD1-276[»]
4V8IX-ray2.70BD/DD1-276[»]
4V8JX-ray3.90BD/DD1-276[»]
4V8NX-ray3.10BD/DD1-276[»]
4V8OX-ray3.80BD1-276[»]
4V8QX-ray3.10AD1-276[»]
4V8UX-ray3.70BD/DD1-276[»]
4V8XX-ray3.35BD/DD1-276[»]
4V90X-ray2.95BD2-276[»]
4V95X-ray3.20BD/DD1-276[»]
4V97X-ray3.52BD/DD1-276[»]
4V9AX-ray3.30BD/DD1-276[»]
4V9BX-ray3.10BD/DD1-276[»]
4V9HX-ray2.86BD1-276[»]
4V9IX-ray3.30BD/DD2-272[»]
4V9RX-ray3.00BD/DD1-276[»]
4V9SX-ray3.10BD/DD1-276[»]
4W2EX-ray2.90D1-276[»]
4W2FX-ray2.40BD/DD1-276[»]
4W2GX-ray2.55BD/DD1-276[»]
4W2HX-ray2.70BD/DD1-276[»]
4W2IX-ray2.70BD/DD1-276[»]
ProteinModelPortaliP60405.
SMRiP60405. Positions 2-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1689.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71512; BAD71512; BAD71512.
GeneIDi3168720.
KEGGittj:TTHA1689.
PATRICi23958333. VBITheThe93045_1659.

Phylogenomic databases

eggNOGiCOG0090.
HOGENOMiHOG000232982.
KOiK02886.
OMAiNNLPIRN.
OrthoDBiEOG6TR0J1.
PhylomeDBiP60405.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1728-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60405.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPiMF_01320_B. Ribosomal_L2_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR005880. Ribosomal_L2_bac/org-type.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PTHR13691:SF5. PTHR13691:SF5. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR01171. rplB_bact. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 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 2-22.
  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 nameiRL2_THET8
AccessioniPrimary (citable) accession number: P60405
Secondary accession number(s): Q5SHP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2004
Last sequence update: January 22, 2007
Last modified: March 3, 2015
This is version 104 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

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.