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Protein

50S ribosomal protein L2

Gene

rplB

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 3 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. Makes several contacts with the 16S rRNA in the 70S ribosome (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciDRAD243230:GH46-324-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L2
Gene namesi
Name:rplB
Ordered Locus Names:DR_0314
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002524 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 27527450S ribosomal protein L2PRO_0000129558Add
BLAST

Proteomic databases

PRIDEiQ9RXJ9.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-58602N.
STRINGi243230.DR_0314.

Structurei

Secondary structure

1
275
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Helixi11 – 133Combined sources
Turni31 – 333Combined sources
Beta strandi34 – 374Combined sources
Beta strandi41 – 433Combined sources
Beta strandi46 – 494Combined sources
Beta strandi51 – 533Combined sources
Beta strandi60 – 634Combined sources
Beta strandi65 – 684Combined sources
Helixi69 – 724Combined sources
Beta strandi74 – 8310Combined sources
Turni86 – 883Combined sources
Beta strandi92 – 976Combined sources
Turni98 – 1003Combined sources
Beta strandi102 – 1065Combined sources
Beta strandi116 – 1227Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi141 – 1433Combined sources
Turni149 – 1513Combined sources
Beta strandi158 – 1614Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi170 – 1767Combined sources
Turni178 – 1803Combined sources
Beta strandi182 – 1865Combined sources
Beta strandi189 – 1946Combined sources
Beta strandi196 – 1983Combined sources
Helixi200 – 2034Combined sources
Helixi209 – 2146Combined sources
Beta strandi216 – 2183Combined sources
Helixi223 – 2253Combined sources
Helixi228 – 2303Combined sources
Beta strandi236 – 2394Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi247 – 2504Combined sources
Beta strandi252 – 2543Combined sources
Helixi262 – 2643Combined sources
Helixi265 – 2695Combined sources
Beta strandi270 – 2723Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NKWX-ray3.10A1-275[»]
1NWXX-ray3.50A2-275[»]
1NWYX-ray3.30A2-275[»]
1SM1X-ray3.42A1-275[»]
1XBPX-ray3.50A2-275[»]
2ZJPX-ray3.70A2-275[»]
2ZJQX-ray3.30A2-275[»]
2ZJRX-ray2.91A2-275[»]
3CF5X-ray3.30A2-275[»]
3DLLX-ray3.50A2-275[»]
3PIOX-ray3.25A2-275[»]
3PIPX-ray3.45A2-274[»]
4IO9X-ray3.20A2-275[»]
4IOAX-ray3.20A2-275[»]
4IOCX-ray3.60A2-275[»]
4U67X-ray3.65A1-275[»]
4V49X-ray8.70A4-273[»]
4V4AX-ray9.50A4-273[»]
4V4GX-ray11.50D4-273[»]
4WFNX-ray3.54A1-275[»]
5DM6X-ray2.90A2-275[»]
5DM7X-ray3.00A2-275[»]
ProteinModelPortaliQ9RXJ9.
SMRiQ9RXJ9. Positions 4-273.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RXJ9.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L2P family.Curated

Phylogenomic databases

eggNOGiENOG4105CFD. Bacteria.
COG0090. LUCA.
HOGENOMiHOG000232982.
InParanoidiQ9RXJ9.
KOiK02886.
OMAiPIKAGNN.
OrthoDBiPOG091H01QE.

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. 1 hit.
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.
SMARTiSM01383. Ribosomal_L2. 1 hit.
SM01382. Ribosomal_L2_C. 1 hit.
[Graphical view]
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.

Q9RXJ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVKKYRPYT PSRRQMTTAD FSGLTKKRPE KALTEALPKT GGRNNRGRIT
60 70 80 90 100
SRFIGGGHKR LYRIIDFKRR DKSGVNAKVA AIEYDPNRSA RIALLHYADG
110 120 130 140 150
EKRYILAPEG LTVGATVNAG PEAEPKLGNA LPLRFVPVGA VVHALELVPG
160 170 180 190 200
KGAQLARSAG TSVQVQGKES DYVIVRLPSG ELRRVHSECY ATIGAVGNAE
210 220 230 240 250
HKNIVLGKAG RSRWLGRKPH QRGSAMNPVD HPHGGGEGRT GAGRVPVTPW
260 270
GKPTKGLKTR RKRKTSDRFI VTRRK
Length:275
Mass (Da):30,045
Last modified:January 23, 2007 - v3
Checksum:iA96E5853B592C11E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF09895.1.
PIRiB75534.
RefSeqiNP_294037.1. NC_001263.1.
WP_010886959.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF09895; AAF09895; DR_0314.
GeneIDi1798735.
KEGGidra:DR_0314.
PATRICi21628126. VBIDeiRad64572_0480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF09895.1.
PIRiB75534.
RefSeqiNP_294037.1. NC_001263.1.
WP_010886959.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NKWX-ray3.10A1-275[»]
1NWXX-ray3.50A2-275[»]
1NWYX-ray3.30A2-275[»]
1SM1X-ray3.42A1-275[»]
1XBPX-ray3.50A2-275[»]
2ZJPX-ray3.70A2-275[»]
2ZJQX-ray3.30A2-275[»]
2ZJRX-ray2.91A2-275[»]
3CF5X-ray3.30A2-275[»]
3DLLX-ray3.50A2-275[»]
3PIOX-ray3.25A2-275[»]
3PIPX-ray3.45A2-274[»]
4IO9X-ray3.20A2-275[»]
4IOAX-ray3.20A2-275[»]
4IOCX-ray3.60A2-275[»]
4U67X-ray3.65A1-275[»]
4V49X-ray8.70A4-273[»]
4V4AX-ray9.50A4-273[»]
4V4GX-ray11.50D4-273[»]
4WFNX-ray3.54A1-275[»]
5DM6X-ray2.90A2-275[»]
5DM7X-ray3.00A2-275[»]
ProteinModelPortaliQ9RXJ9.
SMRiQ9RXJ9. Positions 4-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58602N.
STRINGi243230.DR_0314.

Proteomic databases

PRIDEiQ9RXJ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF09895; AAF09895; DR_0314.
GeneIDi1798735.
KEGGidra:DR_0314.
PATRICi21628126. VBIDeiRad64572_0480.

Phylogenomic databases

eggNOGiENOG4105CFD. Bacteria.
COG0090. LUCA.
HOGENOMiHOG000232982.
InParanoidiQ9RXJ9.
KOiK02886.
OMAiPIKAGNN.
OrthoDBiPOG091H01QE.

Enzyme and pathway databases

BioCyciDRAD243230:GH46-324-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9RXJ9.

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. 1 hit.
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.
SMARTiSM01383. Ribosomal_L2. 1 hit.
SM01382. Ribosomal_L2_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR01171. rplB_bact. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL2_DEIRA
AccessioniPrimary (citable) accession number: Q9RXJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 110 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

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 one 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.