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Protein

50S ribosomal protein L2

Gene

rplB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

One of the primary rRNA binding proteins (PubMed:3298242). Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation (PubMed:8722025). It has been suggested to have peptidyltransferase activity; this is highly controversial.7 Publications
In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.1 Publication

Miscellaneous

This protein can be partially replaced in vivo by its H.marismortui (HmaL2) or human (L8, from the 60S cytoplasmic ribosome) homolog.1 Publication

GO - Molecular functioni

  • RNA binding Source: GO_Central
  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: CAFA
  • transferase activity Source: InterPro
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

  • cytoplasmic translation Source: GO_Central
  • ribosomal large subunit assembly Source: CAFA

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10865-MONOMER
MetaCyc:EG10865-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L2
Alternative name(s):
Large ribosomal subunit protein uL21 Publication
Gene namesi
Name:rplB
Ordered Locus Names:b3317, JW3279
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10865 rplB

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic large ribosomal subunit Source: CAFA

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi230H → Q: Loss of peptidyltransferase activity in reconstituted ribosomes. No change in rRNA binding or assembly into ribosomes. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001295592 – 27350S ribosomal protein L2Add BLAST272

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei242N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP60422
PaxDbiP60422
PRIDEiP60422

PTM databases

iPTMnetiP60422

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit (Ref. 4, PubMed:7556101, PubMed:11114255, PubMed:10094780, PubMed:10756104, PubMed:12809609, PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161). Forms a bridge to the 30S subunit in the 70S ribosome, contacting the 16S rRNA (PubMed:12809609). Interacts weakly with S6 in one of the 3.5 A resolved structures.12 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi8521321 interactor.
DIPiDIP-35747N
IntActiP60422 372 interactors.
STRINGi316385.ECDH10B_3492

Structurei

Secondary structure

1273
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Turni11 – 13Combined sources3
Beta strandi17 – 19Combined sources3
Helixi31 – 33Combined sources3
Beta strandi47 – 54Combined sources8
Beta strandi76 – 82Combined sources7
Beta strandi85 – 89Combined sources5
Beta strandi91 – 96Combined sources6
Beta strandi101 – 105Combined sources5
Beta strandi118 – 121Combined sources4
Beta strandi129 – 131Combined sources3
Turni132 – 134Combined sources3
Beta strandi140 – 144Combined sources5
Turni148 – 150Combined sources3
Beta strandi162 – 168Combined sources7
Beta strandi171 – 175Combined sources5
Beta strandi181 – 185Combined sources5
Beta strandi189 – 193Combined sources5
Helixi198 – 202Combined sources5
Helixi208 – 213Combined sources6
Helixi222 – 224Combined sources3
Turni227 – 229Combined sources3
Beta strandi236 – 238Combined sources3
Beta strandi261 – 263Combined sources3
Helixi264 – 266Combined sources3
Beta strandi267 – 269Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00C4-270[»]
2RDOelectron microscopy9.10C2-273[»]
3BBXelectron microscopy10.00C1-273[»]
3J5Lelectron microscopy6.60C2-272[»]
3J7Zelectron microscopy3.90C1-273[»]
3J8Gelectron microscopy5.00C1-273[»]
3J9Yelectron microscopy3.90C1-273[»]
3J9Zelectron microscopy3.60LN2-273[»]
3JA1electron microscopy3.60LD2-273[»]
3JBUelectron microscopy3.64c1-273[»]
3JBVelectron microscopy3.32c1-273[»]
3JCDelectron microscopy3.70C1-273[»]
3JCEelectron microscopy3.20C1-273[»]
3JCJelectron microscopy3.70B1-273[»]
3JCNelectron microscopy4.60C1-273[»]
487Delectron microscopy7.50I62-172[»]
4CSUelectron microscopy5.50C2-273[»]
4U1UX-ray2.95BC/DC2-272[»]
4U1VX-ray3.00BC/DC2-272[»]
4U20X-ray2.90BC/DC2-272[»]
4U24X-ray2.90BC/DC2-272[»]
4U25X-ray2.90BC/DC2-272[»]
4U26X-ray2.80BC/DC2-272[»]
4U27X-ray2.80BC/DC2-272[»]
4UY8electron microscopy3.80C2-272[»]
4V47electron microscopy12.30AA2-273[»]
4V48electron microscopy11.50AA2-273[»]
4V4HX-ray3.46BC/DC1-273[»]
4V4QX-ray3.46BC/DC1-273[»]
4V4Velectron microscopy15.00BA39-265[»]
4V4Welectron microscopy15.00BA39-265[»]
4V50X-ray3.22BC/DC2-273[»]
4V52X-ray3.21BC/DC2-273[»]
4V53X-ray3.54BC/DC2-273[»]
4V54X-ray3.30BC/DC2-273[»]
4V55X-ray4.00BC/DC2-273[»]
4V56X-ray3.93BC/DC2-273[»]
4V57X-ray3.50BC/DC2-273[»]
4V5BX-ray3.74AC/CC1-273[»]
4V5Helectron microscopy5.80BC2-272[»]
4V5YX-ray4.45BC/DC2-273[»]
4V64X-ray3.50BC/DC1-273[»]
4V65electron microscopy9.00BN1-270[»]
4V66electron microscopy9.00BN1-270[»]
4V69electron microscopy6.70BC2-272[»]
4V6CX-ray3.19BC/DC1-273[»]
4V6DX-ray3.81BC/DC1-273[»]
4V6EX-ray3.71BC/DC1-273[»]
4V6Kelectron microscopy8.25AD1-273[»]
4V6Lelectron microscopy13.20BD1-273[»]
4V6Melectron microscopy7.10B62-273[»]
4V6Nelectron microscopy12.10AD2-273[»]
4V6Oelectron microscopy14.70BD2-273[»]
4V6Pelectron microscopy13.50BD2-273[»]
4V6Qelectron microscopy11.50BD2-273[»]
4V6Relectron microscopy11.50BD2-273[»]
4V6Selectron microscopy13.10AD2-273[»]
4V6Telectron microscopy8.30BC2-272[»]
4V6Velectron microscopy9.80BD2-273[»]
4V6Yelectron microscopy12.00BC1-272[»]
4V6Zelectron microscopy12.00BC1-272[»]
4V70electron microscopy17.00BC1-272[»]
4V71electron microscopy20.00BC1-272[»]
4V72electron microscopy13.00BC1-272[»]
4V73electron microscopy15.00BC1-272[»]
4V74electron microscopy17.00BC1-272[»]
4V75electron microscopy12.00BC1-272[»]
4V76electron microscopy17.00BC1-272[»]
4V77electron microscopy17.00BC1-272[»]
4V78electron microscopy20.00BC1-272[»]
4V79electron microscopy15.00BC1-272[»]
4V7Aelectron microscopy9.00BC1-272[»]
4V7Belectron microscopy6.80BC1-273[»]
4V7Celectron microscopy7.60BD2-273[»]
4V7Delectron microscopy7.60AD2-273[»]
4V7Ielectron microscopy9.60A61-273[»]
4V7SX-ray3.25BC/DC2-272[»]
4V7TX-ray3.19BC/DC2-272[»]
4V7UX-ray3.10BC/DC2-272[»]
4V7VX-ray3.29BC/DC2-272[»]
4V85X-ray3.20C1-273[»]
4V89X-ray3.70BC1-273[»]
4V9CX-ray3.30BC/DC1-273[»]
4V9DX-ray3.00CC/DC2-272[»]
4V9OX-ray2.90AC/CC/EC/GC1-273[»]
4V9PX-ray2.90AC/CC/EC/GC1-273[»]
4WF1X-ray3.09BC/DC2-272[»]
4WOIX-ray3.00BC/CC1-273[»]
4WWWX-ray3.10RC/YC2-272[»]
4YBBX-ray2.10CC/DC2-272[»]
5ADYelectron microscopy4.50C1-273[»]
5AFIelectron microscopy2.90C1-273[»]
5AKAelectron microscopy5.70C1-273[»]
5GADelectron microscopy3.70C1-273[»]
5GAEelectron microscopy3.33C1-273[»]
5GAFelectron microscopy4.30C2-272[»]
5GAGelectron microscopy3.80C1-273[»]
5GAHelectron microscopy3.80C1-273[»]
5H5Uelectron microscopy3.00C2-273[»]
5IQRelectron microscopy3.00B1-273[»]
5IT8X-ray3.12CC/DC2-272[»]
5J5BX-ray2.80CC/DC2-272[»]
5J7LX-ray3.00CC/DC2-272[»]
5J88X-ray3.32CC/DC2-273[»]
5J8AX-ray3.10CC/DC2-273[»]
5J91X-ray2.96CC/DC2-273[»]
5JC9X-ray3.03CC/DC2-272[»]
5JTEelectron microscopy3.60BC1-273[»]
5JU8electron microscopy3.60BC1-273[»]
5KCRelectron microscopy3.601D1-273[»]
5KCSelectron microscopy3.901D1-273[»]
5KPSelectron microscopy3.90B1-273[»]
5KPVelectron microscopy4.10A1-273[»]
5KPWelectron microscopy3.90A1-273[»]
5KPXelectron microscopy3.90A1-273[»]
5L3Pelectron microscopy3.70D1-273[»]
5LZAelectron microscopy3.60C2-272[»]
5LZBelectron microscopy5.30C2-272[»]
5LZCelectron microscopy4.80C2-272[»]
5LZDelectron microscopy3.40C2-272[»]
5LZEelectron microscopy3.50C2-272[»]
5LZFelectron microscopy4.60C2-272[»]
5MDVelectron microscopy2.97B1-273[»]
5MDWelectron microscopy3.06B1-273[»]
5MDYelectron microscopy3.35B1-273[»]
5MDZelectron microscopy3.10B1-273[»]
5MGPelectron microscopy3.10C2-272[»]
5NCOelectron microscopy4.80C2-272[»]
5NP6electron microscopy3.60a2-272[»]
5NWYelectron microscopy2.93P1-273[»]
5O2Relectron microscopy3.40C2-272[»]
5U4Ielectron microscopy3.50C1-273[»]
5U9Felectron microscopy3.20041-273[»]
5U9Gelectron microscopy3.20041-273[»]
5UYKelectron microscopy3.90042-272[»]
5UYLelectron microscopy3.60042-272[»]
5UYMelectron microscopy3.20042-272[»]
5UYNelectron microscopy4.00042-272[»]
5UYPelectron microscopy3.90042-272[»]
5UYQelectron microscopy3.80042-272[»]
6BU8electron microscopy3.50042-272[»]
6C4Helectron microscopy3.10C1-273[»]
6ENFelectron microscopy3.20C2-272[»]
6ENJelectron microscopy3.70C2-272[»]
6ENUelectron microscopy3.10C2-272[»]
ProteinModelPortaliP60422
SMRiP60422
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60422

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CFD Bacteria
COG0090 LUCA
HOGENOMiHOG000232982
InParanoidiP60422
KOiK02886
OMAiHGYIKGV
PhylomeDBiP60422

Family and domain databases

Gene3Di2.30.30.301 hit
4.10.950.101 hit
HAMAPiMF_01320_B Ribosomal_L2_B, 1 hit
InterProiView protein in InterPro
IPR012340 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_sf
PANTHERiPTHR13691 PTHR13691, 1 hit
PfamiView protein in Pfam
PF00181 Ribosomal_L2, 1 hit
PF03947 Ribosomal_L2_C, 1 hit
PIRSFiPIRSF002158 Ribosomal_L2, 1 hit
SMARTiView protein in SMART
SM01383 Ribosomal_L2, 1 hit
SM01382 Ribosomal_L2_C, 1 hit
SUPFAMiSSF50104 SSF50104, 1 hit
SSF50249 SSF50249, 1 hit
TIGRFAMsiTIGR01171 rplB_bact, 1 hit
PROSITEiView protein in PROSITE
PS00467 RIBOSOMAL_L2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P60422-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVVKCKPTS PGRRHVVKVV NPELHKGKPF APLLEKNSKS GGRNNNGRIT
60 70 80 90 100
TRHIGGGHKQ AYRIVDFKRN KDGIPAVVER LEYDPNRSAN IALVLYKDGE
110 120 130 140 150
RRYILAPKGL KAGDQIQSGV DAAIKPGNTL PMRNIPVGST VHNVEMKPGK
160 170 180 190 200
GGQLARSAGT YVQIVARDGA YVTLRLRSGE MRKVEADCRA TLGEVGNAEH
210 220 230 240 250
MLRVLGKAGA ARWRGVRPTV RGTAMNPVDH PHGGGEGRNF GKHPVTPWGV
260 270
QTKGKKTRSN KRTDKFIVRR RSK
Length:273
Mass (Da):29,860
Last modified:January 23, 2007 - v2
Checksum:i1010BDE8D8C68B9B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti232 – 235HGGG → GGGH AA sequence (Ref. 4) Curated4

Mass spectrometryi

Molecular mass is 29732.3 Da from positions 2 - 273. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA Translation: CAA26463.1
U18997 Genomic DNA Translation: AAA58114.1
U00096 Genomic DNA Translation: AAC76342.1
AP009048 Genomic DNA Translation: BAE77974.1
PIRiE23129 R5EC2
RefSeqiNP_417776.1, NC_000913.3
WP_000301864.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76342; AAC76342; b3317
BAE77974; BAE77974; BAE77974
GeneIDi29456695
947820
KEGGiecj:JW3279
eco:b3317
PATRICifig|1411691.4.peg.3414

Similar proteinsi

Entry informationi

Entry nameiRL2_ECOLI
AccessioniPrimary (citable) accession number: P60422
Secondary accession number(s): P02387, Q2M6Y2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 161 of the entry and version 2 of the sequence. See 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