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Protein

50S ribosomal protein L10

Gene

rplJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.1 Publication
Protein L10 is also a translational repressor protein. It controls the translation of the rplJL-rpoBC operon by binding to its mRNA.1 Publication

Miscellaneous

Ribosomal protein L8 appears to be an aggregate of ribosomal proteins L7/L12 and L10.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionRepressor, Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding
Biological processTranslation regulation

Enzyme and pathway databases

BioCyciEcoCyc:EG10871-MONOMER.
MetaCyc:EG10871-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L10
Alternative name(s):
50S ribosomal protein L8
Large ribosomal subunit protein uL101 Publication
Gene namesi
Name:rplJ
Ordered Locus Names:b3985, JW3948
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10871. rplJ.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi156 – 165Missing : Generation time doubles, only 1 L12 dimer binds to the ribosome. Decreased association of IF-2 with L7/L12 and decreased stimulation of GTPase activity of EF-G by L7/L12. 1 Publication10

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00001546272 – 16550S ribosomal protein L10Add BLAST164

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei37N6-acetyllysine1 Publication1
Modified residuei105N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A7J3.
PaxDbiP0A7J3.
PRIDEiP0A7J3.

Interactioni

Subunit structurei

Part of the ribosomal stalk of the 50S ribosomal subunit (PubMed:15923259). The N-terminus interacts with L11 and the large rRNA to form the base of the stalk. The C-terminus forms an elongated spine to which 2 L12 dimers bind in a sequential fashion forming a pentameric L10(L12)(L12)2 complex. Two L12 dimers associate with a copy of L10 to form a very strong complex (called L8).9 Publications

Protein-protein interaction databases

BioGridi852784. 1 interactor.
DIPiDIP-35816N.
IntActiP0A7J3. 52 interactors.
MINTiMINT-1264502.
STRINGi511145.b3985.

Structurei

Secondary structure

1165
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 19Combined sources15
Beta strandi23 – 28Combined sources6
Helixi35 – 47Combined sources13
Beta strandi50 – 54Combined sources5
Helixi57 – 64Combined sources8
Turni65 – 68Combined sources4
Helixi72 – 74Combined sources3
Beta strandi81 – 85Combined sources5
Beta strandi87 – 91Combined sources5
Helixi92 – 103Combined sources12
Beta strandi110 – 113Combined sources4
Beta strandi116 – 118Combined sources3
Helixi122 – 124Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J7Zelectron microscopy3.9051-165[»]
3J9Yelectron microscopy3.9051-165[»]
3J9Zelectron microscopy3.60LD2-165[»]
3JA1electron microscopy3.60LJ2-165[»]
3JCJelectron microscopy3.70e1-165[»]
4UY8electron microscopy3.8051-148[»]
4V6Nelectron microscopy12.10AJ2-165[»]
4V6Oelectron microscopy14.70BJ2-165[»]
4V6Pelectron microscopy13.50BJ2-165[»]
4V6Qelectron microscopy11.50BJ2-165[»]
4V6Relectron microscopy11.50BJ2-165[»]
4V6Selectron microscopy13.10AJ2-165[»]
4V6Velectron microscopy9.80BJ2-165[»]
4V7Belectron microscopy6.80B51-165[»]
4V7Celectron microscopy7.60BJ1-165[»]
4V7Delectron microscopy7.60AJ1-165[»]
4V85X-ray3.20H1-165[»]
4V89X-ray3.70BH1-165[»]
4V9OX-ray2.90A5/C5/E51-165[»]
4V9PX-ray2.90A5/E51-165[»]
4YBBX-ray2.10DI2-136[»]
5ADYelectron microscopy4.5071-165[»]
5AFIelectron microscopy2.9051-165[»]
5GADelectron microscopy3.70I1-165[»]
5GAEelectron microscopy3.33I1-165[»]
5GAFelectron microscopy4.30I2-126[»]
5GAGelectron microscopy3.80I1-165[»]
5GAHelectron microscopy3.80I1-165[»]
5H5Uelectron microscopy3.00I2-165[»]
5IQRelectron microscopy3.00H1-165[»]
5IT8X-ray3.12DI2-136[»]
5J5BX-ray2.80DI2-136[»]
5J7LX-ray3.00DI2-136[»]
5J88X-ray3.32DI2-136[»]
5J8AX-ray3.10DI2-136[»]
5J91X-ray2.96DI2-136[»]
5JC9X-ray3.03DI2-136[»]
5KCRelectron microscopy3.601J1-165[»]
5KCSelectron microscopy3.901J1-165[»]
5KPSelectron microscopy3.90H1-165[»]
5KPVelectron microscopy4.10G1-165[»]
5KPWelectron microscopy3.90G1-165[»]
5KPXelectron microscopy3.90G1-165[»]
5L3Pelectron microscopy3.70J1-165[»]
5MDVelectron microscopy2.97H1-165[»]
5MDWelectron microscopy3.06H1-165[»]
5MDYelectron microscopy3.35H1-165[»]
5MDZelectron microscopy3.10H1-165[»]
ProteinModelPortaliP0A7J3.
SMRiP0A7J3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108VZM. Bacteria.
COG0244. LUCA.
HOGENOMiHOG000004851.
InParanoidiP0A7J3.
KOiK02864.
OMAiAKANPAF.
PhylomeDBiP0A7J3.

Family and domain databases

HAMAPiMF_00362. Ribosomal_L10. 1 hit.
InterProiView protein in InterPro
IPR022973. Ribosomal_L10.
IPR002363. Ribosomal_L10_eubac_CS.
IPR001790. Ribosomal_L10P.
PfamiView protein in Pfam
PF00466. Ribosomal_L10. 1 hit.
PROSITEiView protein in PROSITE
PS01109. RIBOSOMAL_L10. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0A7J3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALNLQDKQA IVAEVSEVAK GALSAVVADS RGVTVDKMTE LRKAGREAGV
60 70 80 90 100
YMRVVRNTLL RRAVEGTPFE CLKDAFVGPT LIAYSMEHPG AAARLFKEFA
110 120 130 140 150
KANAKFEVKA AAFEGELIPA SQIDRLATLP TYEEAIARLM ATMKEASAGK
160
LVRTLAAVRD AKEAA
Length:165
Mass (Da):17,712
Last modified:January 23, 2007 - v2
Checksum:iF15822B0EDB6AC02
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti84Y → YR AA sequence (PubMed:773698).Curated1
Sequence conflicti84Y → YR AA sequence (PubMed:782920).Curated1
Sequence conflicti84Y → YR AA sequence (PubMed:797648).Curated1
Sequence conflicti116E → Q AA sequence (PubMed:773698).Curated1

Mass spectrometryi

Molecular mass is 17581.1 Da from positions 2 - 165. Determined by MALDI. 1 Publication
Molecular mass is 66643±13 Da from positions 2 - 165. Determined by ESI. Isolated L10(L12)4.1 Publication
Molecular mass is 17580±2 Da from positions 2 - 165. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00339 Genomic DNA. Translation: CAA23623.1.
U00006 Genomic DNA. Translation: AAC43083.1.
U00096 Genomic DNA. Translation: AAC76959.1.
AP009048 Genomic DNA. Translation: BAE77335.1.
PIRiS12574. R5EC10.
RefSeqiNP_418412.1. NC_000913.3.
WP_001207201.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76959; AAC76959; b3985.
BAE77335; BAE77335; BAE77335.
GeneIDi948490.
KEGGiecj:JW3948.
eco:b3985.
PATRICi32123491. VBIEscCol129921_4098.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00339 Genomic DNA. Translation: CAA23623.1.
U00006 Genomic DNA. Translation: AAC43083.1.
U00096 Genomic DNA. Translation: AAC76959.1.
AP009048 Genomic DNA. Translation: BAE77335.1.
PIRiS12574. R5EC10.
RefSeqiNP_418412.1. NC_000913.3.
WP_001207201.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J7Zelectron microscopy3.9051-165[»]
3J9Yelectron microscopy3.9051-165[»]
3J9Zelectron microscopy3.60LD2-165[»]
3JA1electron microscopy3.60LJ2-165[»]
3JCJelectron microscopy3.70e1-165[»]
4UY8electron microscopy3.8051-148[»]
4V6Nelectron microscopy12.10AJ2-165[»]
4V6Oelectron microscopy14.70BJ2-165[»]
4V6Pelectron microscopy13.50BJ2-165[»]
4V6Qelectron microscopy11.50BJ2-165[»]
4V6Relectron microscopy11.50BJ2-165[»]
4V6Selectron microscopy13.10AJ2-165[»]
4V6Velectron microscopy9.80BJ2-165[»]
4V7Belectron microscopy6.80B51-165[»]
4V7Celectron microscopy7.60BJ1-165[»]
4V7Delectron microscopy7.60AJ1-165[»]
4V85X-ray3.20H1-165[»]
4V89X-ray3.70BH1-165[»]
4V9OX-ray2.90A5/C5/E51-165[»]
4V9PX-ray2.90A5/E51-165[»]
4YBBX-ray2.10DI2-136[»]
5ADYelectron microscopy4.5071-165[»]
5AFIelectron microscopy2.9051-165[»]
5GADelectron microscopy3.70I1-165[»]
5GAEelectron microscopy3.33I1-165[»]
5GAFelectron microscopy4.30I2-126[»]
5GAGelectron microscopy3.80I1-165[»]
5GAHelectron microscopy3.80I1-165[»]
5H5Uelectron microscopy3.00I2-165[»]
5IQRelectron microscopy3.00H1-165[»]
5IT8X-ray3.12DI2-136[»]
5J5BX-ray2.80DI2-136[»]
5J7LX-ray3.00DI2-136[»]
5J88X-ray3.32DI2-136[»]
5J8AX-ray3.10DI2-136[»]
5J91X-ray2.96DI2-136[»]
5JC9X-ray3.03DI2-136[»]
5KCRelectron microscopy3.601J1-165[»]
5KCSelectron microscopy3.901J1-165[»]
5KPSelectron microscopy3.90H1-165[»]
5KPVelectron microscopy4.10G1-165[»]
5KPWelectron microscopy3.90G1-165[»]
5KPXelectron microscopy3.90G1-165[»]
5L3Pelectron microscopy3.70J1-165[»]
5MDVelectron microscopy2.97H1-165[»]
5MDWelectron microscopy3.06H1-165[»]
5MDYelectron microscopy3.35H1-165[»]
5MDZelectron microscopy3.10H1-165[»]
ProteinModelPortaliP0A7J3.
SMRiP0A7J3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852784. 1 interactor.
DIPiDIP-35816N.
IntActiP0A7J3. 52 interactors.
MINTiMINT-1264502.
STRINGi511145.b3985.

Proteomic databases

EPDiP0A7J3.
PaxDbiP0A7J3.
PRIDEiP0A7J3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76959; AAC76959; b3985.
BAE77335; BAE77335; BAE77335.
GeneIDi948490.
KEGGiecj:JW3948.
eco:b3985.
PATRICi32123491. VBIEscCol129921_4098.

Organism-specific databases

EchoBASEiEB0864.
EcoGeneiEG10871. rplJ.

Phylogenomic databases

eggNOGiENOG4108VZM. Bacteria.
COG0244. LUCA.
HOGENOMiHOG000004851.
InParanoidiP0A7J3.
KOiK02864.
OMAiAKANPAF.
PhylomeDBiP0A7J3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10871-MONOMER.
MetaCyc:EG10871-MONOMER.

Miscellaneous databases

PROiPR:P0A7J3.

Family and domain databases

HAMAPiMF_00362. Ribosomal_L10. 1 hit.
InterProiView protein in InterPro
IPR022973. Ribosomal_L10.
IPR002363. Ribosomal_L10_eubac_CS.
IPR001790. Ribosomal_L10P.
PfamiView protein in Pfam
PF00466. Ribosomal_L10. 1 hit.
PROSITEiView protein in PROSITE
PS01109. RIBOSOMAL_L10. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL10_ECOLI
AccessioniPrimary (citable) accession number: P0A7J3
Secondary accession number(s): P02408, Q2M8S1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 12, 2017
This is version 107 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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. 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.