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P0A7J3

- RL10_ECOLI

UniProt

P0A7J3 - RL10_ECOLI

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Protein

50S ribosomal protein L10

Gene

rplJ

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.
Protein L10 is also a translational repressor protein. It controls the translation of the rplJL-rpoBC operon by binding to its mRNA.

GO - Molecular functioni

  1. large ribosomal subunit rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. regulation of translation Source: UniProtKB-KW
  2. ribosome biogenesis Source: InterPro
  3. 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

Enzyme and pathway databases

BioCyciEcoCyc:EG10871-MONOMER.
ECOL316407:JW3948-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L10
Alternative name(s):
50S ribosomal protein L8
Gene namesi
Name:rplJ
Ordered Locus Names:b3985, JW3948
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10871. rplJ.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi156 – 16510Missing: 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 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 16516450S ribosomal protein L10PRO_0000154627Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371N6-acetyllysine1 Publication
Modified residuei105 – 1051N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A7J3.
PRIDEiP0A7J3.

Expressioni

Gene expression databases

GenevestigatoriP0A7J3.

Interactioni

Subunit structurei

Part of the ribosomal stalk of the 50S ribosomal subunit. 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).1 Publication

Protein-protein interaction databases

BioGridi852784. 1 interaction.
DIPiDIP-35816N.
IntActiP0A7J3. 52 interactions.
MINTiMINT-1264502.
STRINGi511145.b3985.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74
Helixi9 – 1810
Beta strandi24 – 263
Helixi34 – 4613
Beta strandi49 – 524
Helixi60 – 634
Turni64 – 696
Turni75 – 773
Beta strandi79 – 813
Beta strandi86 – 905
Helixi95 – 1039
Beta strandi105 – 1084
Turni117 – 1204
Beta strandi128 – 1303
Helixi134 – 1385
Helixi140 – 1478
Turni148 – 1569
Helixi158 – 1603

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J0Telectron microscopy12.10J2-165[»]
3J0Welectron microscopy14.70J2-165[»]
3J0Yelectron microscopy13.50J2-165[»]
3J11electron microscopy13.10J2-165[»]
3J12electron microscopy11.50J2-165[»]
3J14electron microscopy11.50J2-165[»]
3J37electron microscopy9.80J2-165[»]
3J5Oelectron microscopy6.8051-165[»]
3J5Uelectron microscopy7.60J1-165[»]
3J5Welectron microscopy7.60J1-165[»]
3SGFX-ray3.20H1-165[»]
3UOSX-ray3.70H1-165[»]
4KIXX-ray2.9051-165[»]
4KIZX-ray2.9051-165[»]
4KJ1X-ray2.9051-165[»]
4KJ5X-ray2.9051-165[»]
4KJ9X-ray2.9051-165[»]
ProteinModelPortaliP0A7J3.
SMRiP0A7J3. Positions 1-163.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L10P family.Curated

Phylogenomic databases

eggNOGiCOG0244.
HOGENOMiHOG000004851.
InParanoidiP0A7J3.
KOiK02864.
OMAiFSMEDPG.
OrthoDBiEOG6DNTDR.
PhylomeDBiP0A7J3.

Family and domain databases

HAMAPiMF_00362. Ribosomal_L10.
InterProiIPR022973. Ribosomal_L10.
IPR001790. Ribosomal_L10/acidic_P0.
IPR002363. Ribosomal_L10_eubac_CS.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
PROSITEiPS01109. RIBOSOMAL_L10. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841Y → YR AA sequence (PubMed:773698)Curated
Sequence conflicti84 – 841Y → YR AA sequence (PubMed:782920)Curated
Sequence conflicti84 – 841Y → YR AA sequence (PubMed:797648)Curated
Sequence conflicti116 – 1161E → Q AA sequence (PubMed:773698)Curated

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:
EMBL
GenBank
DDBJ
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.
YP_491476.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76959; AAC76959; b3985.
BAE77335; BAE77335; BAE77335.
GeneIDi12930514.
948490.
KEGGiecj:Y75_p3212.
eco:b3985.
PATRICi32123491. VBIEscCol129921_4098.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi S12574. R5EC10.
RefSeqi NP_418412.1. NC_000913.3.
YP_491476.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J0T electron microscopy 12.10 J 2-165 [» ]
3J0W electron microscopy 14.70 J 2-165 [» ]
3J0Y electron microscopy 13.50 J 2-165 [» ]
3J11 electron microscopy 13.10 J 2-165 [» ]
3J12 electron microscopy 11.50 J 2-165 [» ]
3J14 electron microscopy 11.50 J 2-165 [» ]
3J37 electron microscopy 9.80 J 2-165 [» ]
3J5O electron microscopy 6.80 5 1-165 [» ]
3J5U electron microscopy 7.60 J 1-165 [» ]
3J5W electron microscopy 7.60 J 1-165 [» ]
3SGF X-ray 3.20 H 1-165 [» ]
3UOS X-ray 3.70 H 1-165 [» ]
4KIX X-ray 2.90 5 1-165 [» ]
4KIZ X-ray 2.90 5 1-165 [» ]
4KJ1 X-ray 2.90 5 1-165 [» ]
4KJ5 X-ray 2.90 5 1-165 [» ]
4KJ9 X-ray 2.90 5 1-165 [» ]
ProteinModelPortali P0A7J3.
SMRi P0A7J3. Positions 1-163.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852784. 1 interaction.
DIPi DIP-35816N.
IntActi P0A7J3. 52 interactions.
MINTi MINT-1264502.
STRINGi 511145.b3985.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7J3.
PRIDEi P0A7J3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76959 ; AAC76959 ; b3985 .
BAE77335 ; BAE77335 ; BAE77335 .
GeneIDi 12930514.
948490.
KEGGi ecj:Y75_p3212.
eco:b3985.
PATRICi 32123491. VBIEscCol129921_4098.

Organism-specific databases

EchoBASEi EB0864.
EcoGenei EG10871. rplJ.

Phylogenomic databases

eggNOGi COG0244.
HOGENOMi HOG000004851.
InParanoidi P0A7J3.
KOi K02864.
OMAi FSMEDPG.
OrthoDBi EOG6DNTDR.
PhylomeDBi P0A7J3.

Enzyme and pathway databases

BioCyci EcoCyc:EG10871-MONOMER.
ECOL316407:JW3948-MONOMER.

Miscellaneous databases

PROi P0A7J3.

Gene expression databases

Genevestigatori P0A7J3.

Family and domain databases

HAMAPi MF_00362. Ribosomal_L10.
InterProi IPR022973. Ribosomal_L10.
IPR001790. Ribosomal_L10/acidic_P0.
IPR002363. Ribosomal_L10_eubac_CS.
[Graphical view ]
Pfami PF00466. Ribosomal_L10. 1 hit.
[Graphical view ]
PROSITEi PS01109. RIBOSOMAL_L10. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli."
    Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.
    Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The ribosomal protein L8 is a complex L7/L12 and L10."
    Pettersson I., Hardy S.J.S., Liljas A.
    FEBS Lett. 64:135-138(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-165.
    Strain: MRE-600.
  6. "The primary structure of protein L10 from Escherichia coli ribosomes."
    Dovgas N.V., Vinokurov L.M., Velmoga I.S., Alakhov Y.B., Ovchinnikov Y.A.
    FEBS Lett. 67:58-61(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-165, SEQUENCE REVISION.
    Strain: MRE-600.
  7. "Primary structure of protein L10 from the large subunit of Escherichia coli ribosomes."
    Heiland I., Brauer D., Wittmann-Liebold B.
    Hoppe-Seyler's Z. Physiol. Chem. 357:1751-1770(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-165.
    Strain: K12.
  8. "Feedback regulation of the rplJL-rpoBC ribosomal protein operon of Escherichia coli requires a region of mRNA secondary structure."
    Climie S.C., Friesen J.D.
    J. Mol. Biol. 198:371-381(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: MECHANISM OF TRANSLATION REGULATION.
  9. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  10. "Heptameric (L12)6/L10 rather than canonical pentameric complexes are found by tandem MS of intact ribosomes from thermophilic bacteria."
    Ilag L.L., Videler H., McKay A.R., Sobott F., Fucini P., Nierhaus K.H., Robinson C.V.
    Proc. Natl. Acad. Sci. U.S.A. 102:8192-8197(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, STOICHIOMETRY, MASS SPECTROMETRY.
  11. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-37 AND LYS-105, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  12. "Bacterial ribosome requires multiple L12 dimers for efficient initiation and elongation of protein synthesis involving IF2 and EF-G."
    Mandava C.S., Peisker K., Ederth J., Kumar R., Ge X., Szaflarski W., Sanyal S.
    Nucleic Acids Res. 40:2054-2064(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 156-ALA--ALA-165.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiRL10_ECOLI
AccessioniPrimary (citable) accession number: P0A7J3
Secondary accession number(s): P02408, Q2M8S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

External Data

Dasty 3