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P0A7J3 (RL10_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L10
Alternative name(s):
50S ribosomal protein L8
Gene names
Name:rplJ
Ordered Locus Names:b3985, JW3948
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. HAMAP-Rule MF_00362

Protein L10 is also a translational repressor protein. It controls the translation of the rplJL-rpoBC operon by binding to its mRNA. HAMAP-Rule MF_00362

Subunit structure

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). Ref.10

Miscellaneous

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

Sequence similarities

Belongs to the ribosomal protein L10P family.

Mass spectrometry

Molecular mass is 17581.1 Da from positions 2 - 165. Determined by MALDI. Ref.9

Molecular mass is 66643±13 Da from positions 2 - 165. Determined by ESI. Isolated L10(L12)4. Ref.10

Molecular mass is 17580±2 Da from positions 2 - 165. Determined by ESI. Ref.10

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6 Ref.7
Chain2 – 16516450S ribosomal protein L10 HAMAP-Rule MF_00362
PRO_0000154627

Amino acid modifications

Modified residue371N6-acetyllysine Ref.11
Modified residue1051N6-acetyllysine Ref.11

Experimental info

Mutagenesis156 – 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. Ref.12
Sequence conflict841Y → YR AA sequence Ref.5
Sequence conflict841Y → YR AA sequence Ref.6
Sequence conflict841Y → YR AA sequence Ref.7
Sequence conflict1161E → Q AA sequence Ref.5

Secondary structure

................................... 165
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7J3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F15822B0EDB6AC02

FASTA16517,712
        10         20         30         40         50         60 
MALNLQDKQA IVAEVSEVAK GALSAVVADS RGVTVDKMTE LRKAGREAGV YMRVVRNTLL 

        70         80         90        100        110        120 
RRAVEGTPFE CLKDAFVGPT LIAYSMEHPG AAARLFKEFA KANAKFEVKA AAFEGELIPA 

       130        140        150        160 
SQIDRLATLP TYEEAIARLM ATMKEASAGK LVRTLAAVRD AKEAA 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00339 Genomic DNA. Translation: CAA23623.1.
U00006 Genomic DNA. Translation: AAC43083.1.
U00096 Genomic DNA. Translation: AAC76959.1.
AP009048 Genomic DNA. Translation: BAE77335.1.
PIRR5EC10. S12574.
RefSeqNP_418412.1. NC_000913.3.
YP_491476.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J0Telectron microscopy12.10J2-164[»]
3J0Welectron microscopy14.70J2-164[»]
3J0Yelectron microscopy13.50J2-164[»]
3J11electron microscopy13.10J2-164[»]
3J12electron microscopy11.50J2-164[»]
3J14electron microscopy11.50J2-164[»]
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[»]
ProteinModelPortalP0A7J3.
SMRP0A7J3. Positions 1-163.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852784. 1 interaction.
DIPDIP-35816N.
IntActP0A7J3. 52 interactions.
MINTMINT-1264502.
STRING511145.b3985.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7J3.
PRIDEP0A7J3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76959; AAC76959; b3985.
BAE77335; BAE77335; BAE77335.
GeneID12930514.
948490.
KEGGecj:Y75_p3212.
eco:b3985.
PATRIC32123491. VBIEscCol129921_4098.

Organism-specific databases

EchoBASEEB0864.
EcoGeneEG10871. rplJ.

Phylogenomic databases

eggNOGCOG0244.
HOGENOMHOG000004851.
KOK02864.
OMAEGTDFEC.
OrthoDBEOG6DNTDR.
PhylomeDBP0A7J3.
ProtClustDBPRK00099.

Enzyme and pathway databases

BioCycEcoCyc:EG10871-MONOMER.
ECOL316407:JW3948-MONOMER.

Gene expression databases

GenevestigatorP0A7J3.

Family and domain databases

HAMAPMF_00362. Ribosomal_L10.
InterProIPR022973. Ribosomal_L10.
IPR001790. Ribosomal_L10/acidic_P0.
IPR002363. Ribosomal_L10_eubac_CS.
[Graphical view]
PANTHERPTHR11560:SF8. PTHR11560:SF8. 1 hit.
PfamPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
PROSITEPS01109. RIBOSOMAL_L10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP0A7J3.

Entry information

Entry nameRL10_ECOLI
AccessionPrimary (citable) accession number: P0A7J3
Secondary accession number(s): P02408, Q2M8S1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene