UniProtKB - P0A7J3 (RL10_ECOLI)
50S ribosomal protein L10
rplJ
Functioni
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
1 PublicationProtein L10 is also a translational repressor protein. It controls the translation of the rplJL-rpoBC operon by binding to its mRNA.
1 PublicationMiscellaneous
GO - Molecular functioni
- large ribosomal subunit rRNA binding Source: UniProtKB-UniRule
- ribosome binding Source: CAFA
- structural constituent of ribosome Source: GO_Central
GO - Biological processi
- cytoplasmic translation Source: ComplexPortal
- negative regulation of translation Source: CAFA
- translation Source: CAFA
Keywordsi
Molecular function | Repressor, Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding |
Biological process | Translation regulation |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10871-MONOMER |
Protein family/group databases
MoonProti | P0A7J3 |
Names & Taxonomyi
Protein namesi | Recommended name: 50S ribosomal protein L10Alternative name(s): 50S ribosomal protein L8 Large ribosomal subunit protein uL101 Publication |
Gene namesi | Name:rplJ Ordered Locus Names:b3985, JW3948 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytosol
- cytosol Source: EcoCyc
- cytosolic large ribosomal subunit Source: EcoCyc
Other locations
- cytoplasm Source: ComplexPortal
- large ribosomal subunit Source: CAFA
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 156 – 165 | Missing : 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 | 10 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed3 Publications | |||
ChainiPRO_0000154627 | 2 – 165 | 50S ribosomal protein L10Add BLAST | 164 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 37 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 105 | N6-acetyllysine1 Publication | 1 |
Keywords - PTMi
AcetylationProteomic databases
jPOSTi | P0A7J3 |
PaxDbi | P0A7J3 |
PRIDEi | P0A7J3 |
PTM databases
iPTMneti | P0A7J3 |
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 PublicationsBinary interactionsi
P0A7J3
With | #Exp. | IntAct |
---|---|---|
rpiB [P37351] | 2 | EBI-546827,EBI-557460 |
Protein-protein interaction databases
BioGRIDi | 852784, 1 interactor |
ComplexPortali | CPX-3807, 50S large ribosomal subunit |
DIPi | DIP-35816N |
IntActi | P0A7J3, 111 interactors |
STRINGi | 511145.b3985 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P0A7J3 |
SMRi | P0A7J3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0244, Bacteria |
HOGENOMi | CLU_092227_0_2_6 |
InParanoidi | P0A7J3 |
OMAi | VRDQKQA |
PhylomeDBi | P0A7J3 |
Family and domain databases
CDDi | cd05797, Ribosomal_L10, 1 hit |
Gene3Di | 3.30.70.1730, 1 hit |
HAMAPi | MF_00362, Ribosomal_L10, 1 hit |
InterProi | View protein in InterPro IPR022973, Ribosomal_L10 IPR043141, Ribosomal_L10-like_sf IPR002363, Ribosomal_L10_eubac_CS IPR001790, Ribosomal_L10P |
PANTHERi | PTHR11560, PTHR11560, 1 hit |
Pfami | View protein in Pfam PF00466, Ribosomal_L10, 1 hit |
SUPFAMi | SSF160369, SSF160369, 1 hit |
PROSITEi | View protein in PROSITE PS01109, RIBOSOMAL_L10, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 84 | Y → YR AA sequence (PubMed:773698).Curated | 1 | |
Sequence conflicti | 84 | Y → YR AA sequence (PubMed:782920).Curated | 1 | |
Sequence conflicti | 84 | Y → YR AA sequence (PubMed:797648).Curated | 1 | |
Sequence conflicti | 116 | E → Q AA sequence (PubMed:773698).Curated | 1 |
Mass spectrometryi
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 |
PIRi | S12574, R5EC10 |
RefSeqi | NP_418412.1, NC_000913.3 WP_001207201.1, NZ_STEB01000045.1 |
Genome annotation databases
EnsemblBacteriai | AAC76959; AAC76959; b3985 BAE77335; BAE77335; BAE77335 |
GeneIDi | 67415314 948490 |
KEGGi | ecj:JW3948 eco:b3985 |
PATRICi | fig|1411691.4.peg.2727 |
Similar proteinsi
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 |
PIRi | S12574, R5EC10 |
RefSeqi | NP_418412.1, NC_000913.3 WP_001207201.1, NZ_STEB01000045.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3J7Z | electron microscopy | 3.90 | 5 | 1-165 | [»] | |
3J9Y | electron microscopy | 3.90 | 5 | 1-165 | [»] | |
3J9Z | electron microscopy | 3.60 | LD | 2-165 | [»] | |
3JA1 | electron microscopy | 3.60 | LJ | 2-165 | [»] | |
3JCJ | electron microscopy | 3.70 | e | 1-165 | [»] | |
4UY8 | electron microscopy | 3.80 | 5 | 1-148 | [»] | |
4V6N | electron microscopy | 12.10 | AJ | 2-165 | [»] | |
4V6O | electron microscopy | 14.70 | BJ | 2-165 | [»] | |
4V6P | electron microscopy | 13.50 | BJ | 2-165 | [»] | |
4V6Q | electron microscopy | 11.50 | BJ | 2-165 | [»] | |
4V6R | electron microscopy | 11.50 | BJ | 2-165 | [»] | |
4V6S | electron microscopy | 13.10 | AJ | 2-165 | [»] | |
4V6V | electron microscopy | 9.80 | BJ | 2-165 | [»] | |
4V7B | electron microscopy | 6.80 | B5 | 1-165 | [»] | |
4V7C | electron microscopy | 7.60 | BJ | 1-165 | [»] | |
4V7D | electron microscopy | 7.60 | AJ | 1-165 | [»] | |
4V85 | X-ray | 3.20 | BH | 1-165 | [»] | |
4V89 | X-ray | 3.70 | BH | 1-165 | [»] | |
4V9O | X-ray | 2.90 | A5/C5/E5 | 1-165 | [»] | |
4V9P | X-ray | 2.90 | A5/E5 | 1-165 | [»] | |
4YBB | X-ray | 2.10 | DI | 2-136 | [»] | |
5ADY | electron microscopy | 4.50 | 7 | 1-165 | [»] | |
5AFI | electron microscopy | 2.90 | 5 | 1-165 | [»] | |
5GAD | electron microscopy | 3.70 | I | 1-165 | [»] | |
5GAE | electron microscopy | 3.33 | I | 1-165 | [»] | |
5GAF | electron microscopy | 4.30 | I | 2-126 | [»] | |
5GAG | electron microscopy | 3.80 | I | 1-165 | [»] | |
5GAH | electron microscopy | 3.80 | I | 1-165 | [»] | |
5H5U | electron microscopy | 3.00 | I | 2-165 | [»] | |
5IQR | electron microscopy | 3.00 | H | 1-165 | [»] | |
5IT8 | X-ray | 3.12 | DI | 2-136 | [»] | |
5J5B | X-ray | 2.80 | DI | 2-136 | [»] | |
5J7L | X-ray | 3.00 | DI | 2-136 | [»] | |
5J88 | X-ray | 3.32 | DI | 2-136 | [»] | |
5J8A | X-ray | 3.10 | DI | 2-136 | [»] | |
5J91 | X-ray | 2.96 | DI | 2-136 | [»] | |
5JC9 | X-ray | 3.03 | DI | 2-136 | [»] | |
5KCR | electron microscopy | 3.60 | 1J | 1-165 | [»] | |
5KCS | electron microscopy | 3.90 | 1J | 1-165 | [»] | |
5KPS | electron microscopy | 3.90 | H | 1-165 | [»] | |
5KPV | electron microscopy | 4.10 | G | 1-165 | [»] | |
5KPW | electron microscopy | 3.90 | G | 1-165 | [»] | |
5KPX | electron microscopy | 3.90 | G | 1-165 | [»] | |
5L3P | electron microscopy | 3.70 | J | 1-165 | [»] | |
5MDV | electron microscopy | 2.97 | H | 1-165 | [»] | |
5MDW | electron microscopy | 3.06 | H | 1-165 | [»] | |
5MDY | electron microscopy | 3.35 | H | 1-165 | [»] | |
5MDZ | electron microscopy | 3.10 | H | 1-165 | [»] | |
5NCO | electron microscopy | 4.80 | I | 2-126 | [»] | |
5NP6 | electron microscopy | 3.60 | 3 | 1-131 | [»] | |
5O2R | electron microscopy | 3.40 | 5 | 1-131 | [»] | |
5U9F | electron microscopy | 3.20 | 10 | 1-165 | [»] | |
5U9G | electron microscopy | 3.20 | 10 | 1-165 | [»] | |
5UYK | electron microscopy | 3.90 | 10 | 1-131 | [»] | |
5UYL | electron microscopy | 3.60 | 10 | 1-131 | [»] | |
5UYM | electron microscopy | 3.20 | 10 | 1-131 | [»] | |
5UYN | electron microscopy | 4.00 | 10 | 1-131 | [»] | |
5UYP | electron microscopy | 3.90 | 10 | 1-131 | [»] | |
5UYQ | electron microscopy | 3.80 | 10 | 1-131 | [»] | |
5WDT | electron microscopy | 3.00 | 5 | 1-131 | [»] | |
5WE4 | electron microscopy | 3.10 | 5 | 1-131 | [»] | |
5WE6 | electron microscopy | 3.40 | 5 | 1-131 | [»] | |
5WFK | electron microscopy | 3.40 | 5 | 1-131 | [»] | |
6BU8 | electron microscopy | 3.50 | 10 | 1-131 | [»] | |
6BY1 | X-ray | 3.94 | C5 | 2-110 | [»] | |
6C4I | electron microscopy | 3.24 | I | 1-165 | [»] | |
6GWT | electron microscopy | 3.80 | 5 | 1-131 | [»] | |
6GXM | electron microscopy | 3.80 | 5 | 1-131 | [»] | |
6GXN | electron microscopy | 3.90 | 5 | 1-131 | [»] | |
6GXO | electron microscopy | 3.90 | 5 | 1-131 | [»] | |
6GXP | electron microscopy | 4.40 | 5 | 1-131 | [»] | |
6HRM | electron microscopy | 2.96 | H | 2-131 | [»] | |
6I0Y | electron microscopy | 3.20 | 5 | 1-165 | [»] | |
6O9K | electron microscopy | 4.00 | G | 1-117 | [»] | |
6Q97 | electron microscopy | 3.90 | H | 2-131 | [»] | |
6Q98 | electron microscopy | 4.30 | H | 1-165 | [»] | |
6Q9A | electron microscopy | 3.70 | H | 2-131 | [»] | |
6WD6 | electron microscopy | 3.70 | h | 1-131 | [»] | |
6WDB | electron microscopy | 4.00 | h | 1-131 | [»] | |
6WDC | electron microscopy | 4.20 | h | 1-131 | [»] | |
6WDD | electron microscopy | 3.20 | h | 1-131 | [»] | |
6WDE | electron microscopy | 3.00 | h | 1-131 | [»] | |
6WDF | electron microscopy | 3.30 | h | 1-131 | [»] | |
6WDG | electron microscopy | 3.30 | h | 1-131 | [»] | |
6WDH | electron microscopy | 4.30 | h | 1-131 | [»] | |
6WDI | electron microscopy | 4.00 | h | 1-131 | [»] | |
6WDJ | electron microscopy | 3.70 | h | 1-131 | [»] | |
6WDK | electron microscopy | 3.60 | h | 1-131 | [»] | |
6WDL | electron microscopy | 3.70 | h | 1-131 | [»] | |
6WDM | electron microscopy | 3.60 | h | 1-131 | [»] | |
6WNT | electron microscopy | 3.10 | h | 1-131 | [»] | |
6WNV | electron microscopy | 3.50 | h | 1-131 | [»] | |
6WNW | electron microscopy | 3.20 | h | 1-131 | [»] | |
6XZ7 | electron microscopy | 2.10 | H | 2-136 | [»] | |
6XZA | electron microscopy | 2.66 | H2 | 2-136 | [»] | |
6XZB | electron microscopy | 2.54 | H2 | 2-136 | [»] | |
7ABZ | electron microscopy | 3.21 | H | 2-131 | [»] | |
7AC7 | electron microscopy | 3.08 | H | 2-131 | [»] | |
7BL5 | electron microscopy | 3.30 | e | 1-165 | [»] | |
7BV8 | electron microscopy | 3.14 | I | 1-165 | [»] | |
7JSZ | electron microscopy | 3.70 | h | 1-165 | [»] | |
7JT2 | electron microscopy | 3.50 | h | 1-165 | [»] | |
7JT3 | electron microscopy | 3.70 | h | 1-165 | [»] | |
7K50 | electron microscopy | 3.40 | h | 1-131 | [»] | |
7K51 | electron microscopy | 3.50 | h | 1-131 | [»] | |
7K52 | electron microscopy | 3.40 | h | 1-131 | [»] | |
7K53 | electron microscopy | 3.20 | h | 1-131 | [»] | |
7K54 | electron microscopy | 3.20 | h | 1-131 | [»] | |
7K55 | electron microscopy | 3.30 | h | 1-131 | [»] | |
7LV0 | electron microscopy | 3.20 | h | 1-131 | [»] | |
7N1P | electron microscopy | 2.33 | LJ | 1-165 | [»] | |
7N2C | electron microscopy | 2.72 | LJ | 1-165 | [»] | |
7N2V | electron microscopy | 2.54 | LJ | 1-165 | [»] | |
7OJ0 | electron microscopy | 3.50 | 5 | 2-131 | [»] | |
7PJV | electron microscopy | 3.10 | 5 | 1-165 | [»] | |
7PJY | electron microscopy | 3.10 | 5 | 1-165 | [»] | |
AlphaFoldDBi | P0A7J3 | |||||
SMRi | P0A7J3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 852784, 1 interactor |
ComplexPortali | CPX-3807, 50S large ribosomal subunit |
DIPi | DIP-35816N |
IntActi | P0A7J3, 111 interactors |
STRINGi | 511145.b3985 |
Protein family/group databases
MoonProti | P0A7J3 |
PTM databases
iPTMneti | P0A7J3 |
Proteomic databases
jPOSTi | P0A7J3 |
PaxDbi | P0A7J3 |
PRIDEi | P0A7J3 |
Genome annotation databases
EnsemblBacteriai | AAC76959; AAC76959; b3985 BAE77335; BAE77335; BAE77335 |
GeneIDi | 67415314 948490 |
KEGGi | ecj:JW3948 eco:b3985 |
PATRICi | fig|1411691.4.peg.2727 |
Organism-specific databases
EchoBASEi | EB0864 |
Phylogenomic databases
eggNOGi | COG0244, Bacteria |
HOGENOMi | CLU_092227_0_2_6 |
InParanoidi | P0A7J3 |
OMAi | VRDQKQA |
PhylomeDBi | P0A7J3 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10871-MONOMER |
Miscellaneous databases
PROi | PR:P0A7J3 |
Family and domain databases
CDDi | cd05797, Ribosomal_L10, 1 hit |
Gene3Di | 3.30.70.1730, 1 hit |
HAMAPi | MF_00362, Ribosomal_L10, 1 hit |
InterProi | View protein in InterPro IPR022973, Ribosomal_L10 IPR043141, Ribosomal_L10-like_sf IPR002363, Ribosomal_L10_eubac_CS IPR001790, Ribosomal_L10P |
PANTHERi | PTHR11560, PTHR11560, 1 hit |
Pfami | View protein in Pfam PF00466, Ribosomal_L10, 1 hit |
SUPFAMi | SSF160369, SSF160369, 1 hit |
PROSITEi | View protein in PROSITE PS01109, RIBOSOMAL_L10, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RL10_ECOLI | |
Accessioni | P0A7J3Primary (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: | May 25, 2022 | |
This is version 142 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Ribosomal proteins
Ribosomal proteins families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families