UniProtKB - P0A7K2 (RL7_ECOLI)
50S ribosomal protein L7/L12
rplL
Functioni
The binding site for several of the GTPase factors involved in protein synthesis (IF-2, EF-Tu, EF-G and RF3). Is thus essential for accurate translation. Deletion of 1 of the L12 dimers from the ribosome (by deleting the binding site on L10) leads to decreased IF-2 association with the 70S ribosome and decreased stimulation of the GTPase activity of EF-G.
2 PublicationsMiscellaneous
GO - Molecular functioni
- protein homodimerization activity Source: CAFA
- ribosome binding Source: CAFA
- structural constituent of ribosome Source: InterPro
GO - Biological processi
- translation Source: CAFA
Keywordsi
Molecular function | Ribonucleoprotein, Ribosomal protein |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10873-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: 50S ribosomal protein L7/L12UniRule annotationAlternative name(s): L8 Large ribosomal subunit protein bL121 Publication |
Gene namesi | Name:rplLUniRule annotation Ordered Locus Names:b3986, JW3949 |
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: EcoliWiki
Other locations
- cytoplasm Source: ComplexPortal
- large ribosomal subunit Source: CAFA
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 66 | K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication | 1 | |
Mutagenesisi | 67 | V → D: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication | 1 | |
Mutagenesisi | 70 | I → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication | 1 | |
Mutagenesisi | 71 | K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication | 1 | |
Mutagenesisi | 74 | R → M: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication | 1 | |
Mutagenesisi | 85 | K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed5 Publications | |||
ChainiPRO_0000157528 | 2 – 121 | 50S ribosomal protein L7/L12Add BLAST | 120 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserine; in L71 Publication | 1 | |
Modified residuei | 82 | N6-methyllysine; partial1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, MethylationProteomic databases
jPOSTi | P0A7K2 |
PaxDbi | P0A7K2 |
PRIDEi | P0A7K2 |
2D gel databases
SWISS-2DPAGEi | P0A7K2 |
PTM databases
iPTMneti | P0A7K2 |
MetOSitei | P0A7K2 |
Interactioni
Subunit structurei
Homodimer. Part of the 50S ribosomal subunit; present in 4 copies per ribosome. L7/L12 forms dimers with an elongated shape. Two dimers associate with a copy of L10 to form part of the ribosomal stalk (called L8). The ribosomal stalk helps the ribosome interact with GTP-bound translation factors.
Forms a pentameric L10(L12)2(L12)2 complex, where L10 forms an elongated spine to which 2 L12 dimers bind in a sequential fashion.
2 PublicationsBinary interactionsi
P0A7K2
GO - Molecular functioni
- protein homodimerization activity Source: CAFA
Protein-protein interaction databases
BioGRIDi | 852783, 3 interactors |
ComplexPortali | CPX-3807, 50S large ribosomal subunit |
DIPi | DIP-36009N |
IntActi | P0A7K2, 135 interactors |
STRINGi | 511145.b3986 |
Structurei
Secondary structure
3D structure databases
SMRi | P0A7K2 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A7K2 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 54 – 121 | Required for recruitment of EF-Tu and EF-G, and for EF-Tu and EF-G-promoted GTP hydrolysisAdd BLAST | 68 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0222, Bacteria |
HOGENOMi | CLU_086499_3_2_6 |
InParanoidi | P0A7K2 |
PhylomeDBi | P0A7K2 |
Family and domain databases
CDDi | cd00387, Ribosomal_L7_L12, 1 hit |
DisProti | DP01650 |
Gene3Di | 1.20.5.710, 1 hit 3.30.1390.10, 1 hit |
HAMAPi | MF_00368, Ribosomal_L7_L12, 1 hit |
InterProi | View protein in InterPro IPR000206, Ribosomal_L7/12 IPR014719, Ribosomal_L7/12_C/ClpS-like IPR013823, Ribosomal_L7/L12_C IPR008932, Ribosomal_L7/L12_oligo IPR036235, Ribosomal_L7/L12_oligo_N_sf |
PANTHERi | PTHR45987, PTHR45987, 1 hit |
Pfami | View protein in Pfam PF00542, Ribosomal_L12, 1 hit PF16320, Ribosomal_L12_N, 1 hit |
SUPFAMi | SSF48300, SSF48300, 1 hit SSF54736, SSF54736, 1 hit |
TIGRFAMsi | TIGR00855, L12, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MSITKDQIIE AVAAMSVMDV VELISAMEEK FGVSAAAAVA VAAGPVEAAE
60 70 80 90 100
EKTEFDVILK AAGANKVAVI KAVRGATGLG LKEAKDLVES APAALKEGVS
110 120
KDDAEALKKA LEEAGAEVEV K
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 6 | D → F AA sequence (PubMed:9868784).Curated | 1 |
Mass spectrometryi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V00339 Genomic DNA Translation: CAA23624.1 M38301 Genomic DNA Translation: AAA24573.1 U00006 Genomic DNA Translation: AAC43084.1 U00096 Genomic DNA Translation: AAC76960.1 AP009048 Genomic DNA Translation: BAE77334.1 |
PIRi | S12575, R5EC7 |
RefSeqi | NP_418413.1, NC_000913.3 WP_000028878.1, NZ_STEB01000045.1 |
Genome annotation databases
EnsemblBacteriai | AAC76960; AAC76960; b3986 BAE77334; BAE77334; BAE77334 |
GeneIDi | 67415313 948489 |
KEGGi | ecj:JW3949 eco:b3986 |
PATRICi | fig|1411691.4.peg.2726 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | V00339 Genomic DNA Translation: CAA23624.1 M38301 Genomic DNA Translation: AAA24573.1 U00006 Genomic DNA Translation: AAC43084.1 U00096 Genomic DNA Translation: AAC76960.1 AP009048 Genomic DNA Translation: BAE77334.1 |
PIRi | S12575, R5EC7 |
RefSeqi | NP_418413.1, NC_000913.3 WP_000028878.1, NZ_STEB01000045.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1CTF | X-ray | 1.70 | A | 48-121 | [»] | |
1RQS | NMR | - | A | 48-121 | [»] | |
1RQT | NMR | - | A/B | 2-38 | [»] | |
1RQU | NMR | - | A/B | 2-121 | [»] | |
1RQV | NMR | - | A/B | 2-121 | [»] | |
2BCW | electron microscopy | 11.20 | B | 54-121 | [»] | |
3J7Z | electron microscopy | 3.90 | 6 | 1-121 | [»] | |
4UY8 | electron microscopy | 3.80 | 6 | 2-31 | [»] | |
4V4V | electron microscopy | 15.00 | B3/B5 | 3-121 | [»] | |
4V4W | electron microscopy | 15.00 | B3/B5 | 3-121 | [»] | |
4V5M | electron microscopy | 7.80 | BL | 1-121 | [»] | |
4V5N | electron microscopy | 7.60 | BL | 1-121 | [»] | |
4V7B | electron microscopy | 6.80 | B6 | 1-121 | [»] | |
4V7D | electron microscopy | 7.60 | AL | 2-121 | [»] | |
4V85 | X-ray | 3.20 | BJ/BK/BL/BM | 1-121 | [»] | |
4V89 | X-ray | 3.70 | BJ/BK/BL/BM | 1-121 | [»] | |
4V9O | X-ray | 2.90 | A6 | 1-121 | [»] | |
5KCS | electron microscopy | 3.90 | 1L | 1-121 | [»] | |
6I0Y | electron microscopy | 3.20 | 6 | 1-121 | [»] | |
7N2C | electron microscopy | 2.72 | LG | 1-121 | [»] | |
SMRi | P0A7K2 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 852783, 3 interactors |
ComplexPortali | CPX-3807, 50S large ribosomal subunit |
DIPi | DIP-36009N |
IntActi | P0A7K2, 135 interactors |
STRINGi | 511145.b3986 |
PTM databases
iPTMneti | P0A7K2 |
MetOSitei | P0A7K2 |
2D gel databases
SWISS-2DPAGEi | P0A7K2 |
Proteomic databases
jPOSTi | P0A7K2 |
PaxDbi | P0A7K2 |
PRIDEi | P0A7K2 |
Genome annotation databases
EnsemblBacteriai | AAC76960; AAC76960; b3986 BAE77334; BAE77334; BAE77334 |
GeneIDi | 67415313 948489 |
KEGGi | ecj:JW3949 eco:b3986 |
PATRICi | fig|1411691.4.peg.2726 |
Organism-specific databases
EchoBASEi | EB0866 |
Phylogenomic databases
eggNOGi | COG0222, Bacteria |
HOGENOMi | CLU_086499_3_2_6 |
InParanoidi | P0A7K2 |
PhylomeDBi | P0A7K2 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10873-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P0A7K2 |
PROi | PR:P0A7K2 |
Family and domain databases
CDDi | cd00387, Ribosomal_L7_L12, 1 hit |
DisProti | DP01650 |
Gene3Di | 1.20.5.710, 1 hit 3.30.1390.10, 1 hit |
HAMAPi | MF_00368, Ribosomal_L7_L12, 1 hit |
InterProi | View protein in InterPro IPR000206, Ribosomal_L7/12 IPR014719, Ribosomal_L7/12_C/ClpS-like IPR013823, Ribosomal_L7/L12_C IPR008932, Ribosomal_L7/L12_oligo IPR036235, Ribosomal_L7/L12_oligo_N_sf |
PANTHERi | PTHR45987, PTHR45987, 1 hit |
Pfami | View protein in Pfam PF00542, Ribosomal_L12, 1 hit PF16320, Ribosomal_L12_N, 1 hit |
SUPFAMi | SSF48300, SSF48300, 1 hit SSF54736, SSF54736, 1 hit |
TIGRFAMsi | TIGR00855, L12, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RL7_ECOLI | |
Accessioni | P0A7K2Primary (citable) accession number: P0A7K2 Secondary accession number(s): P02392, Q2M8S2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 144 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