UniProtKB - P0A7K2 (RL7_ECOLI)
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Protein
50S ribosomal protein L7/L12
Gene
rplL
Organism
Escherichia coli (strain K12)
Status
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 Publications
Miscellaneous
Ribosomal protein L8 appears to be an aggregate of ribosomal proteins L7/L12 and L10.1 Publication
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. MetaCyc: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 |
|
Organism-specific databases
EcoGenei | EG10873. rplL. |
Subcellular locationi
GO - Cellular componenti
- cytosol Source: EcoCyc
- cytosolic large ribosomal subunit Source: EcoliWiki
- 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
Acetylation of Ser-2 converts L12 to L7.
Lys-82 was found to be 50% monomethylated.1 Publication
Keywords - PTMi
Acetylation, MethylationProteomic databases
EPDi | P0A7K2. |
PaxDbi | P0A7K2. |
PRIDEi | P0A7K2. |
2D gel databases
SWISS-2DPAGEi | P0A7K2. |
PTM databases
iPTMneti | 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 Publications
Binary interactionsi
GO - Molecular functioni
- protein homodimerization activity Source: CAFA
Protein-protein interaction databases
BioGridi | 852783. 1 interactor. |
DIPi | DIP-36009N. |
IntActi | P0A7K2. 135 interactors. |
STRINGi | 316385.ECDH10B_4174. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Helixi | 5 – 12 | Combined sources | 8 | |
Helixi | 17 – 30 | Combined sources | 14 | |
Helixi | 33 – 50 | Combined sources | 18 | |
Beta strandi | 55 – 61 | Combined sources | 7 | |
Helixi | 63 – 65 | Combined sources | 3 | |
Helixi | 66 – 77 | Combined sources | 12 | |
Helixi | 81 – 89 | Combined sources | 9 | |
Beta strandi | 92 – 99 | Combined sources | 8 | |
Helixi | 101 – 114 | Combined sources | 14 | |
Beta strandi | 117 – 121 | Combined sources | 5 |
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 | J/K/L/M | 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 | [»] | |
ProteinModelPortali | P0A7K2. | |||||
SMRi | P0A7K2. | |||||
ModBasei | Search... | |||||
MobiDBi | 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
Belongs to the bacterial ribosomal protein bL12 family.UniRule annotation
Phylogenomic databases
eggNOGi | ENOG4105KBC. Bacteria. COG0222. LUCA. |
HOGENOMi | HOG000248813. |
InParanoidi | P0A7K2. |
KOi | K02935. |
OMAi | VDNAPKP. |
PhylomeDBi | P0A7K2. |
Family and domain databases
CDDi | cd00387. Ribosomal_L7_L12. 1 hit. |
Gene3Di | 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. |
Pfami | View protein in Pfam PF00542. Ribosomal_L12. 1 hit. PF16320. Ribosomal_L12_N. 1 hit. |
ProDomi | View protein in ProDom or Entries sharing at least one domain PD001326. Ribosomal_L7/L12_C. 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
P0A7K2-1 [UniParc]FASTAAdd to basket
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
Molecular mass is 12206.7 Da from positions 2 - 121. Determined by MALDI. Non-methylated.1 Publication
Molecular mass is 66643±13 Da from positions 2 - 121. Determined by ESI. Isolated L10(L12)4.1 Publication
Molecular mass is 12223±1 Da from positions 2 - 121. Determined by ESI. L7, acetylated Ser-2.1 Publication
Molecular mass is 12164±1 Da from positions 2 - 121. Determined by ESI. L12, unacetylated.1 Publication
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_LN832404.1. |
Genome annotation databases
EnsemblBacteriai | AAC76960; AAC76960; b3986. BAE77334; BAE77334; BAE77334. |
GeneIDi | 948489. |
KEGGi | ecj:JW3949. eco:b3986. |
PATRICi | fig|1411691.4.peg.2726. |
Similar proteinsi
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: | March 28, 2018 | |
This is version 124 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |