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Protein

50S ribosomal protein L7/L12

Gene

rplL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10873-MONOMER.
ECOL316407:JW3949-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L7/L12UniRule annotation
Alternative name(s):
L8
Gene namesi
Name:rplLUniRule annotation
Ordered Locus Names:b3986, JW3949
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10873. rplL.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic large ribosomal subunit Source: EcoliWiki
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication
Mutagenesisi67 – 671V → D: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication
Mutagenesisi70 – 701I → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication
Mutagenesisi71 – 711K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication
Mutagenesisi74 – 741R → M: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication
Mutagenesisi85 – 851K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication

Chemistry

ChEMBLiCHEMBL2363135.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved5 Publications
Chaini2 – 12112050S ribosomal protein L7/L12PRO_0000157528Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine; in L71 Publication
Modified residuei82 – 821N6-methyllysine; partial1 Publication

Post-translational modificationi

Acetylation of Ser-2 converts L12 to L7.
Lys-82 was found to be 50% monomethylated.1 Publication

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

EPDiP0A7K2.
PaxDbiP0A7K2.
PRIDEiP0A7K2.

2D gel databases

SWISS-2DPAGEP0A7K2.

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

Protein-protein interaction databases

BioGridi852783. 1 interaction.
DIPiDIP-36009N.
IntActiP0A7K2. 127 interactions.
MINTiMINT-1277405.
STRINGi511145.b3986.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 128Combined sources
Helixi17 – 3014Combined sources
Helixi33 – 5018Combined sources
Beta strandi55 – 617Combined sources
Helixi63 – 653Combined sources
Helixi66 – 7712Combined sources
Helixi81 – 899Combined sources
Beta strandi92 – 998Combined sources
Helixi101 – 11414Combined sources
Beta strandi117 – 1215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CTFX-ray1.70A48-121[»]
1RQSNMR-A48-121[»]
1RQTNMR-A/B2-38[»]
1RQUNMR-A/B2-121[»]
1RQVNMR-A/B2-121[»]
2BCWelectron microscopy11.20B54-121[»]
3J7Zelectron microscopy3.9061-121[»]
4UY8electron microscopy3.8062-31[»]
4V4Velectron microscopy15.00B3/B53-121[»]
4V4Welectron microscopy15.00B3/B53-121[»]
4V5Melectron microscopy7.80BL1-121[»]
4V5Nelectron microscopy7.60BL1-121[»]
4V7Belectron microscopy6.80B61-121[»]
4V7Delectron microscopy7.60AL2-121[»]
4V85X-ray3.20J/K/L/M1-121[»]
4V89X-ray3.70BJ/BK/BL/BM1-121[»]
4V9OX-ray2.90A61-121[»]
ProteinModelPortaliP0A7K2.
SMRiP0A7K2. Positions 2-121.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7K2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 12168Required for recruitment of EF-Tu and EF-G, and for EF-Tu and EF-G-promoted GTP hydrolysisAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein L7/L12P family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105KBC. Bacteria.
COG0222. LUCA.
HOGENOMiHOG000248813.
InParanoidiP0A7K2.
KOiK02935.
OMAiGLKETWG.
PhylomeDBiP0A7K2.

Family and domain databases

CDDicd00387. Ribosomal_L7_L12. 1 hit.
Gene3Di3.30.1390.10. 1 hit.
HAMAPiMF_00368. Ribosomal_L7_L12. 1 hit.
InterProiIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PfamiPF00542. Ribosomal_L12. 1 hit.
PF16320. Ribosomal_L12_N. 1 hit.
[Graphical view]
ProDomiPD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.
TIGRFAMsiTIGR00855. L12. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7K2-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:121
Mass (Da):12,295
Last modified:January 23, 2007 - v2
Checksum:i08B051A0CDAA527E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61D → F AA sequence (PubMed:9868784).Curated

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.
PIRiS12575. R5EC7.
RefSeqiNP_418413.1. NC_000913.3.
WP_000028878.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76960; AAC76960; b3986.
BAE77334; BAE77334; BAE77334.
GeneIDi948489.
KEGGiecj:JW3949.
eco:b3986.
PATRICi32123493. VBIEscCol129921_4099.

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.
PIRiS12575. R5EC7.
RefSeqiNP_418413.1. NC_000913.3.
WP_000028878.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CTFX-ray1.70A48-121[»]
1RQSNMR-A48-121[»]
1RQTNMR-A/B2-38[»]
1RQUNMR-A/B2-121[»]
1RQVNMR-A/B2-121[»]
2BCWelectron microscopy11.20B54-121[»]
3J7Zelectron microscopy3.9061-121[»]
4UY8electron microscopy3.8062-31[»]
4V4Velectron microscopy15.00B3/B53-121[»]
4V4Welectron microscopy15.00B3/B53-121[»]
4V5Melectron microscopy7.80BL1-121[»]
4V5Nelectron microscopy7.60BL1-121[»]
4V7Belectron microscopy6.80B61-121[»]
4V7Delectron microscopy7.60AL2-121[»]
4V85X-ray3.20J/K/L/M1-121[»]
4V89X-ray3.70BJ/BK/BL/BM1-121[»]
4V9OX-ray2.90A61-121[»]
ProteinModelPortaliP0A7K2.
SMRiP0A7K2. Positions 2-121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852783. 1 interaction.
DIPiDIP-36009N.
IntActiP0A7K2. 127 interactions.
MINTiMINT-1277405.
STRINGi511145.b3986.

Chemistry

ChEMBLiCHEMBL2363135.

2D gel databases

SWISS-2DPAGEP0A7K2.

Proteomic databases

EPDiP0A7K2.
PaxDbiP0A7K2.
PRIDEiP0A7K2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76960; AAC76960; b3986.
BAE77334; BAE77334; BAE77334.
GeneIDi948489.
KEGGiecj:JW3949.
eco:b3986.
PATRICi32123493. VBIEscCol129921_4099.

Organism-specific databases

EchoBASEiEB0866.
EcoGeneiEG10873. rplL.

Phylogenomic databases

eggNOGiENOG4105KBC. Bacteria.
COG0222. LUCA.
HOGENOMiHOG000248813.
InParanoidiP0A7K2.
KOiK02935.
OMAiGLKETWG.
PhylomeDBiP0A7K2.

Enzyme and pathway databases

BioCyciEcoCyc:EG10873-MONOMER.
ECOL316407:JW3949-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7K2.
PROiP0A7K2.

Family and domain databases

CDDicd00387. Ribosomal_L7_L12. 1 hit.
Gene3Di3.30.1390.10. 1 hit.
HAMAPiMF_00368. Ribosomal_L7_L12. 1 hit.
InterProiIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PfamiPF00542. Ribosomal_L12. 1 hit.
PF16320. Ribosomal_L12_N. 1 hit.
[Graphical view]
ProDomiPD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.
TIGRFAMsiTIGR00855. L12. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL7_ECOLI
AccessioniPrimary (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: September 7, 2016
This is version 110 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 L10.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.