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P0A7K2 - RL7_ECOLI

UniProt

P0A7K2 - RL7_ECOLI

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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

  1. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10873. rplL.

Subcellular locationi

GO - Cellular componenti

  1. 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 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.

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PaxDbiP0A7K2.
PRIDEiP0A7K2.

2D gel databases

SWISS-2DPAGEP0A7K2.

PTM databases

PhosSiteiP0810430.

Expressioni

Gene expression databases

GenevestigatoriP0A7K2.

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 – 73Combined sources
Beta strandi9 – 135Combined sources
Helixi17 – 204Combined sources
Beta strandi23 – 253Combined sources
Helixi26 – 294Combined 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[»]
2GYAelectron microscopy15.003/53-121[»]
2GYCelectron microscopy15.003/53-121[»]
2XTGelectron microscopy7.80L1-121[»]
2XUXelectron microscopy7.60L1-121[»]
3J5Oelectron microscopy6.8061-121[»]
3J5Welectron microscopy7.60L2-121[»]
3J7Zelectron microscopy3.9061-121[»]
3SGFX-ray3.20J/K/L/M1-121[»]
3UOSX-ray3.70J/K/L/M1-121[»]
4KIXX-ray2.9061-121[»]
ProteinModelPortaliP0A7K2.
SMRiP0A7K2. Positions 3-121.
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

eggNOGiCOG0222.
HOGENOMiHOG000248813.
InParanoidiP0A7K2.
KOiK02935.
OMAiASMSVME.
OrthoDBiEOG6WMJ69.
PhylomeDBiP0A7K2.

Family and domain databases

Gene3Di3.30.1390.10. 1 hit.
HAMAPiMF_00368. Ribosomal_L7_L12.
InterProiIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PANTHERiPTHR11809. PTHR11809. 1 hit.
PfamiPF00542. Ribosomal_L12. 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.
YP_491475.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76960; AAC76960; b3986.
BAE77334; BAE77334; BAE77334.
GeneIDi12930512.
948489.
KEGGiecj:Y75_p3211.
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.
YP_491475.1. NC_007779.1.

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[»]
2GYAelectron microscopy15.003/53-121[»]
2GYCelectron microscopy15.003/53-121[»]
2XTGelectron microscopy7.80L1-121[»]
2XUXelectron microscopy7.60L1-121[»]
3J5Oelectron microscopy6.8061-121[»]
3J5Welectron microscopy7.60L2-121[»]
3J7Zelectron microscopy3.9061-121[»]
3SGFX-ray3.20J/K/L/M1-121[»]
3UOSX-ray3.70J/K/L/M1-121[»]
4KIXX-ray2.9061-121[»]
ProteinModelPortaliP0A7K2.
SMRiP0A7K2. Positions 3-121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL2363135.

PTM databases

PhosSiteiP0810430.

2D gel databases

SWISS-2DPAGEP0A7K2.

Proteomic databases

PaxDbiP0A7K2.
PRIDEiP0A7K2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76960; AAC76960; b3986.
BAE77334; BAE77334; BAE77334.
GeneIDi12930512.
948489.
KEGGiecj:Y75_p3211.
eco:b3986.
PATRICi32123493. VBIEscCol129921_4099.

Organism-specific databases

EchoBASEiEB0866.
EcoGeneiEG10873. rplL.

Phylogenomic databases

eggNOGiCOG0222.
HOGENOMiHOG000248813.
InParanoidiP0A7K2.
KOiK02935.
OMAiASMSVME.
OrthoDBiEOG6WMJ69.
PhylomeDBiP0A7K2.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7K2.
PROiP0A7K2.

Gene expression databases

GenevestigatoriP0A7K2.

Family and domain databases

Gene3Di3.30.1390.10. 1 hit.
HAMAPiMF_00368. Ribosomal_L7_L12.
InterProiIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PANTHERiPTHR11809. PTHR11809. 1 hit.
PfamiPF00542. Ribosomal_L12. 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...

Publicationsi

« Hide 'large scale' publications
  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. "Sequence determination in 3'-end proximalely labelled DNA."
    Gurevich A.I., Avakov A.E.
    Bioorg. Khim. 5:301-304(1979)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "The primary structure of an acidic protein from 50-S ribosomes of Escherichia coli which is involved in GTP hydrolysis dependent on elongation factors G and T."
    Terhorst C., Moeller W., Laursen R., Wittmann-Liebold B.
    Eur. J. Biochem. 34:138-152(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-121, METHYLATION AT LYS-82.
    Strain: MRE-600.
  7. "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 2-121.
    Strain: MRE-600.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  9. "Small genes/gene-products in Escherichia coli K-12."
    Wasinger V.C., Humphery-Smith I.
    FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Strain: K12.
  10. Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  11. "The nucleotide sequence at the proximal end of rpoB gene of Escherichia coli."
    Gurevich A.I., Avakov A.E., Kolosov M.N.
    Bioorg. Khim. 5:1735-1739(1979)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-121.
  12. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  13. "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.
  14. "Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation."
    Diaconu M., Kothe U., Schlunzen F., Fischer N., Harms J.M., Tonevitsky A.G., Stark H., Rodnina M.V., Wahl M.C.
    Cell 121:991-1004(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BINDING OF EF-TU AND EF-G, SUBUNIT, MUTAGENESIS OF LYS-66; VAL-67; ILE-70; LYS-71; ARG-74 AND LYS-85.
  15. "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.
  16. "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: FUNCTION IN IF-2 (INFB) AND EF-G (FUSA) ASSOCIATION WITH RIBOSOME.
    Strain: K12 / MG1655 / ATCC 47076.
  17. "Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A."
    Leijonmarck M., Liljas A.
    J. Mol. Biol. 195:555-580(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  18. "Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solution."
    Bocharov E.V., Gudkov A.T., Arseniev A.S.
    FEBS Lett. 379:291-294(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  19. "Conformational independence of N- and C-domains in ribosomal protein L7/L12 and in the complex with protein L10."
    Bocharov E.V., Gudkov A.T., Budovskaya E.V., Arseniev A.S.
    FEBS Lett. 423:347-350(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

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: January 7, 2015
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3

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 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.