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P0A7K2

- RL7_ECOLI

UniProt

P0A7K2 - RL7_ECOLI

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Protein
50S ribosomal protein L7/L12
Gene
rplL, b3986, JW3949
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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/L12
Alternative name(s):
L8
Gene namesi
Name:rplL
Ordered Locus Names:b3986, JW3949
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10873. rplL.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: EcoCyc
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/L12UniRule annotation
PRO_0000157528Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine; in L7UniRule annotation
Modified residuei82 – 821N6-methyllysine; partialUniRule annotation

Post-translational modificationi

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

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

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73
Beta strandi9 – 135
Helixi17 – 204
Beta strandi23 – 253
Helixi26 – 294
Helixi33 – 5018
Beta strandi55 – 617
Helixi63 – 653
Helixi66 – 7712
Helixi81 – 899
Beta strandi92 – 998
Helixi101 – 11414
Beta strandi117 – 1215

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
3SGFX-ray3.20J/K/L/M1-121[»]
3UOSX-ray3.70J/K/L/M1-121[»]
4KIXX-ray2.9061-121[»]
ProteinModelPortaliP0A7K2.
SMRiP0A7K2. Positions 3-121.

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 hydrolysisUniRule annotation
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0222.
HOGENOMiHOG000248813.
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

MSITKDQIIE AVAAMSVMDV VELISAMEEK FGVSAAAAVA VAAGPVEAAE    50
EKTEFDVILK AAGANKVAVI KAVRGATGLG LKEAKDLVES APAALKEGVS 100
KDDAEALKKA LEEAGAEVEV K 121
Length:121
Mass (Da):12,295
Last modified:January 23, 2007 - v2
Checksum:i08B051A0CDAA527E
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61D → F AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
YP_491475.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
2GYA electron microscopy 15.00 3/5 3-121 [» ]
2GYC electron microscopy 15.00 3/5 3-121 [» ]
2XTG electron microscopy 7.80 L 1-121 [» ]
2XUX electron microscopy 7.60 L 1-121 [» ]
3J5O electron microscopy 6.80 6 1-121 [» ]
3J5W electron microscopy 7.60 L 2-121 [» ]
3SGF X-ray 3.20 J/K/L/M 1-121 [» ]
3UOS X-ray 3.70 J/K/L/M 1-121 [» ]
4KIX X-ray 2.90 6 1-121 [» ]
ProteinModelPortali P0A7K2.
SMRi P0A7K2. Positions 3-121.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852783. 1 interaction.
DIPi DIP-36009N.
IntActi P0A7K2. 127 interactions.
MINTi MINT-1277405.
STRINGi 511145.b3986.

Chemistry

ChEMBLi CHEMBL2363135.

PTM databases

PhosSitei P0810430.

2D gel databases

SWISS-2DPAGE P0A7K2.

Proteomic databases

PaxDbi P0A7K2.
PRIDEi P0A7K2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76960 ; AAC76960 ; b3986 .
BAE77334 ; BAE77334 ; BAE77334 .
GeneIDi 12930512.
948489.
KEGGi ecj:Y75_p3211.
eco:b3986.
PATRICi 32123493. VBIEscCol129921_4099.

Organism-specific databases

EchoBASEi EB0866.
EcoGenei EG10873. rplL.

Phylogenomic databases

eggNOGi COG0222.
HOGENOMi HOG000248813.
KOi K02935.
OMAi ASMSVME.
OrthoDBi EOG6WMJ69.
PhylomeDBi P0A7K2.

Enzyme and pathway databases

BioCyci EcoCyc:EG10873-MONOMER.
ECOL316407:JW3949-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7K2.
PROi P0A7K2.

Gene expression databases

Genevestigatori P0A7K2.

Family and domain databases

Gene3Di 3.30.1390.10. 1 hit.
HAMAPi MF_00368. Ribosomal_L7_L12.
InterProi IPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view ]
PANTHERi PTHR11809. PTHR11809. 1 hit.
Pfami PF00542. Ribosomal_L12. 1 hit.
[Graphical view ]
ProDomi PD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.
TIGRFAMsi TIGR00855. L12. 1 hit.
ProtoNeti Search...

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.
    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.

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: July 9, 2014
This is version 95 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