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P0A7K2 (RL7_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L7/L12
Alternative name(s):
L8
Gene names
Name:rplL
Ordered Locus Names:b3986, JW3949
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length121 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.14 Ref.16

Subunit structure

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. Ref.14 Ref.15

Post-translational modification

Acetylation of Ser-2 converts L12 to L7. HAMAP-Rule MF_00368

Lys-82 was found to be 50% monomethylated. HAMAP-Rule MF_00368

Sequence similarities

Belongs to the ribosomal protein L7/L12P family.

Mass spectrometry

Molecular mass is 12206.7 Da from positions 2 - 121. Determined by MALDI. Non-methylated. Ref.13

Molecular mass is 66643±13 Da from positions 2 - 121. Determined by ESI. Isolated L10(L12)4. Ref.15

Molecular mass is 12223±1 Da from positions 2 - 121. Determined by ESI. L7, acetylated Ser-2. Ref.15

Molecular mass is 12164±1 Da from positions 2 - 121. Determined by ESI. L12, unacetylated. Ref.15

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Chain2 – 12112050S ribosomal protein L7/L12 HAMAP-Rule MF_00368
PRO_0000157528

Regions

Region54 – 12168Required for recruitment of EF-Tu and EF-G, and for EF-Tu and EF-G-promoted GTP hydrolysis HAMAP-Rule MF_00368

Amino acid modifications

Modified residue21N-acetylserine; in L7 HAMAP-Rule MF_00368
Modified residue821N6-methyllysine; partial HAMAP-Rule MF_00368

Experimental info

Mutagenesis661K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. Ref.14
Mutagenesis671V → D: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. Ref.14
Mutagenesis701I → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. Ref.14
Mutagenesis711K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. Ref.14
Mutagenesis741R → M: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. Ref.14
Mutagenesis851K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. Ref.14
Sequence conflict61D → F AA sequence Ref.9

Secondary structure

........................ 121
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7K2 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 08B051A0CDAA527E

FASTA12112,295
        10         20         30         40         50         60 
MSITKDQIIE AVAAMSVMDV VELISAMEEK FGVSAAAAVA VAAGPVEAAE EKTEFDVILK 

        70         80         90        100        110        120 
AAGANKVAVI KAVRGATGLG LKEAKDLVES APAALKEGVS KDDAEALKKA LEEAGAEVEV 


K 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Protein identification with N and C-terminal sequence tags in proteome projects."
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRR5EC7. S12575.
RefSeqNP_418413.1. NC_000913.3.
YP_491475.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CTFX-ray1.70A48-121[»]
1RQSNMR-A48-120[»]
1RQTNMR-A/B2-37[»]
1RQUNMR-A/B2-120[»]
1RQVNMR-A/B2-120[»]
2BCWelectron microscopy11.20B54-120[»]
2GYAelectron microscopy15.003/53-120[»]
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[»]
ProteinModelPortalP0A7K2.
SMRP0A7K2. Positions 3-121.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852783. 1 interaction.
DIPDIP-36009N.
IntActP0A7K2. 127 interactions.
MINTMINT-1277405.
STRING511145.b3986.

Chemistry

ChEMBLCHEMBL2363135.

PTM databases

PhosSiteP0810430.

2D gel databases

SWISS-2DPAGEP0A7K2.

Proteomic databases

PaxDbP0A7K2.
PRIDEP0A7K2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76960; AAC76960; b3986.
BAE77334; BAE77334; BAE77334.
GeneID12930512.
948489.
KEGGecj:Y75_p3211.
eco:b3986.
PATRIC32123493. VBIEscCol129921_4099.

Organism-specific databases

EchoBASEEB0866.
EcoGeneEG10873. rplL.

Phylogenomic databases

eggNOGCOG0222.
HOGENOMHOG000248813.
KOK02935.
OMALDSMSVM.
OrthoDBEOG6WMJ69.
PhylomeDBP0A7K2.
ProtClustDBPRK00157.

Enzyme and pathway databases

BioCycEcoCyc:EG10873-MONOMER.
ECOL316407:JW3949-MONOMER.

Gene expression databases

GenevestigatorP0A7K2.

Family and domain databases

Gene3D3.30.1390.10. 1 hit.
HAMAPMF_00368. Ribosomal_L7_L12.
InterProIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PANTHERPTHR11809. PTHR11809. 1 hit.
PfamPF00542. Ribosomal_L12. 1 hit.
[Graphical view]
ProDomPD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.
TIGRFAMsTIGR00855. L12. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A7K2.
PROP0A7K2.

Entry information

Entry nameRL7_ECOLI
AccessionPrimary (citable) accession number: P0A7K2
Secondary accession number(s): P02392, Q2M8S2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene