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P0A7J7 (RL11_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L11
Gene names
Name:rplK
Synonyms:relC
Ordered Locus Names:b3983, JW3946
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. HAMAP-Rule MF_00736

Subunit structure

Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which 2 L12 dimers bind in a sequential fashion forming a pentameric L10(L12)2(L12)2 complex.

Sequence similarities

Belongs to the ribosomal protein L11P family.

Mass spectrometry

Molecular mass is 14870.2 Da from positions 2 - 142. Determined by MALDI. Ref.9

Binary interactions

With

Entry

#Exp.

IntAct

Notes

prmAP0A8T13EBI-547288,EBI-556300

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 14214150S ribosomal protein L11 HAMAP-Rule MF_00736
PRO_0000104283

Amino acid modifications

Modified residue21N,N,N-trimethylalanine HAMAP-Rule MF_00736
Modified residue41N6,N6,N6-trimethyllysine HAMAP-Rule MF_00736
Modified residue401N6,N6,N6-trimethyllysine HAMAP-Rule MF_00736
Modified residue721N6-succinyllysine Ref.11
Modified residue811N6-succinyllysine Ref.11

Secondary structure

......................................... 142
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7J7 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C49226BB2462BE0F

FASTA14214,875
        10         20         30         40         50         60 
MAKKVQAYVK LQVAAGMANP SPPVGPALGQ QGVNIMEFCK AFNAKTDSIE KGLPIPVVIT 

        70         80         90        100        110        120 
VYADRSFTFV TKTPPAAVLL KKAAGIKSGS GKPNKDKVGK ISRAQLQEIA QTKAADMTGA 

       130        140 
DIEAMTRSIE GTARSMGLVV ED 

« 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]"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.
[3]"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.
[4]"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.
[5]"Purification and primary structure determination of the N-terminal blocked protein, L11, from Escherichia coli ribosomes."
Dognin M.J., Wittmann-Liebold B.
Eur. J. Biochem. 112:131-151(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-142.
Strain: K12.
[6]"Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon."
Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P.
J. Bacteriol. 172:1621-1627(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
[7]"Structural properties of ribosomal protein L11 from Escherichia coli."
Choli T.
Biochem. Int. 19:1323-1338(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURAL STUDIES.
[8]"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.
[9]"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.
[10]"The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 A resolution."
Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J., Goerlach M., van Heel M., Brimacombe R.
J. Mol. Biol. 298:35-59(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[11]"Identification of lysine succinylation as a new post-translational modification."
Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION AT LYS-72 AND LYS-81.
Strain: K12.
[12]"Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
Strain: MRE-600.
[13]"Structures of the bacterial ribosome at 3.5 A resolution."
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.
Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00339 Genomic DNA. Translation: CAA23621.1. Sequence problems.
M30610 Genomic DNA. Translation: AAA24623.1.
U00006 Genomic DNA. Translation: AAC43081.1.
U00096 Genomic DNA. Translation: AAC76957.1.
AP009048 Genomic DNA. Translation: BAE77337.1.
PIRR5EC11. S12572.
RefSeqNP_418410.1. NC_000913.3.
YP_491478.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50K1-140[»]
1MJ1electron microscopy13.00L1-141[»]
1ML5electron microscopy14.00l1-141[»]
1P85electron microscopy12.30G2-142[»]
1P86electron microscopy11.50G2-142[»]
1VS6X-ray3.46I1-142[»]
1VS8X-ray3.46I1-142[»]
1VT2X-ray3.30I1-142[»]
2AW4X-ray3.46I2-142[»]
2AWBX-ray3.46I2-142[»]
2GYAelectron microscopy15.00G3-141[»]
2GYCelectron microscopy15.00G3-141[»]
2I2TX-ray3.22I2-142[»]
2I2VX-ray3.22I2-142[»]
2J28electron microscopy8.00I2-142[»]
2QAMX-ray3.21I2-142[»]
2QAOX-ray3.21I2-142[»]
2QBAX-ray3.54I2-142[»]
2QBCX-ray3.54I2-142[»]
2QBEX-ray3.30I2-142[»]
2QBGX-ray3.30I2-142[»]
2QBIX-ray4.00I2-142[»]
2QBKX-ray4.00I2-142[»]
2QOVX-ray3.93I2-142[»]
2QOXX-ray3.93I2-142[»]
2QOZX-ray3.50I2-142[»]
2QP1X-ray3.50I2-142[»]
2RDOelectron microscopy9.10I2-142[»]
2VHMX-ray3.74I2-142[»]
2VHNX-ray3.74I2-142[»]
2WWQelectron microscopy5.80I2-142[»]
2Z4LX-ray4.45I2-142[»]
2Z4NX-ray4.45I2-142[»]
3DEGelectron microscopy-H2-142[»]
3DF2X-ray3.50I2-141[»]
3DF4X-ray3.50I2-141[»]
3E1Belectron microscopy-51-142[»]
3E1Delectron microscopy-51-142[»]
3EP2electron microscopy-I2-142[»]
3EQ3electron microscopy-I2-142[»]
3EQ4electron microscopy-I2-142[»]
3FIKelectron microscopy6.70I2-142[»]
3I1NX-ray3.19I1-142[»]
3I1PX-ray3.19I1-142[»]
3I1RX-ray3.81I1-142[»]
3I1TX-ray3.81I1-142[»]
3I20X-ray3.71I1-142[»]
3I22X-ray3.71I1-142[»]
3IZTelectron microscopy-J1-142[»]
3IZUelectron microscopy-J1-142[»]
3J01electron microscopy-I2-142[»]
3J0Delectron microscopy11.10G2-142[»]
3J0Telectron microscopy12.10K2-142[»]
3J0Welectron microscopy14.70K2-142[»]
3J0Yelectron microscopy13.50K2-142[»]
3J11electron microscopy13.10K2-142[»]
3J12electron microscopy11.50K2-142[»]
3J14electron microscopy11.50K2-142[»]
3J19electron microscopy8.30I2-142[»]
3J37electron microscopy9.80K2-142[»]
3J4Xelectron microscopy12.00I1-142[»]
3J50electron microscopy20.00I1-142[»]
3J51electron microscopy17.00I1-142[»]
3J52electron microscopy12.00I1-142[»]
3J54electron microscopy13.00I1-142[»]
3J56electron microscopy15.00I1-142[»]
3J58electron microscopy17.00I1-142[»]
3J5Aelectron microscopy12.00I1-142[»]
3J5Celectron microscopy17.00I1-142[»]
3J5Eelectron microscopy17.00I1-142[»]
3J5Gelectron microscopy20.00I1-142[»]
3J5Ielectron microscopy15.00I1-142[»]
3J5Kelectron microscopy9.00I1-142[»]
3J5Lelectron microscopy6.60I2-142[»]
3J5Oelectron microscopy6.80I1-142[»]
3J5Uelectron microscopy7.60K2-142[»]
3J5Welectron microscopy7.60K2-142[»]
3KCRelectron microscopy-I1-142[»]
3OASX-ray3.25I2-142[»]
3OATX-ray3.25I2-142[»]
3OFCX-ray3.19I2-142[»]
3OFDX-ray3.19I2-142[»]
3OFQX-ray3.10I2-142[»]
3OFRX-ray3.10I2-142[»]
3OFZX-ray3.29I2-142[»]
3OG0X-ray3.29I2-142[»]
3ORBX-ray3.30I1-142[»]
3R8SX-ray3.00I2-142[»]
3R8TX-ray3.00I2-142[»]
3SGFX-ray3.20I1-142[»]
3UOSX-ray3.70I1-142[»]
487Delectron microscopy7.50L10-86[»]
4GARX-ray3.30I1-142[»]
4GAUX-ray3.30I1-142[»]
4KIXX-ray2.90I1-142[»]
4KIZX-ray2.90I1-142[»]
4KJ1X-ray2.90I1-142[»]
4KJ3X-ray2.90I1-142[»]
4KJ5X-ray2.90I1-142[»]
4KJ7X-ray2.90I1-142[»]
4KJ9X-ray2.90I1-142[»]
4KJBX-ray2.90I1-142[»]
ProteinModelPortalP0A7J7.
SMRP0A7J7. Positions 3-141.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852778. 1 interaction.
DIPDIP-35882N.
IntActP0A7J7. 46 interactions.
MINTMINT-1232893.
STRING511145.b3983.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7J7.
PRIDEP0A7J7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76957; AAC76957; b3983.
BAE77337; BAE77337; BAE77337.
GeneID12930523.
948484.
KEGGecj:Y75_p3214.
eco:b3983.
PATRIC32123487. VBIEscCol129921_4096.

Organism-specific databases

EchoBASEEB0865.
EcoGeneEG10872. rplK.

Phylogenomic databases

eggNOGCOG0080.
HOGENOMHOG000082123.
KOK02867.
OMAIEAYIKL.
OrthoDBEOG69PQ9D.
PhylomeDBP0A7J7.

Enzyme and pathway databases

BioCycEcoCyc:EG10872-MONOMER.
ECOL316407:JW3946-MONOMER.

Gene expression databases

GenevestigatorP0A7J7.

Family and domain databases

Gene3D1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.
HAMAPMF_00736. Ribosomal_L11.
InterProIPR000911. Ribosomal_L11/L12.
IPR006519. Ribosomal_L11_bac-typ.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view]
PANTHERPTHR11661. PTHR11661. 1 hit.
PfamPF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view]
SMARTSM00649. RL11. 1 hit.
[Graphical view]
SUPFAMSSF46906. SSF46906. 1 hit.
SSF54747. SSF54747. 1 hit.
TIGRFAMsTIGR01632. L11_bact. 1 hit.
PROSITEPS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7J7.
PROP0A7J7.

Entry information

Entry nameRL11_ECOLI
AccessionPrimary (citable) accession number: P0A7J7
Secondary accession number(s): P02409, P76778, Q2M8R9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 97 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