Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0AG55 (RL6_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. 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 L6
Gene names
Name:rplF
Ordered Locus Names:b3305, JW3267
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. HAMAP-Rule MF_01365

Gentamicin-resistant mutations in this protein affect translation fidelity. HAMAP-Rule MF_01365

Subunit structure

Part of the 50S ribosomal subunit.

Sequence similarities

Belongs to the ribosomal protein L6P family.

Mass spectrometry

Molecular mass is 18772.7 Da from positions 2 - 177. Determined by MALDI. Ref.10

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.5
Chain2 – 17717650S ribosomal protein L6 HAMAP-Rule MF_01365
PRO_0000131048

Amino acid modifications

Modified residue441N6-acetyllysine Ref.11

Natural variations

Natural variant152 – 17726RRPEP…EAKKK → AL in gentamicin resistant strain: GS50-15.
Natural variant158 – 17720KGKGV…EAKKK → TL in gentamicin resistant strain: GS20-8.

Experimental info

Sequence conflict821G → D in CAA25720. Ref.2
Sequence conflict881Q → E AA sequence Ref.1

Secondary structure

........................................... 177
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AG55 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 946B64E9FA42FE61

FASTA17718,904
        10         20         30         40         50         60 
MSRVAKAPVV VPAGVDVKIN GQVITIKGKN GELTRTLNDA VEVKHADNTL TFGPRDGYAD 

        70         80         90        100        110        120 
GWAQAGTARA LLNSMVIGVT EGFTKKLQLV GVGYRAAVKG NVINLSLGFS HPVDHQLPAG 

       130        140        150        160        170 
ITAECPTQTE IVLKGADKQV IGQVAADLRA YRRPEPYKGK GVRYADEVVR TKEAKKK 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of protein L6 from the aminoacyl-tRNA binding site of the Escherichia coli ribosome."
Chen R., Arfsten U., Chen-Schmeisser U.
Hoppe-Seyler's Z. Physiol. Chem. 358:531-535(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-177.
Strain: K.
[2]"The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[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]"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.
[6]"Alteration of ribosomal protein L6 in gentamicin-resistant strains of Escherichia coli. Effects on fidelity of protein synthesis."
Kuehberger R., Piepersberg W., Petzet A., Buckel P., Boeck A.
Biochemistry 18:187-193(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOLATION, CHARACTERIZATION OF VARIANTS GENTAMICIN-RESISTANT GE20-8; GS20-10 AND GS50-15.
Strain: K12 / A19.
[7]"The use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29."
Wower I., Wower J., Meinke M., Brimacombe R.
Nucleic Acids Res. 9:4285-4302(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO 23S RRNA.
Strain: MRE-600.
[8]"Ribosomal proteins S5 and L6: high-resolution crystal structures and roles in protein synthesis and antibiotic resistance."
Davies C., Bussiere D.E., Golden B.L., Porter S.J., Ramakrishnan V., White S.W.
J. Mol. Biol. 279:873-888(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF VARIANTS GENTAMICIN-RESISTANT.
[9]"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.
[10]"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.
[11]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[12]"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.
[13]"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.
[14]"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
X01563 Genomic DNA. Translation: CAA25720.1.
U18997 Genomic DNA. Translation: AAA58102.1.
U00096 Genomic DNA. Translation: AAC76330.1.
AP009048 Genomic DNA. Translation: BAE77986.1.
PIRR5EC6. D65123.
RefSeqNP_417764.1. NC_000913.3.
YP_492127.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50J1-171[»]
1ML5electron microscopy14.00h2-177[»]
1P85electron microscopy12.30E2-177[»]
1P86electron microscopy11.50E2-177[»]
1VS6X-ray3.46G1-177[»]
1VS8X-ray3.46G1-177[»]
1VT2X-ray3.30G1-177[»]
2AW4X-ray3.46G2-177[»]
2AWBX-ray3.46G2-177[»]
2GYAelectron microscopy15.00E6-172[»]
2GYCelectron microscopy15.00E6-172[»]
2I2TX-ray3.22G2-177[»]
2I2VX-ray3.22G2-177[»]
2J28electron microscopy8.00G2-177[»]
2QAMX-ray3.21G2-177[»]
2QAOX-ray3.21G2-177[»]
2QBAX-ray3.54G2-177[»]
2QBCX-ray3.54G2-177[»]
2QBEX-ray3.30G2-177[»]
2QBGX-ray3.30G2-177[»]
2QBIX-ray4.00G2-177[»]
2QBKX-ray4.00G2-177[»]
2QOVX-ray3.93G2-177[»]
2QOXX-ray3.93G2-177[»]
2QOZX-ray3.50G2-177[»]
2QP1X-ray3.50G2-177[»]
2RDOelectron microscopy9.10G2-177[»]
2VHMX-ray3.74G2-177[»]
2VHNX-ray3.74G2-177[»]
2WWQelectron microscopy5.80G2-177[»]
2Z4LX-ray4.45G2-177[»]
2Z4NX-ray4.45G2-177[»]
3BBXelectron microscopy10.00G2-177[»]
3E1Belectron microscopy-31-177[»]
3E1Delectron microscopy-31-177[»]
3FIKelectron microscopy6.70G2-177[»]
3I1NX-ray3.19G1-177[»]
3I1PX-ray3.19G1-177[»]
3I1RX-ray3.81G1-177[»]
3I1TX-ray3.81G1-177[»]
3I20X-ray3.71G1-177[»]
3I22X-ray3.71G1-177[»]
3IZTelectron microscopy-H1-177[»]
3IZUelectron microscopy-H1-177[»]
3J01electron microscopy-G2-177[»]
3J0Telectron microscopy12.10H2-177[»]
3J0Welectron microscopy14.70H2-177[»]
3J0Yelectron microscopy13.50H2-177[»]
3J11electron microscopy13.10H2-177[»]
3J12electron microscopy11.50H2-177[»]
3J14electron microscopy11.50H2-177[»]
3J19electron microscopy8.30G2-177[»]
3J37electron microscopy9.80H2-177[»]
3J4Xelectron microscopy12.00G1-177[»]
3J50electron microscopy20.00G1-177[»]
3J51electron microscopy17.00G1-177[»]
3J52electron microscopy12.00G1-177[»]
3J54electron microscopy13.00G1-177[»]
3J56electron microscopy15.00G1-177[»]
3J58electron microscopy17.00G1-177[»]
3J5Aelectron microscopy12.00G1-177[»]
3J5Celectron microscopy17.00G1-177[»]
3J5Eelectron microscopy17.00G1-177[»]
3J5Gelectron microscopy20.00G1-177[»]
3J5Ielectron microscopy15.00G1-177[»]
3J5Kelectron microscopy9.00G1-177[»]
3J5Oelectron microscopy6.80G1-177[»]
3J5Uelectron microscopy7.60H2-177[»]
3J5Welectron microscopy7.60H2-177[»]
3KCRelectron microscopy-G1-177[»]
3OASX-ray3.25G2-177[»]
3OATX-ray3.25G2-177[»]
3OFCX-ray3.19G2-177[»]
3OFDX-ray3.19G2-177[»]
3OFQX-ray3.10G2-177[»]
3OFRX-ray3.10G2-177[»]
3OFZX-ray3.29G2-177[»]
3OG0X-ray3.29G2-177[»]
3ORBX-ray3.30G1-177[»]
3R8SX-ray3.00G2-177[»]
3R8TX-ray3.00G2-177[»]
3SGFX-ray3.20G1-177[»]
3UOSX-ray3.70G1-177[»]
487Delectron microscopy7.50J31-165[»]
4GARX-ray3.30G1-177[»]
4GAUX-ray3.30G1-177[»]
4KIXX-ray2.90G1-177[»]
4KIZX-ray2.90G1-177[»]
4KJ1X-ray2.90G1-177[»]
4KJ3X-ray2.90G1-177[»]
4KJ5X-ray2.90G1-177[»]
4KJ7X-ray2.90G1-177[»]
4KJ9X-ray2.90G1-177[»]
4KJBX-ray2.90G1-177[»]
ProteinModelPortalP0AG55.
SMRP0AG55. Positions 2-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852115. 1 interaction.
DIPDIP-35860N.
IntActP0AG55. 83 interactions.
MINTMINT-1244940.
STRING511145.b3305.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0AG55.
PRIDEP0AG55.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76330; AAC76330; b3305.
BAE77986; BAE77986; BAE77986.
GeneID12934434.
947803.
KEGGecj:Y75_p3871.
eco:b3305.
PATRIC32122042. VBIEscCol129921_3398.

Organism-specific databases

EchoBASEEB0862.
EcoGeneEG10869. rplF.

Phylogenomic databases

eggNOGCOG0097.
HOGENOMHOG000039903.
KOK02933.
OMAMPAGITV.
OrthoDBEOG67DPRD.
PhylomeDBP0AG55.
ProtClustDBPRK05498.

Enzyme and pathway databases

BioCycEcoCyc:EG10869-MONOMER.
ECOL316407:JW3267-MONOMER.

Gene expression databases

GenevestigatorP0AG55.

Family and domain databases

Gene3D3.90.930.12. 2 hits.
HAMAPMF_01365_B. Ribosomal_L6_B.
InterProIPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR019906. Ribosomal_L6_bac-type.
IPR002358. Ribosomal_L6_CS.
[Graphical view]
PANTHERPTHR11655. PTHR11655. 1 hit.
PTHR11655:SF6. PTHR11655:SF6. 1 hit.
PfamPF00347. Ribosomal_L6. 2 hits.
[Graphical view]
PIRSFPIRSF002162. Ribosomal_L6. 1 hit.
PRINTSPR00059. RIBOSOMALL6.
SUPFAMSSF56053. SSF56053. 2 hits.
TIGRFAMsTIGR03654. L6_bact. 1 hit.
PROSITEPS00525. RIBOSOMAL_L6_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AG55.
PROP0AG55.

Entry information

Entry nameRL6_ECOLI
AccessionPrimary (citable) accession number: P0AG55
Secondary accession number(s): P02390, Q2M6X0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 87 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