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P0AG55

- RL6_ECOLI

UniProt

P0AG55 - RL6_ECOLI

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Protein
50S ribosomal protein L6
Gene
rplF, b3305, JW3267
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation
Gentamicin-resistant mutations in this protein affect translation fidelity.UniRule annotation

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. response to antibiotic Source: UniProtKB-KW
  2. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10869-MONOMER.
ECOL316407:JW3267-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L6
Gene namesi
Name:rplF
Ordered Locus Names:b3305, JW3267
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10869. rplF.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 17717650S ribosomal protein L6UniRule annotation
PRO_0000131048Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0AG55.
PRIDEiP0AG55.

Expressioni

Gene expression databases

GenevestigatoriP0AG55.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

BioGridi852115. 1 interaction.
DIPiDIP-35860N.
IntActiP0AG55. 83 interactions.
MINTiMINT-1244940.
STRINGi511145.b3305.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64
Beta strandi18 – 203
Beta strandi21 – 255
Beta strandi29 – 313
Beta strandi35 – 373
Beta strandi39 – 446
Beta strandi46 – 483
Beta strandi49 – 546
Beta strandi55 – 573
Turni59 – 624
Helixi63 – 8119
Beta strandi83 – 853
Beta strandi87 – 915
Beta strandi94 – 963
Beta strandi97 – 993
Beta strandi100 – 1034
Beta strandi105 – 1084
Beta strandi109 – 1113
Beta strandi113 – 1164
Beta strandi119 – 1246
Beta strandi126 – 1294
Beta strandi130 – 1367
Helixi138 – 15013
Turni156 – 1583
Beta strandi161 – 1666

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
3J5Lelectron microscopy6.60G2-177[»]
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[»]
4CSUelectron microscopy5.50G2-177[»]
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[»]
ProteinModelPortaliP0AG55.
SMRiP0AG55. Positions 2-177.

Miscellaneous databases

EvolutionaryTraceiP0AG55.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0097.
HOGENOMiHOG000039903.
KOiK02933.
OMAiSHPINYE.
OrthoDBiEOG67DPRD.
PhylomeDBiP0AG55.

Family and domain databases

Gene3Di3.90.930.12. 2 hits.
HAMAPiMF_01365_B. Ribosomal_L6_B.
InterProiIPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR019906. Ribosomal_L6_bac-type.
IPR002358. Ribosomal_L6_CS.
[Graphical view]
PANTHERiPTHR11655. PTHR11655. 1 hit.
PfamiPF00347. Ribosomal_L6. 2 hits.
[Graphical view]
PIRSFiPIRSF002162. Ribosomal_L6. 1 hit.
PRINTSiPR00059. RIBOSOMALL6.
SUPFAMiSSF56053. SSF56053. 2 hits.
TIGRFAMsiTIGR03654. L6_bact. 1 hit.
PROSITEiPS00525. RIBOSOMAL_L6_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AG55-1 [UniParc]FASTAAdd to Basket

« Hide

MSRVAKAPVV VPAGVDVKIN GQVITIKGKN GELTRTLNDA VEVKHADNTL    50
TFGPRDGYAD GWAQAGTARA LLNSMVIGVT EGFTKKLQLV GVGYRAAVKG 100
NVINLSLGFS HPVDHQLPAG ITAECPTQTE IVLKGADKQV IGQVAADLRA 150
YRRPEPYKGK GVRYADEVVR TKEAKKK 177
Length:177
Mass (Da):18,904
Last modified:January 23, 2007 - v2
Checksum:i946B64E9FA42FE61
GO

Mass spectrometryi

Molecular mass is 18772.7 Da from positions 2 - 177. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti152 – 17726RRPEP…EAKKK → AL in gentamicin resistant strain: GS50-15.
Add
BLAST
Natural varianti158 – 17720KGKGV…EAKKK → TL in gentamicin resistant strain: GS20-8.
Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821G → D in CAA25720. 1 Publication
Sequence conflicti88 – 881Q → E AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01563 Genomic DNA. Translation: CAA25720.1.
U18997 Genomic DNA. Translation: AAA58102.1.
U00096 Genomic DNA. Translation: AAC76330.1.
AP009048 Genomic DNA. Translation: BAE77986.1.
PIRiD65123. R5EC6.
RefSeqiNP_417764.1. NC_000913.3.
YP_492127.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76330; AAC76330; b3305.
BAE77986; BAE77986; BAE77986.
GeneIDi12934434.
947803.
KEGGiecj:Y75_p3871.
eco:b3305.
PATRICi32122042. VBIEscCol129921_3398.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X01563 Genomic DNA. Translation: CAA25720.1 .
U18997 Genomic DNA. Translation: AAA58102.1 .
U00096 Genomic DNA. Translation: AAC76330.1 .
AP009048 Genomic DNA. Translation: BAE77986.1 .
PIRi D65123. R5EC6.
RefSeqi NP_417764.1. NC_000913.3.
YP_492127.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EG0 electron microscopy 11.50 J 1-171 [» ]
1ML5 electron microscopy 14.00 h 2-177 [» ]
1P85 electron microscopy 12.30 E 2-177 [» ]
1P86 electron microscopy 11.50 E 2-177 [» ]
1VS6 X-ray 3.46 G 1-177 [» ]
1VS8 X-ray 3.46 G 1-177 [» ]
1VT2 X-ray 3.30 G 1-177 [» ]
2AW4 X-ray 3.46 G 2-177 [» ]
2AWB X-ray 3.46 G 2-177 [» ]
2GYA electron microscopy 15.00 E 6-172 [» ]
2GYC electron microscopy 15.00 E 6-172 [» ]
2I2T X-ray 3.22 G 2-177 [» ]
2I2V X-ray 3.22 G 2-177 [» ]
2J28 electron microscopy 8.00 G 2-177 [» ]
2QAM X-ray 3.21 G 2-177 [» ]
2QAO X-ray 3.21 G 2-177 [» ]
2QBA X-ray 3.54 G 2-177 [» ]
2QBC X-ray 3.54 G 2-177 [» ]
2QBE X-ray 3.30 G 2-177 [» ]
2QBG X-ray 3.30 G 2-177 [» ]
2QBI X-ray 4.00 G 2-177 [» ]
2QBK X-ray 4.00 G 2-177 [» ]
2QOV X-ray 3.93 G 2-177 [» ]
2QOX X-ray 3.93 G 2-177 [» ]
2QOZ X-ray 3.50 G 2-177 [» ]
2QP1 X-ray 3.50 G 2-177 [» ]
2RDO electron microscopy 9.10 G 2-177 [» ]
2VHM X-ray 3.74 G 2-177 [» ]
2VHN X-ray 3.74 G 2-177 [» ]
2WWQ electron microscopy 5.80 G 2-177 [» ]
2Z4L X-ray 4.45 G 2-177 [» ]
2Z4N X-ray 4.45 G 2-177 [» ]
3BBX electron microscopy 10.00 G 2-177 [» ]
3E1B electron microscopy - 3 1-177 [» ]
3E1D electron microscopy - 3 1-177 [» ]
3FIK electron microscopy 6.70 G 2-177 [» ]
3I1N X-ray 3.19 G 1-177 [» ]
3I1P X-ray 3.19 G 1-177 [» ]
3I1R X-ray 3.81 G 1-177 [» ]
3I1T X-ray 3.81 G 1-177 [» ]
3I20 X-ray 3.71 G 1-177 [» ]
3I22 X-ray 3.71 G 1-177 [» ]
3IZT electron microscopy - H 1-177 [» ]
3IZU electron microscopy - H 1-177 [» ]
3J01 electron microscopy - G 2-177 [» ]
3J0T electron microscopy 12.10 H 2-177 [» ]
3J0W electron microscopy 14.70 H 2-177 [» ]
3J0Y electron microscopy 13.50 H 2-177 [» ]
3J11 electron microscopy 13.10 H 2-177 [» ]
3J12 electron microscopy 11.50 H 2-177 [» ]
3J14 electron microscopy 11.50 H 2-177 [» ]
3J19 electron microscopy 8.30 G 2-177 [» ]
3J37 electron microscopy 9.80 H 2-177 [» ]
3J4X electron microscopy 12.00 G 1-177 [» ]
3J50 electron microscopy 20.00 G 1-177 [» ]
3J51 electron microscopy 17.00 G 1-177 [» ]
3J52 electron microscopy 12.00 G 1-177 [» ]
3J54 electron microscopy 13.00 G 1-177 [» ]
3J56 electron microscopy 15.00 G 1-177 [» ]
3J58 electron microscopy 17.00 G 1-177 [» ]
3J5A electron microscopy 12.00 G 1-177 [» ]
3J5C electron microscopy 17.00 G 1-177 [» ]
3J5E electron microscopy 17.00 G 1-177 [» ]
3J5G electron microscopy 20.00 G 1-177 [» ]
3J5I electron microscopy 15.00 G 1-177 [» ]
3J5K electron microscopy 9.00 G 1-177 [» ]
3J5L electron microscopy 6.60 G 2-177 [» ]
3J5O electron microscopy 6.80 G 1-177 [» ]
3J5U electron microscopy 7.60 H 2-177 [» ]
3J5W electron microscopy 7.60 H 2-177 [» ]
3KCR electron microscopy - G 1-177 [» ]
3OAS X-ray 3.25 G 2-177 [» ]
3OAT X-ray 3.25 G 2-177 [» ]
3OFC X-ray 3.19 G 2-177 [» ]
3OFD X-ray 3.19 G 2-177 [» ]
3OFQ X-ray 3.10 G 2-177 [» ]
3OFR X-ray 3.10 G 2-177 [» ]
3OFZ X-ray 3.29 G 2-177 [» ]
3OG0 X-ray 3.29 G 2-177 [» ]
3ORB X-ray 3.30 G 1-177 [» ]
3R8S X-ray 3.00 G 2-177 [» ]
3R8T X-ray 3.00 G 2-177 [» ]
3SGF X-ray 3.20 G 1-177 [» ]
3UOS X-ray 3.70 G 1-177 [» ]
487D electron microscopy 7.50 J 31-165 [» ]
4CSU electron microscopy 5.50 G 2-177 [» ]
4GAR X-ray 3.30 G 1-177 [» ]
4GAU X-ray 3.30 G 1-177 [» ]
4KIX X-ray 2.90 G 1-177 [» ]
4KIZ X-ray 2.90 G 1-177 [» ]
4KJ1 X-ray 2.90 G 1-177 [» ]
4KJ3 X-ray 2.90 G 1-177 [» ]
4KJ5 X-ray 2.90 G 1-177 [» ]
4KJ7 X-ray 2.90 G 1-177 [» ]
4KJ9 X-ray 2.90 G 1-177 [» ]
4KJB X-ray 2.90 G 1-177 [» ]
ProteinModelPortali P0AG55.
SMRi P0AG55. Positions 2-177.
ModBasei Search...

Protein-protein interaction databases

BioGridi 852115. 1 interaction.
DIPi DIP-35860N.
IntActi P0AG55. 83 interactions.
MINTi MINT-1244940.
STRINGi 511145.b3305.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0AG55.
PRIDEi P0AG55.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76330 ; AAC76330 ; b3305 .
BAE77986 ; BAE77986 ; BAE77986 .
GeneIDi 12934434.
947803.
KEGGi ecj:Y75_p3871.
eco:b3305.
PATRICi 32122042. VBIEscCol129921_3398.

Organism-specific databases

EchoBASEi EB0862.
EcoGenei EG10869. rplF.

Phylogenomic databases

eggNOGi COG0097.
HOGENOMi HOG000039903.
KOi K02933.
OMAi SHPINYE.
OrthoDBi EOG67DPRD.
PhylomeDBi P0AG55.

Enzyme and pathway databases

BioCyci EcoCyc:EG10869-MONOMER.
ECOL316407:JW3267-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AG55.
PROi P0AG55.

Gene expression databases

Genevestigatori P0AG55.

Family and domain databases

Gene3Di 3.90.930.12. 2 hits.
HAMAPi MF_01365_B. Ribosomal_L6_B.
InterProi IPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR019906. Ribosomal_L6_bac-type.
IPR002358. Ribosomal_L6_CS.
[Graphical view ]
PANTHERi PTHR11655. PTHR11655. 1 hit.
Pfami PF00347. Ribosomal_L6. 2 hits.
[Graphical view ]
PIRSFi PIRSF002162. Ribosomal_L6. 1 hit.
PRINTSi PR00059. RIBOSOMALL6.
SUPFAMi SSF56053. SSF56053. 2 hits.
TIGRFAMsi TIGR03654. L6_bact. 1 hit.
PROSITEi PS00525. RIBOSOMAL_L6_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL6_ECOLI
AccessioniPrimary (citable) accession number: P0AG55
Secondary accession number(s): P02390, Q2M6X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 90 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

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