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P60723

- RL4_ECOLI

UniProt

P60723 - RL4_ECOLI

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Protein
50S ribosomal protein L4
Gene
rplD, eryA, b3319, JW3281
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.1 Publication
Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).1 Publication
Forms part of the polypeptide exit tunnel.1 Publication
Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.1 Publication

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro
  3. translation repressor activity Source: EcoliWiki
Complete GO annotation...

GO - Biological processi

  1. DNA-templated transcription, termination Source: UniProtKB-KW
  2. negative regulation of translation Source: GOC
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. response to antibiotic Source: UniProtKB-KW
  5. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance, Transcription, Transcription regulation, Transcription termination, Translation regulation

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10867-MONOMER.
ECOL316407:JW3281-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L4
Gene namesi
Name:rplD
Synonyms:eryA
Ordered Locus Names:b3319, JW3281
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10867. rplD.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 8849Missing: Regulates the S10 operon normally. Assembles into ribosomes in vivo.
Add
BLAST
Mutagenesisi67 – 10337Missing: Regulates the S10 operon normally. Does not assemble into ribosomes in vivo.
Add
BLAST
Mutagenesisi93 – 1019Missing: Regulates the S10 operon normally. Not stably associated with the ribosome in vivo.
Mutagenesisi131 – 1311T → I: Does not regulate the S10 operon; assembles into ribosomes in vivo.
Mutagenesisi134 – 1341L → P: Does not regulate the S10 operon in vivo.
Mutagenesisi160 – 1601A → V: Does not regulate the S10 operon; assembles into ribosomes in vivo.
Mutagenesisi167 – 1671V → D: Does not regulate the S10 operon in vivo.
Mutagenesisi171 – 20131DATGI…EEMLA → RRSK: Loss of S10 operon regulation. Assembles into ribosomes in vivo.
Add
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20120150S ribosomal protein L4UniRule annotation
PRO_0000129215Add
BLAST

Proteomic databases

PaxDbiP60723.
PRIDEiP60723.

Expressioni

Gene expression databases

GenevestigatoriP60723.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.1 Publication

Protein-protein interaction databases

DIPiDIP-35791N.
IntActiP60723. 214 interactions.
MINTiMINT-1219709.
STRINGi511145.b3319.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83
Helixi16 – 194
Beta strandi22 – 243
Helixi25 – 3612
Turni37 – 393
Turni49 – 513
Beta strandi52 – 543
Beta strandi62 – 676
Beta strandi78 – 814
Beta strandi83 – 853
Helixi98 – 11215
Turni113 – 1164
Beta strandi118 – 1203
Beta strandi121 – 1233
Beta strandi127 – 1293
Helixi131 – 14111
Beta strandi144 – 1463
Beta strandi149 – 1524
Helixi155 – 1595
Beta strandi160 – 1634
Beta strandi165 – 1673
Helixi172 – 1743
Helixi177 – 1826
Beta strandi183 – 1864
Helixi190 – 19910

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30C1-201[»]
1P86electron microscopy11.50C1-201[»]
1VS6X-ray3.46E1-201[»]
1VS8X-ray3.46E1-201[»]
1VT2X-ray3.30E1-201[»]
2AW4X-ray3.46E1-201[»]
2AWBX-ray3.46E1-201[»]
2GYAelectron microscopy15.00C1-198[»]
2GYCelectron microscopy15.00C1-198[»]
2I2TX-ray3.22E1-201[»]
2I2VX-ray3.22E1-201[»]
2J28electron microscopy8.00E1-201[»]
2QAMX-ray3.21E1-201[»]
2QAOX-ray3.21E1-201[»]
2QBAX-ray3.54E1-201[»]
2QBCX-ray3.54E1-201[»]
2QBEX-ray3.30E1-201[»]
2QBGX-ray3.30E1-201[»]
2QBIX-ray4.00E1-201[»]
2QBKX-ray4.00E1-201[»]
2QOVX-ray3.93E1-201[»]
2QOXX-ray3.93E1-201[»]
2QOZX-ray3.50E1-201[»]
2QP1X-ray3.50E1-201[»]
2RDOelectron microscopy9.10E1-201[»]
2VHMX-ray3.74E1-201[»]
2VHNX-ray3.74E1-201[»]
2WWQelectron microscopy5.80E1-201[»]
2Z4LX-ray4.45E1-201[»]
2Z4NX-ray4.45E1-201[»]
3BBXelectron microscopy10.00E1-201[»]
3DF2X-ray3.50E1-201[»]
3DF4X-ray3.50E1-201[»]
3E1Belectron microscopy-11-201[»]
3E1Delectron microscopy-11-201[»]
3FIKelectron microscopy6.70E1-201[»]
3I1NX-ray3.19E1-201[»]
3I1PX-ray3.19E1-201[»]
3I1RX-ray3.81E1-201[»]
3I1TX-ray3.81E1-201[»]
3I20X-ray3.71E1-201[»]
3I22X-ray3.71E1-201[»]
3IZTelectron microscopy-F1-201[»]
3IZUelectron microscopy-F1-201[»]
3J01electron microscopy-E1-201[»]
3J0Telectron microscopy12.10F1-201[»]
3J0Welectron microscopy14.70F1-201[»]
3J0Yelectron microscopy13.50F1-201[»]
3J11electron microscopy13.10F1-201[»]
3J12electron microscopy11.50F1-201[»]
3J14electron microscopy11.50F1-201[»]
3J19electron microscopy8.30E1-201[»]
3J37electron microscopy9.80F1-201[»]
3J4Xelectron microscopy12.00E1-201[»]
3J50electron microscopy20.00E1-201[»]
3J51electron microscopy17.00E1-201[»]
3J52electron microscopy12.00E1-201[»]
3J54electron microscopy13.00E1-201[»]
3J56electron microscopy15.00E1-201[»]
3J58electron microscopy17.00E1-201[»]
3J5Aelectron microscopy12.00E1-201[»]
3J5Celectron microscopy17.00E1-201[»]
3J5Eelectron microscopy17.00E1-201[»]
3J5Gelectron microscopy20.00E1-201[»]
3J5Ielectron microscopy15.00E1-201[»]
3J5Kelectron microscopy9.00E1-201[»]
3J5Lelectron microscopy6.60E1-201[»]
3J5Oelectron microscopy6.80E1-201[»]
3J5Uelectron microscopy7.60F1-201[»]
3J5Welectron microscopy7.60F1-201[»]
3KCRelectron microscopy-E1-201[»]
3OASX-ray3.25E1-201[»]
3OATX-ray3.25E1-201[»]
3OFCX-ray3.19E1-201[»]
3OFDX-ray3.19E1-201[»]
3OFQX-ray3.10E1-201[»]
3OFRX-ray3.10E1-201[»]
3OFZX-ray3.29E1-201[»]
3OG0X-ray3.29E1-201[»]
3ORBX-ray3.30E1-201[»]
3R8SX-ray3.00E1-201[»]
3R8TX-ray3.00E1-201[»]
3SGFX-ray3.20E1-201[»]
3UOSX-ray3.70E1-201[»]
4CSUelectron microscopy5.50E1-201[»]
4GARX-ray3.30E1-201[»]
4GAUX-ray3.30E1-201[»]
4KIXX-ray2.90E1-201[»]
4KIZX-ray2.90E1-201[»]
4KJ1X-ray2.90E1-201[»]
4KJ3X-ray2.90E1-201[»]
4KJ5X-ray2.90E1-201[»]
4KJ7X-ray2.90E1-201[»]
4KJ9X-ray2.90E1-201[»]
4KJBX-ray2.90E1-201[»]
DisProtiDP00600.
ProteinModelPortaliP60723.
SMRiP60723. Positions 1-201.

Miscellaneous databases

EvolutionaryTraceiP60723.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0088.
HOGENOMiHOG000248766.
KOiK02926.
OMAiFDEYLYL.
OrthoDBiEOG6M0T9G.
PhylomeDBiP60723.

Family and domain databases

Gene3Di3.40.1370.10. 1 hit.
HAMAPiMF_01328_B. Ribosomal_L4_B.
InterProiIPR002136. Ribosomal_L4/L1e.
IPR013005. Ribosomal_L4/L1e_bac-type.
IPR023574. Ribosomal_L4_dom.
[Graphical view]
PANTHERiPTHR10746. PTHR10746. 1 hit.
PfamiPF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMiSSF52166. SSF52166. 1 hit.
TIGRFAMsiTIGR03953. rplD_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

P60723-1 [UniParc]FASTAAdd to Basket

« Hide

MELVLKDAQS ALTVSETTFG RDFNEALVHQ VVVAYAAGAR QGTRAQKTRA    50
EVTGSGKKPW RQKGTGRARS GSIKSPIWRS GGVTFAARPQ DHSQKVNKKM 100
YRGALKSILS ELVRQDRLIV VEKFSVEAPK TKLLAQKLKD MALEDVLIIT 150
GELDENLFLA ARNLHKVDVR DATGIDPVSL IAFDKVVMTA DAVKQVEEML 200
A 201
Length:201
Mass (Da):22,087
Last modified:July 21, 1986 - v1
Checksum:i3A953206B0F083B5
GO

Mass spectrometryi

Molecular mass is 22086.2 Da from positions 1 - 201. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631K → E in strain: N282; confers erythromycin resistance. Ribosomes bind erythromycin poorly and have reduced peptidyltransferase activity. 50S subunits assemble normally, even in the presence of drug, but assembly is cold-sensitive at 20 degrees Celsius.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02613 Genomic DNA. Translation: CAA26461.1.
U18997 Genomic DNA. Translation: AAA58116.1.
U00096 Genomic DNA. Translation: AAC76344.1.
AP009048 Genomic DNA. Translation: BAE77972.1.
PIRiC23129. R5EC4.
RefSeqiNP_417778.1. NC_000913.3.
YP_492113.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76344; AAC76344; b3319.
BAE77972; BAE77972; BAE77972.
GeneIDi12932297.
947818.
KEGGiecj:Y75_p3857.
eco:b3319.
PATRICi32122070. VBIEscCol129921_3412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02613 Genomic DNA. Translation: CAA26461.1 .
U18997 Genomic DNA. Translation: AAA58116.1 .
U00096 Genomic DNA. Translation: AAC76344.1 .
AP009048 Genomic DNA. Translation: BAE77972.1 .
PIRi C23129. R5EC4.
RefSeqi NP_417778.1. NC_000913.3.
YP_492113.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P85 electron microscopy 12.30 C 1-201 [» ]
1P86 electron microscopy 11.50 C 1-201 [» ]
1VS6 X-ray 3.46 E 1-201 [» ]
1VS8 X-ray 3.46 E 1-201 [» ]
1VT2 X-ray 3.30 E 1-201 [» ]
2AW4 X-ray 3.46 E 1-201 [» ]
2AWB X-ray 3.46 E 1-201 [» ]
2GYA electron microscopy 15.00 C 1-198 [» ]
2GYC electron microscopy 15.00 C 1-198 [» ]
2I2T X-ray 3.22 E 1-201 [» ]
2I2V X-ray 3.22 E 1-201 [» ]
2J28 electron microscopy 8.00 E 1-201 [» ]
2QAM X-ray 3.21 E 1-201 [» ]
2QAO X-ray 3.21 E 1-201 [» ]
2QBA X-ray 3.54 E 1-201 [» ]
2QBC X-ray 3.54 E 1-201 [» ]
2QBE X-ray 3.30 E 1-201 [» ]
2QBG X-ray 3.30 E 1-201 [» ]
2QBI X-ray 4.00 E 1-201 [» ]
2QBK X-ray 4.00 E 1-201 [» ]
2QOV X-ray 3.93 E 1-201 [» ]
2QOX X-ray 3.93 E 1-201 [» ]
2QOZ X-ray 3.50 E 1-201 [» ]
2QP1 X-ray 3.50 E 1-201 [» ]
2RDO electron microscopy 9.10 E 1-201 [» ]
2VHM X-ray 3.74 E 1-201 [» ]
2VHN X-ray 3.74 E 1-201 [» ]
2WWQ electron microscopy 5.80 E 1-201 [» ]
2Z4L X-ray 4.45 E 1-201 [» ]
2Z4N X-ray 4.45 E 1-201 [» ]
3BBX electron microscopy 10.00 E 1-201 [» ]
3DF2 X-ray 3.50 E 1-201 [» ]
3DF4 X-ray 3.50 E 1-201 [» ]
3E1B electron microscopy - 1 1-201 [» ]
3E1D electron microscopy - 1 1-201 [» ]
3FIK electron microscopy 6.70 E 1-201 [» ]
3I1N X-ray 3.19 E 1-201 [» ]
3I1P X-ray 3.19 E 1-201 [» ]
3I1R X-ray 3.81 E 1-201 [» ]
3I1T X-ray 3.81 E 1-201 [» ]
3I20 X-ray 3.71 E 1-201 [» ]
3I22 X-ray 3.71 E 1-201 [» ]
3IZT electron microscopy - F 1-201 [» ]
3IZU electron microscopy - F 1-201 [» ]
3J01 electron microscopy - E 1-201 [» ]
3J0T electron microscopy 12.10 F 1-201 [» ]
3J0W electron microscopy 14.70 F 1-201 [» ]
3J0Y electron microscopy 13.50 F 1-201 [» ]
3J11 electron microscopy 13.10 F 1-201 [» ]
3J12 electron microscopy 11.50 F 1-201 [» ]
3J14 electron microscopy 11.50 F 1-201 [» ]
3J19 electron microscopy 8.30 E 1-201 [» ]
3J37 electron microscopy 9.80 F 1-201 [» ]
3J4X electron microscopy 12.00 E 1-201 [» ]
3J50 electron microscopy 20.00 E 1-201 [» ]
3J51 electron microscopy 17.00 E 1-201 [» ]
3J52 electron microscopy 12.00 E 1-201 [» ]
3J54 electron microscopy 13.00 E 1-201 [» ]
3J56 electron microscopy 15.00 E 1-201 [» ]
3J58 electron microscopy 17.00 E 1-201 [» ]
3J5A electron microscopy 12.00 E 1-201 [» ]
3J5C electron microscopy 17.00 E 1-201 [» ]
3J5E electron microscopy 17.00 E 1-201 [» ]
3J5G electron microscopy 20.00 E 1-201 [» ]
3J5I electron microscopy 15.00 E 1-201 [» ]
3J5K electron microscopy 9.00 E 1-201 [» ]
3J5L electron microscopy 6.60 E 1-201 [» ]
3J5O electron microscopy 6.80 E 1-201 [» ]
3J5U electron microscopy 7.60 F 1-201 [» ]
3J5W electron microscopy 7.60 F 1-201 [» ]
3KCR electron microscopy - E 1-201 [» ]
3OAS X-ray 3.25 E 1-201 [» ]
3OAT X-ray 3.25 E 1-201 [» ]
3OFC X-ray 3.19 E 1-201 [» ]
3OFD X-ray 3.19 E 1-201 [» ]
3OFQ X-ray 3.10 E 1-201 [» ]
3OFR X-ray 3.10 E 1-201 [» ]
3OFZ X-ray 3.29 E 1-201 [» ]
3OG0 X-ray 3.29 E 1-201 [» ]
3ORB X-ray 3.30 E 1-201 [» ]
3R8S X-ray 3.00 E 1-201 [» ]
3R8T X-ray 3.00 E 1-201 [» ]
3SGF X-ray 3.20 E 1-201 [» ]
3UOS X-ray 3.70 E 1-201 [» ]
4CSU electron microscopy 5.50 E 1-201 [» ]
4GAR X-ray 3.30 E 1-201 [» ]
4GAU X-ray 3.30 E 1-201 [» ]
4KIX X-ray 2.90 E 1-201 [» ]
4KIZ X-ray 2.90 E 1-201 [» ]
4KJ1 X-ray 2.90 E 1-201 [» ]
4KJ3 X-ray 2.90 E 1-201 [» ]
4KJ5 X-ray 2.90 E 1-201 [» ]
4KJ7 X-ray 2.90 E 1-201 [» ]
4KJ9 X-ray 2.90 E 1-201 [» ]
4KJB X-ray 2.90 E 1-201 [» ]
DisProti DP00600.
ProteinModelPortali P60723.
SMRi P60723. Positions 1-201.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-35791N.
IntActi P60723. 214 interactions.
MINTi MINT-1219709.
STRINGi 511145.b3319.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P60723.
PRIDEi P60723.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76344 ; AAC76344 ; b3319 .
BAE77972 ; BAE77972 ; BAE77972 .
GeneIDi 12932297.
947818.
KEGGi ecj:Y75_p3857.
eco:b3319.
PATRICi 32122070. VBIEscCol129921_3412.

Organism-specific databases

EchoBASEi EB0860.
EcoGenei EG10867. rplD.

Phylogenomic databases

eggNOGi COG0088.
HOGENOMi HOG000248766.
KOi K02926.
OMAi FDEYLYL.
OrthoDBi EOG6M0T9G.
PhylomeDBi P60723.

Enzyme and pathway databases

BioCyci EcoCyc:EG10867-MONOMER.
ECOL316407:JW3281-MONOMER.

Miscellaneous databases

EvolutionaryTracei P60723.
PROi P60723.

Gene expression databases

Genevestigatori P60723.

Family and domain databases

Gene3Di 3.40.1370.10. 1 hit.
HAMAPi MF_01328_B. Ribosomal_L4_B.
InterProi IPR002136. Ribosomal_L4/L1e.
IPR013005. Ribosomal_L4/L1e_bac-type.
IPR023574. Ribosomal_L4_dom.
[Graphical view ]
PANTHERi PTHR10746. PTHR10746. 1 hit.
Pfami PF00573. Ribosomal_L4. 1 hit.
[Graphical view ]
SUPFAMi SSF52166. SSF52166. 1 hit.
TIGRFAMsi TIGR03953. rplD_bact. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of protein L4 from the large subunit of the Escherichia coli ribosome."
    Kimura M., Wittmann-Liebold B.
    FEBS Lett. 121:317-322(1980)
    Cited for: PROTEIN SEQUENCE.
  2. "Structure of the Escherichia coli S10 ribosomal protein operon."
    Zurawski G., Zurawski S.M.
    Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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 1-12.
    Strain: K12 / EMG2.
  6. "Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
    Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
    EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-50, CROSS-LINKING TO RRNA.
    Strain: MRE-600.
  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. "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. "Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins."
    Wittmann H.G., Stoffler G., Apirion D., Rosen L., Tanaka K., Tamaki M., Takata R., Dekio S., Otaka E.
    Mol. Gen. Genet. 127:175-189(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOCHEMICAL CHARACTERIZATION OF AN ERYTHROMYCIN-RESISTANT VARIANT.
    Strain: N282.
  10. "Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
    Herold M., Nierhaus K.H.
    J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
    Strain: K12.
  11. "Autogenous control of the S10 ribosomal protein operon of Escherichia coli: genetic dissection of transcriptional and posttranscriptional regulation."
    Freedman L.P., Zengel J.M., Archer R.H., Lindahl L.
    Proc. Natl. Acad. Sci. U.S.A. 84:6516-6520(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCRIPTION/TRANSLATION REGULATION.
    Strain: K12 / LL308.
  12. "Escherichia coli ribosomal protein L4 stimulates transcription termination at a specific site in the leader of the S10 operon independent of L4-mediated inhibition of translation."
    Zengel J.M., Lindahl L.
    J. Mol. Biol. 213:67-78(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MECHANISM OF TRANSCRIPTIONAL REGULATION.
    Strain: K12 / LL308.
  13. "Ribosomal protein L4 stimulates in vitro termination of transcription at a NusA-dependent terminator in the S10 operon leader."
    Zengel J.M., Lindahl L.
    Proc. Natl. Acad. Sci. U.S.A. 87:2675-2679(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: REQUIREMENT FOR NUSA IN TRANSCRIPTION TERMINATION CONTROL.
  14. "Ribosomal protein gene sequence changes in erythromycin-resistant mutants of Escherichia coli."
    Chittum H.S., Champney W.S.
    J. Bacteriol. 176:6192-6198(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF CHANGES IN AN ERYTHROMYCIN-RESISTANT VARIANT.
    Strain: N282.
  15. "Erythromycin inhibits the assembly of the large ribosomal subunit in growing Escherichia coli cells."
    Chittum H.S., Champney W.S.
    Curr. Microbiol. 30:273-279(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ERYTHROMYCIN AND RIBOSOME ASSEMBLY.
    Strain: N282 and SK901.
  16. "Ribosomal protein L4 from Escherichia coli utilizes nonidentical determinants for its structural and regulatory functions."
    Li X., Lindahl L., Zengel J.M.
    RNA 2:24-37(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: REQUIREMENT FOR RNA-BINDING, MUTAGENESIS, REGULATION-DEFECTIVE MUTANTS.
    Strain: K12 / LL308.
  17. "Phylogenetic analysis of L4-mediated autogenous control of the S10 ribosomal protein operon."
    Allen T., Shen P., Samsel L., Liu R., Lindahl L., Zengel J.M.
    J. Bacteriol. 181:6124-6132(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ABILITY TO REGULATE S10 OPERON EXPRESSION IN OTHER BACTERIA.
    Strain: K12 / LL308.
  18. "The extended loops of ribosomal proteins L4 and L22 are not required for ribosome assembly or L4-mediated autogenous control."
    Zengel J.M., Jerauld A., Walker A., Wahl M.C., Lindahl L.
    RNA 9:1188-1197(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REQUIREMENT FOR RIBOSOME ASSEMBLY, S10 OPERON REGULATION.
    Strain: K12 / LL308.
  19. "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.
  20. "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.
  21. "The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22."
    Gabashvili I.S., Gregory S.T., Valle M., Grassucci R., Worbs M., Wahl M.C., Dahlberg A.E., Frank J.
    Mol. Cell 8:181-188(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (17.8 ANGSTROMS), EFFECT OF THE ERYTHROMYCIN-RESISTANT VARIANT ON THE POLYPEPTIDE EXIT TUNNEL.
    Strain: N282.
  22. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL4_ECOLI
AccessioniPrimary (citable) accession number: P60723
Secondary accession number(s): P02388, Q2M6Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The erythromycin sensitive allele is dominant over the resistant allele.

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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