Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

50S ribosomal protein L4

Gene

rplD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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. RNA binding Source: GO_Central
  2. rRNA binding Source: UniProtKB-HAMAP
  3. structural constituent of ribosome Source: GO_Central
  4. translation repressor activity Source: EcoliWiki

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: GO_Central
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. 1 PublicationAdd
BLAST
Mutagenesisi67 – 10337Missing : Regulates the S10 operon normally. Does not assemble into ribosomes in vivo. 1 PublicationAdd
BLAST
Mutagenesisi93 – 1019Missing : Regulates the S10 operon normally. Not stably associated with the ribosome in vivo. 1 Publication
Mutagenesisi131 – 1311T → I: Does not regulate the S10 operon; assembles into ribosomes in vivo. 1 Publication
Mutagenesisi134 – 1341L → P: Does not regulate the S10 operon in vivo. 1 Publication
Mutagenesisi160 – 1601A → V: Does not regulate the S10 operon; assembles into ribosomes in vivo. 1 Publication
Mutagenesisi167 – 1671V → D: Does not regulate the S10 operon in vivo. 1 Publication
Mutagenesisi171 – 20131DATGI…EEMLA → RRSK: Loss of S10 operon regulation. Assembles into ribosomes in vivo. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20120150S ribosomal protein L4PRO_0000129215Add
BLAST

Proteomic databases

PaxDbiP60723.
PRIDEiP60723.

Expressioni

Gene expression databases

GenevestigatoriP60723.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

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

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 83Combined sources
Helixi16 – 194Combined sources
Beta strandi22 – 243Combined sources
Helixi25 – 3915Combined sources
Turni49 – 513Combined sources
Beta strandi52 – 543Combined sources
Beta strandi62 – 676Combined sources
Beta strandi78 – 803Combined sources
Beta strandi83 – 853Combined sources
Helixi98 – 11417Combined sources
Beta strandi118 – 1225Combined sources
Beta strandi127 – 1293Combined sources
Helixi131 – 14111Combined sources
Beta strandi144 – 1529Combined sources
Helixi155 – 1595Combined sources
Turni160 – 1634Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi167 – 1715Combined sources
Helixi172 – 1743Combined sources
Helixi179 – 1824Combined sources
Beta strandi183 – 1897Combined sources
Helixi190 – 20011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00E1-201[»]
2RDOelectron microscopy9.10E1-201[»]
3BBXelectron microscopy10.00E1-201[»]
3J5Lelectron microscopy6.60E1-201[»]
3J7Zelectron microscopy3.90E1-201[»]
4CSUelectron microscopy5.50E1-201[»]
4U1UX-ray2.95E1-201[»]
4U1VX-ray3.00E1-201[»]
4U20X-ray2.90E1-201[»]
4U24X-ray2.90E1-201[»]
4U25X-ray2.90E1-201[»]
4U26X-ray2.80E1-201[»]
4U27X-ray2.80E1-201[»]
4V47electron microscopy12.30C1-201[»]
4V48electron microscopy11.50C1-201[»]
4V4HX-ray3.46E1-201[»]
4V4QX-ray3.46E1-201[»]
4V4Velectron microscopy15.00C1-198[»]
4V4Welectron microscopy15.00C1-198[»]
4V50X-ray3.22E1-201[»]
4V52X-ray3.21E1-201[»]
4V53X-ray3.54E1-201[»]
4V54X-ray3.30E1-201[»]
4V55X-ray4.00E1-201[»]
4V56X-ray3.93E1-201[»]
4V57X-ray3.50E1-201[»]
4V5BX-ray3.74E1-201[»]
4V5Helectron microscopy5.80E1-201[»]
4V5YX-ray4.45E1-201[»]
4V64X-ray3.50E1-201[»]
4V65electron microscopy-11-201[»]
4V69electron microscopy6.70E1-201[»]
4V6CX-ray3.19E1-201[»]
4V6DX-ray3.81E1-201[»]
4V6EX-ray3.71E1-201[»]
4V6Kelectron microscopy-F1-201[»]
4V6Lelectron microscopy-F1-201[»]
4V6Melectron microscopy-E1-201[»]
4V6Nelectron microscopy12.10F1-201[»]
4V6Oelectron microscopy14.70F1-201[»]
4V6Pelectron microscopy13.50F1-201[»]
4V6Qelectron microscopy11.50F1-201[»]
4V6Relectron microscopy11.50F1-201[»]
4V6Selectron microscopy13.10F1-201[»]
4V6Telectron microscopy8.30E1-201[»]
4V6Velectron microscopy9.80F1-201[»]
4V6Yelectron microscopy12.00E1-201[»]
4V6Zelectron microscopy12.00E1-201[»]
4V70electron microscopy17.00E1-201[»]
4V71electron microscopy20.00E1-201[»]
4V72electron microscopy13.00E1-201[»]
4V73electron microscopy15.00E1-201[»]
4V74electron microscopy17.00E1-201[»]
4V75electron microscopy12.00E1-201[»]
4V76electron microscopy17.00E1-201[»]
4V77electron microscopy17.00E1-201[»]
4V78electron microscopy20.00E1-201[»]
4V79electron microscopy15.00E1-201[»]
4V7Aelectron microscopy9.00E1-201[»]
4V7Belectron microscopy6.80E1-201[»]
4V7Celectron microscopy7.60F1-201[»]
4V7Delectron microscopy7.60F1-201[»]
4V7Ielectron microscopy-E1-201[»]
4V7SX-ray3.25E1-201[»]
4V7TX-ray3.19E1-201[»]
4V7UX-ray3.10E1-201[»]
4V7VX-ray3.29E1-201[»]
4V85X-ray3.20E1-201[»]
4V89X-ray3.70E1-201[»]
4V9CX-ray3.30E1-201[»]
4V9DX-ray3.00E1-201[»]
4V9OX-ray2.90E1-201[»]
4V9PX-ray2.90E1-201[»]
4WF1X-ray3.09E1-201[»]
4WWWX-ray3.30E1-201[»]
DisProtiDP00600.
ProteinModelPortaliP60723.
SMRiP60723. Positions 1-201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60723.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L4P family.Curated

Phylogenomic databases

eggNOGiCOG0088.
HOGENOMiHOG000248766.
InParanoidiP60723.
KOiK02926.
OMAiTVKGPIW.
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

        10         20         30         40         50
MELVLKDAQS ALTVSETTFG RDFNEALVHQ VVVAYAAGAR QGTRAQKTRA
60 70 80 90 100
EVTGSGKKPW RQKGTGRARS GSIKSPIWRS GGVTFAARPQ DHSQKVNKKM
110 120 130 140 150
YRGALKSILS ELVRQDRLIV VEKFSVEAPK TKLLAQKLKD MALEDVLIIT
160 170 180 190 200
GELDENLFLA ARNLHKVDVR DATGIDPVSL IAFDKVVMTA DAVKQVEEML

A
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00E1-201[»]
2RDOelectron microscopy9.10E1-201[»]
3BBXelectron microscopy10.00E1-201[»]
3J5Lelectron microscopy6.60E1-201[»]
3J7Zelectron microscopy3.90E1-201[»]
4CSUelectron microscopy5.50E1-201[»]
4U1UX-ray2.95E1-201[»]
4U1VX-ray3.00E1-201[»]
4U20X-ray2.90E1-201[»]
4U24X-ray2.90E1-201[»]
4U25X-ray2.90E1-201[»]
4U26X-ray2.80E1-201[»]
4U27X-ray2.80E1-201[»]
4V47electron microscopy12.30C1-201[»]
4V48electron microscopy11.50C1-201[»]
4V4HX-ray3.46E1-201[»]
4V4QX-ray3.46E1-201[»]
4V4Velectron microscopy15.00C1-198[»]
4V4Welectron microscopy15.00C1-198[»]
4V50X-ray3.22E1-201[»]
4V52X-ray3.21E1-201[»]
4V53X-ray3.54E1-201[»]
4V54X-ray3.30E1-201[»]
4V55X-ray4.00E1-201[»]
4V56X-ray3.93E1-201[»]
4V57X-ray3.50E1-201[»]
4V5BX-ray3.74E1-201[»]
4V5Helectron microscopy5.80E1-201[»]
4V5YX-ray4.45E1-201[»]
4V64X-ray3.50E1-201[»]
4V65electron microscopy-11-201[»]
4V69electron microscopy6.70E1-201[»]
4V6CX-ray3.19E1-201[»]
4V6DX-ray3.81E1-201[»]
4V6EX-ray3.71E1-201[»]
4V6Kelectron microscopy-F1-201[»]
4V6Lelectron microscopy-F1-201[»]
4V6Melectron microscopy-E1-201[»]
4V6Nelectron microscopy12.10F1-201[»]
4V6Oelectron microscopy14.70F1-201[»]
4V6Pelectron microscopy13.50F1-201[»]
4V6Qelectron microscopy11.50F1-201[»]
4V6Relectron microscopy11.50F1-201[»]
4V6Selectron microscopy13.10F1-201[»]
4V6Telectron microscopy8.30E1-201[»]
4V6Velectron microscopy9.80F1-201[»]
4V6Yelectron microscopy12.00E1-201[»]
4V6Zelectron microscopy12.00E1-201[»]
4V70electron microscopy17.00E1-201[»]
4V71electron microscopy20.00E1-201[»]
4V72electron microscopy13.00E1-201[»]
4V73electron microscopy15.00E1-201[»]
4V74electron microscopy17.00E1-201[»]
4V75electron microscopy12.00E1-201[»]
4V76electron microscopy17.00E1-201[»]
4V77electron microscopy17.00E1-201[»]
4V78electron microscopy20.00E1-201[»]
4V79electron microscopy15.00E1-201[»]
4V7Aelectron microscopy9.00E1-201[»]
4V7Belectron microscopy6.80E1-201[»]
4V7Celectron microscopy7.60F1-201[»]
4V7Delectron microscopy7.60F1-201[»]
4V7Ielectron microscopy-E1-201[»]
4V7SX-ray3.25E1-201[»]
4V7TX-ray3.19E1-201[»]
4V7UX-ray3.10E1-201[»]
4V7VX-ray3.29E1-201[»]
4V85X-ray3.20E1-201[»]
4V89X-ray3.70E1-201[»]
4V9CX-ray3.30E1-201[»]
4V9DX-ray3.00E1-201[»]
4V9OX-ray2.90E1-201[»]
4V9PX-ray2.90E1-201[»]
4WF1X-ray3.09E1-201[»]
4WWWX-ray3.30E1-201[»]
DisProtiDP00600.
ProteinModelPortaliP60723.
SMRiP60723. Positions 1-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB01361. Troleandomycin.

Proteomic databases

PaxDbiP60723.
PRIDEiP60723.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0860.
EcoGeneiEG10867. rplD.

Phylogenomic databases

eggNOGiCOG0088.
HOGENOMiHOG000248766.
InParanoidiP60723.
KOiK02926.
OMAiTVKGPIW.
OrthoDBiEOG6M0T9G.
PhylomeDBiP60723.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP60723.
PROiP60723.

Gene expression databases

GenevestigatoriP60723.

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.
ProtoNetiSearch...

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: March 4, 2015
This is version 128 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.