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Protein

50S ribosomal protein L1

Gene

rplA

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, it binds very close to the 3'-end of the 23S rRNA. Forms part of the L1 stalk. It is often not seen in high-resolution crystal structures, but can be seen in cryo_EM and 3D reconstruction models. These indicate that the distal end of the stalk moves by approximately 20 angstroms (PubMed:12859903). This stalk movement is thought to be coupled to movement of deacylated tRNA into and out of the E site, and thus to participate in tRNA translocation (PubMed:12859903). Contacts the P and E site tRNAs.1 Publication
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro
  3. tRNA binding Source: UniProtKB-KW

GO - Biological processi

  1. negative regulation of translational initiation Source: EcoCyc
  2. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10864-MONOMER.
ECOL316407:JW3947-MONOMER.

Protein family/group databases

MoonProtiP0A7L0.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L1
Gene namesi
Name:rplA
Ordered Locus Names:b3984, JW3947
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10864. rplA.

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 – 23423350S ribosomal protein L1PRO_0000125654Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051N6-succinyllysine1 Publication
Modified residuei154 – 1541N6-succinyllysine1 Publication
Modified residuei186 – 1861N6-succinyllysine1 Publication
Modified residuei197 – 1971N6-succinyllysine1 Publication

Proteomic databases

PaxDbiP0A7L0.
PRIDEiP0A7L0.

2D gel databases

SWISS-2DPAGEP0A7L0.

Expressioni

Gene expression databases

GenevestigatoriP0A7L0.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Cross-links to the P and E site tRNAs.

Binary interactionsi

WithEntry#Exp.IntActNotes
cspGP0A9782EBI-543771,EBI-547581
thrSP0A8M32EBI-543771,EBI-551254

Protein-protein interaction databases

DIPiDIP-35746N.
IntActiP0A7L0. 125 interactions.
MINTiMINT-1268287.
STRINGi511145.b3984.

Structurei

Secondary structure

1
234
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 105
Beta strandi11 – 144
Helixi22 – 276
Beta strandi30 – 323
Beta strandi35 – 373
Beta strandi45 – 473
Turni54 – 563
Beta strandi74 – 774
Helixi82 – 898
Beta strandi92 – 954
Helixi99 – 1057
Beta strandi111 – 1155
Helixi117 – 1193
Helixi120 – 1256
Helixi127 – 1304
Turni131 – 1344
Turni139 – 1424
Helixi148 – 1547
Beta strandi162 – 1643
Beta strandi168 – 1703
Helixi181 – 19616
Beta strandi207 – 2115
Beta strandi214 – 2174

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50N1-229[»]
1ML5electron microscopy14.00c2-229[»]
2RDOelectron microscopy9.1092-234[»]
3J46electron microscopy10.1051-234[»]
3J5Selectron microscopy7.50F1-234[»]
487Delectron microscopy7.50H29-201[»]
4CSUelectron microscopy5.5051-234[»]
4V4Velectron microscopy15.0026-227[»]
4V4Welectron microscopy15.0026-227[»]
4V5Helectron microscopy5.8051-234[»]
4V65electron microscopy9.00Z131-224[»]
4V66electron microscopy9.00Z131-224[»]
4V69electron microscopy6.7051-234[»]
4V6Kelectron microscopy-C1-234[»]
4V6Lelectron microscopy-C1-234[»]
4V6Melectron microscopy-51-234[»]
4V6Nelectron microscopy12.10C1-234[»]
4V6Oelectron microscopy14.70C1-234[»]
4V6Pelectron microscopy13.50C1-234[»]
4V6Qelectron microscopy11.50C1-234[»]
4V6Relectron microscopy11.50C1-234[»]
4V6Selectron microscopy13.10C1-234[»]
4V6Velectron microscopy9.80C1-234[»]
4V6Yelectron microscopy12.0051-234[»]
4V6Zelectron microscopy12.0051-234[»]
4V70electron microscopy17.0051-234[»]
4V71electron microscopy20.0051-234[»]
4V72electron microscopy13.0051-234[»]
4V73electron microscopy15.0051-234[»]
4V74electron microscopy17.0051-234[»]
4V75electron microscopy12.0051-234[»]
4V76electron microscopy17.0051-234[»]
4V77electron microscopy17.0051-234[»]
4V78electron microscopy20.0051-234[»]
4V79electron microscopy15.0051-234[»]
4V7Aelectron microscopy9.0051-234[»]
4V7Celectron microscopy7.60C2-234[»]
4V7Delectron microscopy7.60C2-234[»]
4V7Ielectron microscopy-51-234[»]
ProteinModelPortaliP0A7L0.
SMRiP0A7L0. Positions 1-234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7L0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L1P family.Curated

Phylogenomic databases

eggNOGiCOG0081.
HOGENOMiHOG000207015.
InParanoidiP0A7L0.
KOiK02863.
OMAiGTKEYSI.
OrthoDBiEOG6FBX2G.
PhylomeDBiP0A7L0.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPiMF_01318_B. Ribosomal_L1_B.
InterProiIPR005878. Ribosom_L1_bac-type.
IPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
[Graphical view]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
TIGRFAMsiTIGR01169. rplA_bact. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7L0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKLTKRMRV IREKVDATKQ YDINEAIALL KELATAKFVE SVDVAVNLGI
60 70 80 90 100
DARKSDQNVR GATVLPHGTG RSVRVAVFTQ GANAEAAKAA GAELVGMEDL
110 120 130 140 150
ADQIKKGEMN FDVVIASPDA MRVVGQLGQV LGPRGLMPNP KVGTVTPNVA
160 170 180 190 200
EAVKNAKAGQ VRYRNDKNGI IHTTIGKVDF DADKLKENLE ALLVALKKAK
210 220 230
PTQAKGVYIK KVSISTTMGA GVAVDQAGLS ASVN
Length:234
Mass (Da):24,730
Last modified:January 23, 2007 - v2
Checksum:iD751704B34748D53
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121R → I AA sequence (PubMed:9298646).Curated

Mass spectrometryi

Molecular mass is 24598.9 Da from positions 2 - 234. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00339 Genomic DNA. Translation: CAA23622.1.
U00006 Genomic DNA. Translation: AAC43082.1.
U00096 Genomic DNA. Translation: AAC76958.1.
AP009048 Genomic DNA. Translation: BAE77336.1.
PIRiS12573. R5EC1.
RefSeqiNP_418411.1. NC_000913.3.
YP_491477.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76958; AAC76958; b3984.
BAE77336; BAE77336; BAE77336.
GeneIDi12930515.
948483.
KEGGiecj:Y75_p3213.
eco:b3984.
PATRICi32123489. VBIEscCol129921_4097.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00339 Genomic DNA. Translation: CAA23622.1.
U00006 Genomic DNA. Translation: AAC43082.1.
U00096 Genomic DNA. Translation: AAC76958.1.
AP009048 Genomic DNA. Translation: BAE77336.1.
PIRiS12573. R5EC1.
RefSeqiNP_418411.1. NC_000913.3.
YP_491477.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50N1-229[»]
1ML5electron microscopy14.00c2-229[»]
2RDOelectron microscopy9.1092-234[»]
3J46electron microscopy10.1051-234[»]
3J5Selectron microscopy7.50F1-234[»]
487Delectron microscopy7.50H29-201[»]
4CSUelectron microscopy5.5051-234[»]
4V4Velectron microscopy15.0026-227[»]
4V4Welectron microscopy15.0026-227[»]
4V5Helectron microscopy5.8051-234[»]
4V65electron microscopy9.00Z131-224[»]
4V66electron microscopy9.00Z131-224[»]
4V69electron microscopy6.7051-234[»]
4V6Kelectron microscopy-C1-234[»]
4V6Lelectron microscopy-C1-234[»]
4V6Melectron microscopy-51-234[»]
4V6Nelectron microscopy12.10C1-234[»]
4V6Oelectron microscopy14.70C1-234[»]
4V6Pelectron microscopy13.50C1-234[»]
4V6Qelectron microscopy11.50C1-234[»]
4V6Relectron microscopy11.50C1-234[»]
4V6Selectron microscopy13.10C1-234[»]
4V6Velectron microscopy9.80C1-234[»]
4V6Yelectron microscopy12.0051-234[»]
4V6Zelectron microscopy12.0051-234[»]
4V70electron microscopy17.0051-234[»]
4V71electron microscopy20.0051-234[»]
4V72electron microscopy13.0051-234[»]
4V73electron microscopy15.0051-234[»]
4V74electron microscopy17.0051-234[»]
4V75electron microscopy12.0051-234[»]
4V76electron microscopy17.0051-234[»]
4V77electron microscopy17.0051-234[»]
4V78electron microscopy20.0051-234[»]
4V79electron microscopy15.0051-234[»]
4V7Aelectron microscopy9.0051-234[»]
4V7Celectron microscopy7.60C2-234[»]
4V7Delectron microscopy7.60C2-234[»]
4V7Ielectron microscopy-51-234[»]
ProteinModelPortaliP0A7L0.
SMRiP0A7L0. Positions 1-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35746N.
IntActiP0A7L0. 125 interactions.
MINTiMINT-1268287.
STRINGi511145.b3984.

Chemistry

ChEMBLiCHEMBL2363135.

Protein family/group databases

MoonProtiP0A7L0.

2D gel databases

SWISS-2DPAGEP0A7L0.

Proteomic databases

PaxDbiP0A7L0.
PRIDEiP0A7L0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76958; AAC76958; b3984.
BAE77336; BAE77336; BAE77336.
GeneIDi12930515.
948483.
KEGGiecj:Y75_p3213.
eco:b3984.
PATRICi32123489. VBIEscCol129921_4097.

Organism-specific databases

EchoBASEiEB0857.
EcoGeneiEG10864. rplA.

Phylogenomic databases

eggNOGiCOG0081.
HOGENOMiHOG000207015.
InParanoidiP0A7L0.
KOiK02863.
OMAiGTKEYSI.
OrthoDBiEOG6FBX2G.
PhylomeDBiP0A7L0.

Enzyme and pathway databases

BioCyciEcoCyc:EG10864-MONOMER.
ECOL316407:JW3947-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7L0.
PROiP0A7L0.

Gene expression databases

GenevestigatoriP0A7L0.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPiMF_01318_B. Ribosomal_L1_B.
InterProiIPR005878. Ribosom_L1_bac-type.
IPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
[Graphical view]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
TIGRFAMsiTIGR01169. rplA_bact. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. "The primary structure of protein L1 from the large ribosomal subunit of Escherichia coli."
    Brauer D., Oechsner I.
    FEBS Lett. 96:317-321(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-234.
    Strain: K.
  6. Erratum
    Brauer D., Oechsner I.
    FEBS Lett. 98:411-411(1979)
  7. "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.
  8. "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 199-203, CROSS-LINKING TO RRNA.
    Strain: MRE-600.
  9. "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.
  10. "Translational regulation of the L11 ribosomal protein operon of Escherichia coli: mutations that define the target site for repression by L1."
    Thomas M.S., Nomura M.
    Nucleic Acids Res. 15:3085-3096(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: MECHANISM OF TRANSLATION REGULATION.
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
  11. "The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
    Osswald M., Doering T., Brimacombe R.
    Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
    Strain: MRE-600.
  12. "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.
  13. "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.
  14. "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.
    Strain: MRE-600.
  15. "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-105; LYS-154; LYS-186 AND LYS-197.
    Strain: K12.
  16. Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES IMPLYING THE INVOLVEMENT OF THE L1 STALK IN TRANSLOCATION OF TRNAS FROM THE P TO E SITE.
  17. Cited for: LOCALIZATION IN THE 3.5 ANGSTROM RIBOSOMAL STRUCTURES AND DISCUSSION OF ITS MOVEMENT.
    Strain: MRE-600.

Entry informationi

Entry nameiRL1_ECOLI
AccessioniPrimary (citable) accession number: P0A7L0
Secondary accession number(s): P02384, Q2M8S0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 99 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

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.