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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, PubMed:16272117). 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, PubMed:16272117). Contacts the P and E site tRNAs.2 Publications
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.

GO - Molecular functioni

GO - Biological processi

  • maturation of LSU-rRNA Source: GO_Central
  • negative regulation of translational initiation Source: EcoCyc
  • 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.
MetaCyc:EG10864-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10864. rplA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001256542 – 23450S ribosomal protein L1Add BLAST233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei105N6-succinyllysine1 Publication1
Modified residuei154N6-succinyllysine1 Publication1
Modified residuei186N6-succinyllysine1 Publication1
Modified residuei197N6-succinyllysine1 Publication1

Proteomic databases

EPDiP0A7L0.
PaxDbiP0A7L0.
PRIDEiP0A7L0.

2D gel databases

SWISS-2DPAGEP0A7L0.

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

BioGridi4259509. 35 interactors.
DIPiDIP-35746N.
IntActiP0A7L0. 125 interactors.
MINTiMINT-1268287.
STRINGi511145.b3984.

Structurei

Secondary structure

1234
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50N1-229[»]
1ML5electron microscopy14.00c2-229[»]
2RDOelectron microscopy9.1092-234[»]
3J46electron microscopy10.1051-234[»]
3J5Selectron microscopy7.50F1-234[»]
3J8Gelectron microscopy5.0051-234[»]
3J9Zelectron microscopy3.60LC1-234[»]
3JA1electron microscopy3.60LC1-234[»]
3JCDelectron microscopy3.7051-234[»]
3JCEelectron microscopy3.2051-234[»]
487Delectron microscopy7.50H29-201[»]
4CSUelectron microscopy5.5051-234[»]
4U1UX-ray2.95B52-229[»]
4U1VX-ray3.00B52-229[»]
4U20X-ray2.90B52-229[»]
4U24X-ray2.90B52-229[»]
4U25X-ray2.90B52-229[»]
4U26X-ray2.80B52-229[»]
4U27X-ray2.80B52-229[»]
4V4Velectron microscopy15.00B26-227[»]
4V4Welectron microscopy15.00B26-227[»]
4V5Helectron microscopy5.80B51-234[»]
4V65electron microscopy9.00BZ5-220[»]
4V66electron microscopy9.00BZ5-220[»]
4V69electron microscopy6.70B51-234[»]
4V6Kelectron microscopy8.25AC1-234[»]
4V6Lelectron microscopy13.20BC1-234[»]
4V6Melectron microscopy7.10B51-234[»]
4V6Nelectron microscopy12.10AC1-234[»]
4V6Oelectron microscopy14.70BC1-234[»]
4V6Pelectron microscopy13.50BC1-234[»]
4V6Qelectron microscopy11.50BC1-234[»]
4V6Relectron microscopy11.50BC1-234[»]
4V6Selectron microscopy13.10AC1-234[»]
4V6Velectron microscopy9.80BC1-234[»]
4V6Yelectron microscopy12.00B51-234[»]
4V6Zelectron microscopy12.00B51-234[»]
4V70electron microscopy17.00B51-234[»]
4V71electron microscopy20.00B51-234[»]
4V72electron microscopy13.00B51-234[»]
4V73electron microscopy15.00B51-234[»]
4V74electron microscopy17.00B51-234[»]
4V75electron microscopy12.00B51-234[»]
4V76electron microscopy17.00B51-234[»]
4V77electron microscopy17.00B51-234[»]
4V78electron microscopy20.00B51-234[»]
4V79electron microscopy15.00B51-234[»]
4V7Aelectron microscopy9.00B51-234[»]
4V7Celectron microscopy7.60BC2-234[»]
4V7Delectron microscopy7.60AC2-234[»]
4V7Ielectron microscopy9.60A51-234[»]
4WOIX-ray3.00B52-229[»]
5ADYelectron microscopy4.5051-234[»]
ProteinModelPortaliP0A7L0.
SMRiP0A7L0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7L0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L1P family.Curated

Phylogenomic databases

eggNOGiENOG4105C64. Bacteria.
COG0081. LUCA.
HOGENOMiHOG000207015.
InParanoidiP0A7L0.
KOiK02863.
OMAiKIQNDKV.
PhylomeDBiP0A7L0.

Family and domain databases

CDDicd00403. Ribosomal_L1. 1 hit.
Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPiMF_01318_B. Ribosomal_L1_B. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti12R → I AA sequence (PubMed:9298646).Curated1

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.
WP_001096684.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76958; AAC76958; b3984.
BAE77336; BAE77336; BAE77336.
GeneIDi948483.
KEGGiecj:JW3947.
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.
WP_001096684.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50N1-229[»]
1ML5electron microscopy14.00c2-229[»]
2RDOelectron microscopy9.1092-234[»]
3J46electron microscopy10.1051-234[»]
3J5Selectron microscopy7.50F1-234[»]
3J8Gelectron microscopy5.0051-234[»]
3J9Zelectron microscopy3.60LC1-234[»]
3JA1electron microscopy3.60LC1-234[»]
3JCDelectron microscopy3.7051-234[»]
3JCEelectron microscopy3.2051-234[»]
487Delectron microscopy7.50H29-201[»]
4CSUelectron microscopy5.5051-234[»]
4U1UX-ray2.95B52-229[»]
4U1VX-ray3.00B52-229[»]
4U20X-ray2.90B52-229[»]
4U24X-ray2.90B52-229[»]
4U25X-ray2.90B52-229[»]
4U26X-ray2.80B52-229[»]
4U27X-ray2.80B52-229[»]
4V4Velectron microscopy15.00B26-227[»]
4V4Welectron microscopy15.00B26-227[»]
4V5Helectron microscopy5.80B51-234[»]
4V65electron microscopy9.00BZ5-220[»]
4V66electron microscopy9.00BZ5-220[»]
4V69electron microscopy6.70B51-234[»]
4V6Kelectron microscopy8.25AC1-234[»]
4V6Lelectron microscopy13.20BC1-234[»]
4V6Melectron microscopy7.10B51-234[»]
4V6Nelectron microscopy12.10AC1-234[»]
4V6Oelectron microscopy14.70BC1-234[»]
4V6Pelectron microscopy13.50BC1-234[»]
4V6Qelectron microscopy11.50BC1-234[»]
4V6Relectron microscopy11.50BC1-234[»]
4V6Selectron microscopy13.10AC1-234[»]
4V6Velectron microscopy9.80BC1-234[»]
4V6Yelectron microscopy12.00B51-234[»]
4V6Zelectron microscopy12.00B51-234[»]
4V70electron microscopy17.00B51-234[»]
4V71electron microscopy20.00B51-234[»]
4V72electron microscopy13.00B51-234[»]
4V73electron microscopy15.00B51-234[»]
4V74electron microscopy17.00B51-234[»]
4V75electron microscopy12.00B51-234[»]
4V76electron microscopy17.00B51-234[»]
4V77electron microscopy17.00B51-234[»]
4V78electron microscopy20.00B51-234[»]
4V79electron microscopy15.00B51-234[»]
4V7Aelectron microscopy9.00B51-234[»]
4V7Celectron microscopy7.60BC2-234[»]
4V7Delectron microscopy7.60AC2-234[»]
4V7Ielectron microscopy9.60A51-234[»]
4WOIX-ray3.00B52-229[»]
5ADYelectron microscopy4.5051-234[»]
ProteinModelPortaliP0A7L0.
SMRiP0A7L0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259509. 35 interactors.
DIPiDIP-35746N.
IntActiP0A7L0. 125 interactors.
MINTiMINT-1268287.
STRINGi511145.b3984.

Protein family/group databases

MoonProtiP0A7L0.

2D gel databases

SWISS-2DPAGEP0A7L0.

Proteomic databases

EPDiP0A7L0.
PaxDbiP0A7L0.
PRIDEiP0A7L0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76958; AAC76958; b3984.
BAE77336; BAE77336; BAE77336.
GeneIDi948483.
KEGGiecj:JW3947.
eco:b3984.
PATRICi32123489. VBIEscCol129921_4097.

Organism-specific databases

EchoBASEiEB0857.
EcoGeneiEG10864. rplA.

Phylogenomic databases

eggNOGiENOG4105C64. Bacteria.
COG0081. LUCA.
HOGENOMiHOG000207015.
InParanoidiP0A7L0.
KOiK02863.
OMAiKIQNDKV.
PhylomeDBiP0A7L0.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7L0.
PROiP0A7L0.

Family and domain databases

CDDicd00403. Ribosomal_L1. 1 hit.
Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPiMF_01318_B. Ribosomal_L1_B. 1 hit.
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...

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: November 2, 2016
This is version 113 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

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 one 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.