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Protein

50S ribosomal protein L1

Gene

rplA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

  • RNA binding Source: GO_Central
  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: CAFA
  • tRNA binding Source: UniProtKB-KW

GO - Biological processi

  • maturation of LSU-rRNA Source: GO_Central
  • negative regulation of translational initiation Source: EcoCyc
  • ribosomal large subunit assembly Source: CAFA
  • translation Source: InterPro

Keywordsi

Molecular functionRepressor, Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, tRNA-binding
Biological processTranslation regulation

Enzyme and pathway databases

BioCyciEcoCyc:EG10864-MONOMER
MetaCyc:EG10864-MONOMER

Protein family/group databases

MoonProtiP0A7L0

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L1
Alternative name(s):
Large ribosomal subunit protein uL11 Publication
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: CAFA

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-2DPAGEiP0A7L0

Interactioni

Subunit structurei

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

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi4259509, 105 interactors
DIPiDIP-35746N
IntActiP0A7L0, 133 interactors
STRINGi316385.ECDH10B_4172

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[»]
5U9Felectron microscopy3.20031-234[»]
5U9Gelectron microscopy3.20031-234[»]
5UYKelectron microscopy3.90033-225[»]
5UYLelectron microscopy3.60031-234[»]
5UYMelectron microscopy3.20033-225[»]
5UYNelectron microscopy4.00033-225[»]
5UYPelectron microscopy3.90033-225[»]
5UYQelectron microscopy3.80033-225[»]
6BU8electron microscopy3.50033-225[»]
6ENJelectron microscopy3.7076-229[»]
6ENUelectron microscopy3.1076-229[»]
ProteinModelPortaliP0A7L0
SMRiP0A7L0
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7L0

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C64 Bacteria
COG0081 LUCA
HOGENOMiHOG000207015
InParanoidiP0A7L0
KOiK02863
OMAiGWTDVDV
PhylomeDBiP0A7L0

Family and domain databases

CDDicd00403 Ribosomal_L1, 1 hit
Gene3Di3.40.50.790, 1 hit
HAMAPiMF_01318_B Ribosomal_L1_B, 1 hit
InterProiView protein in InterPro
IPR005878 Ribosom_L1_bac-type
IPR002143 Ribosomal_L1
IPR023674 Ribosomal_L1-like
IPR028364 Ribosomal_L1/biogenesis
IPR016095 Ribosomal_L1_3-a/b-sand
IPR023673 Ribosomal_L1_CS
PfamiView protein in Pfam
PF00687 Ribosomal_L1, 1 hit
PIRSFiPIRSF002155 Ribosomal_L1, 1 hit
SUPFAMiSSF56808 SSF56808, 1 hit
TIGRFAMsiTIGR01169 rplA_bact, 1 hit
PROSITEiView protein in PROSITE
PS01199 RIBOSOMAL_L1, 1 hit

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
PATRICifig|1411691.4.peg.2728

Similar proteinsi

Entry informationi

Entry nameiRL1_ECOLI
AccessioniPrimary (citable) accession number: P0A7L0
Secondary accession number(s): P02384, Q2M8S0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 125 of the entry and version 2 of the sequence. See 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
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Main funding by: National Institutes of Health