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Protein

50S ribosomal protein L23

Gene

rplW

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233).5 Publications

GO - Molecular functioni

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

GO - Biological processi

  • ribosomal large subunit assembly Source: CAFA
  • translation Source: GO_Central

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10883-MONOMER
MetaCyc:EG10883-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L23UniRule annotation
Alternative name(s):
Large ribosomal subunit protein uL231 Publication
Gene namesi
Name:rplWUniRule annotation
Ordered Locus Names:b3318, JW3280
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10883 rplW

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: CAFA

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi16 – 18VSE → AAA: Strongly reduces trigger factor binding. 1 Publication3
Mutagenesisi18E → A: Binds normally to ribosomes; strongly reduces trigger factor binding. 1 Publication1
Mutagenesisi18E → Q: Strongly reduces trigger factor binding. 1 Publication1
Mutagenesisi51 – 53FEV → AAA: No effect on trigger factor binding. 1 Publication3
Mutagenesisi52E → K: No effect on trigger factor binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001294071 – 10050S ribosomal protein L23Add BLAST100

Proteomic databases

EPDiP0ADZ0
PaxDbiP0ADZ0
PRIDEiP0ADZ0

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit (PubMed:391594, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:21499241, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161). Contacts protein L29 and trigger factor. Might also contact SecE and probably does contact SecG and SecY when the SecYEG translocation complex is docked with the ribosome (PubMed:16292303).1 Publication13 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi4261290352 interactors.
DIPiDIP-35972N
IntActiP0ADZ0 81 interactors.
STRINGi316385.ECDH10B_3493

Structurei

Secondary structure

1100
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 8Combined sources5
Beta strandi11 – 14Combined sources4
Helixi18 – 26Combined sources9
Beta strandi29 – 34Combined sources6
Helixi40 – 50Combined sources11
Beta strandi55 – 63Combined sources9
Beta strandi67 – 70Combined sources4
Beta strandi73 – 76Combined sources4
Beta strandi80 – 87Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00t2-85[»]
2J28electron microscopy8.00T1-99[»]
2RDOelectron microscopy9.10T1-100[»]
2VRHelectron microscopy19.00B1-100[»]
3BBXelectron microscopy10.00T1-100[»]
3IY9electron microscopy14.10T1-99[»]
3J45electron microscopy9.50T1-100[»]
3J46electron microscopy10.10T1-100[»]
3J5Lelectron microscopy6.60T1-93[»]
3J7Zelectron microscopy3.90T1-100[»]
3J8Gelectron microscopy5.00T1-100[»]
3J9Yelectron microscopy3.90T1-100[»]
3J9Zelectron microscopy3.60LR1-100[»]
3JA1electron microscopy3.60LV1-100[»]
3JBUelectron microscopy3.64t1-100[»]
3JBVelectron microscopy3.32t1-100[»]
3JCDelectron microscopy3.70T1-100[»]
3JCEelectron microscopy3.20T1-100[»]
3JCJelectron microscopy3.70S1-100[»]
3JCNelectron microscopy4.60T1-100[»]
4CSUelectron microscopy5.50T1-100[»]
4U1UX-ray2.95BT/DT1-93[»]
4U1VX-ray3.00BT/DT1-93[»]
4U20X-ray2.90BT/DT1-93[»]
4U24X-ray2.90BT/DT1-93[»]
4U25X-ray2.90BT/DT1-93[»]
4U26X-ray2.80BT/DT1-93[»]
4U27X-ray2.80BT/DT1-93[»]
4UY8electron microscopy3.80T1-93[»]
4V47electron microscopy12.30AR1-100[»]
4V48electron microscopy11.50AR1-100[»]
4V4HX-ray3.46BT/DT1-100[»]
4V4QX-ray3.46BT/DT1-100[»]
4V4Velectron microscopy15.00BR7-98[»]
4V4Welectron microscopy15.00BR7-98[»]
4V50X-ray3.22BT/DT1-100[»]
4V52X-ray3.21BT/DT1-100[»]
4V53X-ray3.54BT/DT1-100[»]
4V54X-ray3.30BT/DT1-100[»]
4V55X-ray4.00BT/DT1-100[»]
4V56X-ray3.93BT/DT1-100[»]
4V57X-ray3.50BT/DT1-100[»]
4V5BX-ray3.74AT/CT1-100[»]
4V5Helectron microscopy5.80BT1-93[»]
4V5YX-ray4.45BT/DT1-100[»]
4V64X-ray3.50BT/DT1-100[»]
4V65electron microscopy9.00BM1-99[»]
4V66electron microscopy9.00BM1-99[»]
4V69electron microscopy6.70BT1-93[»]
4V6CX-ray3.19BT/DT1-100[»]
4V6DX-ray3.81BT/DT1-100[»]
4V6EX-ray3.71BT/DT1-100[»]
4V6Kelectron microscopy8.25AU1-100[»]
4V6Lelectron microscopy13.20BU1-100[»]
4V6Melectron microscopy7.10BT1-100[»]
4V6Nelectron microscopy12.10AV1-100[»]
4V6Oelectron microscopy14.70BV1-100[»]
4V6Pelectron microscopy13.50BV1-100[»]
4V6Qelectron microscopy11.50BV1-100[»]
4V6Relectron microscopy11.50BV1-100[»]
4V6Selectron microscopy13.10AV1-100[»]
4V6Telectron microscopy8.30BT1-93[»]
4V6Velectron microscopy9.80BX1-100[»]
4V6Yelectron microscopy12.00BT1-93[»]
4V6Zelectron microscopy12.00BT1-93[»]
4V70electron microscopy17.00BT1-93[»]
4V71electron microscopy20.00BT1-93[»]
4V72electron microscopy13.00BT1-93[»]
4V73electron microscopy15.00BT1-93[»]
4V74electron microscopy17.00BT1-93[»]
4V75electron microscopy12.00BT1-93[»]
4V76electron microscopy17.00BT1-93[»]
4V77electron microscopy17.00BT1-93[»]
4V78electron microscopy20.00BT1-93[»]
4V79electron microscopy15.00BT1-93[»]
4V7Aelectron microscopy9.00BT1-93[»]
4V7Belectron microscopy6.80BT1-100[»]
4V7Celectron microscopy7.60BV1-100[»]
4V7Delectron microscopy7.60AW1-100[»]
4V7Ielectron microscopy9.60AT1-100[»]
4V7SX-ray3.25BT/DT1-93[»]
4V7TX-ray3.19BT/DT1-93[»]
4V7UX-ray3.10BT/DT1-93[»]
4V7VX-ray3.29BT/DT1-93[»]
4V85X-ray3.20X1-100[»]
4V89X-ray3.70BX1-100[»]
4V9CX-ray3.30BT/DT1-100[»]
4V9DX-ray3.00CT/DT1-93[»]
4V9OX-ray2.90AT/CT/ET/GT1-100[»]
4V9PX-ray2.90AT/CT/ET/GT1-100[»]
4WF1X-ray3.09BT/DT1-93[»]
4WOIX-ray3.00BT/CT1-100[»]
4WWWX-ray3.10RT/YT1-93[»]
4YBBX-ray2.10CU/DU1-93[»]
5ADYelectron microscopy4.50T1-100[»]
5AFIelectron microscopy2.90T1-100[»]
5AKAelectron microscopy5.70T1-100[»]
5GADelectron microscopy3.70U1-100[»]
5GAEelectron microscopy3.33U1-100[»]
5GAFelectron microscopy4.30U2-96[»]
5GAGelectron microscopy3.80U1-100[»]
5GAHelectron microscopy3.80U1-100[»]
5H5Uelectron microscopy3.00U1-100[»]
5IQRelectron microscopy3.00T1-100[»]
5IT8X-ray3.12CU/DU1-93[»]
5J5BX-ray2.80CU/DU1-93[»]
5J7LX-ray3.00CU/DU1-93[»]
5J88X-ray3.32CU/DU1-100[»]
5J8AX-ray3.10CU/DU1-93[»]
5J91X-ray2.96CU/DU1-93[»]
5JC9X-ray3.03CU/DU1-93[»]
5JTEelectron microscopy3.60BT1-100[»]
5JU8electron microscopy3.60BT1-100[»]
5KCRelectron microscopy3.601X1-100[»]
5KCSelectron microscopy3.901X1-100[»]
5KPSelectron microscopy3.90T1-100[»]
5KPVelectron microscopy4.10S1-100[»]
5KPWelectron microscopy3.90S1-100[»]
5KPXelectron microscopy3.90S1-100[»]
5L3Pelectron microscopy3.70X1-100[»]
5LZAelectron microscopy3.60T1-93[»]
5LZBelectron microscopy5.30T1-93[»]
5LZCelectron microscopy4.80T1-93[»]
5LZDelectron microscopy3.40T1-93[»]
5LZEelectron microscopy3.50T1-93[»]
5LZFelectron microscopy4.60T1-93[»]
5MDVelectron microscopy2.97T1-100[»]
5MDWelectron microscopy3.06T1-100[»]
5MDYelectron microscopy3.35T1-100[»]
5MDZelectron microscopy3.10T1-100[»]
5MGPelectron microscopy3.10T1-93[»]
5NCOelectron microscopy4.80U2-96[»]
5NP6electron microscopy3.60r1-93[»]
5NWYelectron microscopy2.93g1-100[»]
5O2Relectron microscopy3.40T1-93[»]
5U4Ielectron microscopy3.50U1-100[»]
5U9Felectron microscopy3.20221-100[»]
5U9Gelectron microscopy3.20221-100[»]
5UYKelectron microscopy3.90221-93[»]
5UYLelectron microscopy3.60221-93[»]
5UYMelectron microscopy3.20221-93[»]
5UYNelectron microscopy4.00221-93[»]
5UYPelectron microscopy3.90221-93[»]
5UYQelectron microscopy3.80221-93[»]
6BU8electron microscopy3.50221-93[»]
6C4Ielectron microscopy3.24U1-100[»]
6ENFelectron microscopy3.20T1-93[»]
6ENJelectron microscopy3.70T1-93[»]
6ENUelectron microscopy3.10T1-93[»]
ProteinModelPortaliP0ADZ0
SMRiP0ADZ0
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ADZ0

Family & Domainsi

Sequence similaritiesi

Belongs to the universal ribosomal protein uL23 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG41080KG Bacteria
COG0089 LUCA
HOGENOMiHOG000231364
InParanoidiP0ADZ0
KOiK02892
OMAiTMNPPRR
PhylomeDBiP0ADZ0

Family and domain databases

Gene3Di3.30.70.3301 hit
HAMAPiMF_01369_B Ribosomal_L23_B, 1 hit
InterProiView protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR012678 Ribosomal_L23/L15e_core_dom_sf
IPR001014 Ribosomal_L23/L25_CS
IPR013025 Ribosomal_L25/23
PfamiView protein in Pfam
PF00276 Ribosomal_L23, 1 hit
SUPFAMiSSF54189 SSF54189, 1 hit
PROSITEiView protein in PROSITE
PS00050 RIBOSOMAL_L23, 1 hit

Sequencei

Sequence statusi: Complete.

P0ADZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIREERLLKV LRAPHVSEKA STAMEKSNTI VLKVAKDATK AEIKAAVQKL
60 70 80 90 100
FEVEVEVVNT LVVKGKVKRH GQRIGRRSDW KKAYVTLKEG QNLDFVGGAE
Length:100
Mass (Da):11,199
Last modified:December 6, 2005 - v1
Checksum:i30CD1D77CC7CF9EB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti80Missing AA sequence (PubMed:391594).Curated1

Mass spectrometryi

Molecular mass is 11198.0 Da from positions 1 - 100. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA Translation: CAA26462.1
U18997 Genomic DNA Translation: AAA58115.1
U00096 Genomic DNA Translation: AAC76343.1
AP009048 Genomic DNA Translation: BAE77973.1
PIRiA65125 R5EC23
RefSeqiNP_417777.1, NC_000913.3
WP_000617544.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76343; AAC76343; b3318
BAE77973; BAE77973; BAE77973
GeneIDi947819
KEGGiecj:JW3280
eco:b3318
PATRICifig|1411691.4.peg.3413

Similar proteinsi

Entry informationi

Entry nameiRL23_ECOLI
AccessioniPrimary (citable) accession number: P0ADZ0
Secondary accession number(s): P02424, Q2M6Y3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 6, 2005
Last modified: April 25, 2018
This is version 126 of the entry and version 1 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