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Protein

50S ribosomal protein L24

Gene

rplX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.1 Publication
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.1 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10884-MONOMER.
ECOL316407:JW3271-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L24
Gene namesi
Name:rplX
Ordered Locus Names:b3309, JW3271
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10884. rplX.

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 – 11Removed1 Publication
Chaini2 – 10410350S ribosomal protein L24PRO_0000130654Add
BLAST

Proteomic databases

PaxDbiP60624.
PRIDEiP60624.

Expressioni

Gene expression databases

GenevestigatoriP60624.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Might contact the SecYEG translocation complex when it is docked with the ribosome.

Binary interactionsi

WithEntry#Exp.IntActNotes
phoBP0AFJ51EBI-546481,EBI-1116564

Protein-protein interaction databases

DIPiDIP-47846N.
IntActiP60624. 51 interactions.
MINTiMINT-1294921.
STRINGi511145.b3309.

Structurei

Secondary structure

1
104
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 134Combined sources
Beta strandi15 – 184Combined sources
Beta strandi22 – 298Combined sources
Turni30 – 323Combined sources
Beta strandi33 – 364Combined sources
Turni37 – 393Combined sources
Beta strandi40 – 467Combined sources
Beta strandi50 – 534Combined sources
Beta strandi57 – 626Combined sources
Helixi67 – 693Combined sources
Beta strandi70 – 734Combined sources
Turni75 – 773Combined sources
Beta strandi78 – 803Combined sources
Beta strandi83 – 886Combined sources
Beta strandi91 – 999Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00u2-104[»]
2J28electron microscopy8.00U2-103[»]
2RDOelectron microscopy9.10U2-104[»]
2VRHelectron microscopy19.00C2-104[»]
3BBXelectron microscopy10.00U2-104[»]
3J45electron microscopy9.50U2-104[»]
3J46electron microscopy10.10U2-104[»]
3J5Lelectron microscopy6.60U2-103[»]
3J7Zelectron microscopy3.90U1-104[»]
4CSUelectron microscopy5.50U2-104[»]
4U1UX-ray2.95BU/DU2-103[»]
4U1VX-ray3.00BU/DU2-103[»]
4U20X-ray2.90BU/DU2-103[»]
4U24X-ray2.90BU/DU2-103[»]
4U25X-ray2.90BU/DU2-103[»]
4U26X-ray2.80BU/DU2-103[»]
4U27X-ray2.80BU/DU2-103[»]
4V47electron microscopy12.30AS2-104[»]
4V48electron microscopy11.50AS2-104[»]
4V4HX-ray3.46BU/DU1-104[»]
4V4QX-ray3.46BU/DU2-104[»]
4V4Velectron microscopy15.00BS4-102[»]
4V4Welectron microscopy15.00BS4-102[»]
4V50X-ray3.22BU/DU2-104[»]
4V52X-ray3.21BU/DU2-104[»]
4V53X-ray3.54BU/DU2-104[»]
4V54X-ray3.30BU/DU2-104[»]
4V55X-ray4.00BU/DU2-104[»]
4V56X-ray3.93BU/DU2-104[»]
4V57X-ray3.50BU/DU2-104[»]
4V5BX-ray3.74AU/CU2-104[»]
4V5Helectron microscopy5.80BU2-103[»]
4V5YX-ray4.45BU/DU2-104[»]
4V64X-ray3.50BU/DU2-104[»]
4V65electron microscopy9.00BO1-103[»]
4V66electron microscopy9.00BO1-103[»]
4V69electron microscopy6.70BU2-103[»]
4V6CX-ray3.19BU/DU1-104[»]
4V6DX-ray3.81BU/DU1-104[»]
4V6EX-ray3.71BU/DU1-104[»]
4V6Kelectron microscopy8.25AV1-104[»]
4V6Lelectron microscopy13.20BV1-104[»]
4V6Melectron microscopy7.10BU2-104[»]
4V6Nelectron microscopy12.10AW2-104[»]
4V6Oelectron microscopy14.70BW2-104[»]
4V6Pelectron microscopy13.50BW2-104[»]
4V6Qelectron microscopy11.50BW2-104[»]
4V6Relectron microscopy11.50BW2-104[»]
4V6Selectron microscopy13.10AW2-104[»]
4V6Telectron microscopy8.30BU2-103[»]
4V6Velectron microscopy9.80Y2-104[»]
4V6Yelectron microscopy12.00BU1-103[»]
4V6Zelectron microscopy12.00BU1-103[»]
4V70electron microscopy17.00BU1-103[»]
4V71electron microscopy20.00BU1-103[»]
4V72electron microscopy13.00BU1-103[»]
4V73electron microscopy15.00BU1-103[»]
4V74electron microscopy17.00BU1-103[»]
4V75electron microscopy12.00BU1-103[»]
4V76electron microscopy17.00BU1-103[»]
4V77electron microscopy17.00BU1-103[»]
4V78electron microscopy20.00BU1-103[»]
4V79electron microscopy15.00BU1-103[»]
4V7Aelectron microscopy9.00BU1-103[»]
4V7Belectron microscopy6.80BU1-104[»]
4V7Celectron microscopy7.60BW2-104[»]
4V7Delectron microscopy7.60AX2-104[»]
4V7Ielectron microscopy9.60AU1-104[»]
4V7SX-ray3.25BU/DU2-103[»]
4V7TX-ray3.19BU/DU2-103[»]
4V7UX-ray3.10BU/DU2-103[»]
4V7VX-ray3.29BU/DU2-103[»]
4V85X-ray3.20Y1-104[»]
4V89X-ray3.70BY1-104[»]
4V9CX-ray3.30BU/DU1-104[»]
4V9DX-ray3.00CU/DU2-103[»]
4V9OX-ray2.90AU/CU/EU/GU1-104[»]
4V9PX-ray2.90AU/CU/EU/GU1-104[»]
4WF1X-ray3.09BU/DU2-103[»]
4WWWX-ray3.10RU/YU2-103[»]
5AFIelectron microscopy2.90U1-104[»]
ProteinModelPortaliP60624.
SMRiP60624. Positions 2-103.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60624.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L24P family.Curated

Phylogenomic databases

eggNOGiCOG0198.
HOGENOMiHOG000039892.
InParanoidiP60624.
KOiK02895.
OMAiDIEAPIH.
OrthoDBiEOG6FFSDM.
PhylomeDBiP60624.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
HAMAPiMF_01326_B. Ribosomal_L24_B.
InterProiIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR003256. Ribosomal_L24.
IPR005825. Ribosomal_L24/26_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR12903. PTHR12903. 1 hit.
PfamiPF00467. KOW. 1 hit.
[Graphical view]
SMARTiSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
TIGRFAMsiTIGR01079. rplX_bact. 1 hit.
PROSITEiPS01108. RIBOSOMAL_L24. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P60624-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAKIRRDDE VIVLTGKDKG KRGKVKNVLS SGKVIVEGIN LVKKHQKPVP
60 70 80 90 100
ALNQPGGIVE KEAAIQVSNV AIFNAATGKA DRVGFRFEDG KKVRFFKSNS

ETIK
Length:104
Mass (Da):11,316
Last modified:January 23, 2007 - v2
Checksum:i0ABF7DD305FA07F5
GO

Mass spectrometryi

Molecular mass is 11186.5 Da from positions 2 - 104. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25716.1.
U18997 Genomic DNA. Translation: AAA58106.1.
U00096 Genomic DNA. Translation: AAC76334.1.
AP009048 Genomic DNA. Translation: BAE77982.1.
M10195 Genomic DNA. Translation: AAA24050.1.
PIRiH65123. R5EC24.
RefSeqiNP_417768.1. NC_000913.3.
YP_492123.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76334; AAC76334; b3309.
BAE77982; BAE77982; BAE77982.
GeneIDi12934409.
947810.
KEGGiecj:Y75_p3867.
eco:b3309.
PATRICi32122050. VBIEscCol129921_3402.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25716.1.
U18997 Genomic DNA. Translation: AAA58106.1.
U00096 Genomic DNA. Translation: AAC76334.1.
AP009048 Genomic DNA. Translation: BAE77982.1.
M10195 Genomic DNA. Translation: AAA24050.1.
PIRiH65123. R5EC24.
RefSeqiNP_417768.1. NC_000913.3.
YP_492123.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00u2-104[»]
2J28electron microscopy8.00U2-103[»]
2RDOelectron microscopy9.10U2-104[»]
2VRHelectron microscopy19.00C2-104[»]
3BBXelectron microscopy10.00U2-104[»]
3J45electron microscopy9.50U2-104[»]
3J46electron microscopy10.10U2-104[»]
3J5Lelectron microscopy6.60U2-103[»]
3J7Zelectron microscopy3.90U1-104[»]
4CSUelectron microscopy5.50U2-104[»]
4U1UX-ray2.95BU/DU2-103[»]
4U1VX-ray3.00BU/DU2-103[»]
4U20X-ray2.90BU/DU2-103[»]
4U24X-ray2.90BU/DU2-103[»]
4U25X-ray2.90BU/DU2-103[»]
4U26X-ray2.80BU/DU2-103[»]
4U27X-ray2.80BU/DU2-103[»]
4V47electron microscopy12.30AS2-104[»]
4V48electron microscopy11.50AS2-104[»]
4V4HX-ray3.46BU/DU1-104[»]
4V4QX-ray3.46BU/DU2-104[»]
4V4Velectron microscopy15.00BS4-102[»]
4V4Welectron microscopy15.00BS4-102[»]
4V50X-ray3.22BU/DU2-104[»]
4V52X-ray3.21BU/DU2-104[»]
4V53X-ray3.54BU/DU2-104[»]
4V54X-ray3.30BU/DU2-104[»]
4V55X-ray4.00BU/DU2-104[»]
4V56X-ray3.93BU/DU2-104[»]
4V57X-ray3.50BU/DU2-104[»]
4V5BX-ray3.74AU/CU2-104[»]
4V5Helectron microscopy5.80BU2-103[»]
4V5YX-ray4.45BU/DU2-104[»]
4V64X-ray3.50BU/DU2-104[»]
4V65electron microscopy9.00BO1-103[»]
4V66electron microscopy9.00BO1-103[»]
4V69electron microscopy6.70BU2-103[»]
4V6CX-ray3.19BU/DU1-104[»]
4V6DX-ray3.81BU/DU1-104[»]
4V6EX-ray3.71BU/DU1-104[»]
4V6Kelectron microscopy8.25AV1-104[»]
4V6Lelectron microscopy13.20BV1-104[»]
4V6Melectron microscopy7.10BU2-104[»]
4V6Nelectron microscopy12.10AW2-104[»]
4V6Oelectron microscopy14.70BW2-104[»]
4V6Pelectron microscopy13.50BW2-104[»]
4V6Qelectron microscopy11.50BW2-104[»]
4V6Relectron microscopy11.50BW2-104[»]
4V6Selectron microscopy13.10AW2-104[»]
4V6Telectron microscopy8.30BU2-103[»]
4V6Velectron microscopy9.80Y2-104[»]
4V6Yelectron microscopy12.00BU1-103[»]
4V6Zelectron microscopy12.00BU1-103[»]
4V70electron microscopy17.00BU1-103[»]
4V71electron microscopy20.00BU1-103[»]
4V72electron microscopy13.00BU1-103[»]
4V73electron microscopy15.00BU1-103[»]
4V74electron microscopy17.00BU1-103[»]
4V75electron microscopy12.00BU1-103[»]
4V76electron microscopy17.00BU1-103[»]
4V77electron microscopy17.00BU1-103[»]
4V78electron microscopy20.00BU1-103[»]
4V79electron microscopy15.00BU1-103[»]
4V7Aelectron microscopy9.00BU1-103[»]
4V7Belectron microscopy6.80BU1-104[»]
4V7Celectron microscopy7.60BW2-104[»]
4V7Delectron microscopy7.60AX2-104[»]
4V7Ielectron microscopy9.60AU1-104[»]
4V7SX-ray3.25BU/DU2-103[»]
4V7TX-ray3.19BU/DU2-103[»]
4V7UX-ray3.10BU/DU2-103[»]
4V7VX-ray3.29BU/DU2-103[»]
4V85X-ray3.20Y1-104[»]
4V89X-ray3.70BY1-104[»]
4V9CX-ray3.30BU/DU1-104[»]
4V9DX-ray3.00CU/DU2-103[»]
4V9OX-ray2.90AU/CU/EU/GU1-104[»]
4V9PX-ray2.90AU/CU/EU/GU1-104[»]
4WF1X-ray3.09BU/DU2-103[»]
4WWWX-ray3.10RU/YU2-103[»]
5AFIelectron microscopy2.90U1-104[»]
ProteinModelPortaliP60624.
SMRiP60624. Positions 2-103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47846N.
IntActiP60624. 51 interactions.
MINTiMINT-1294921.
STRINGi511145.b3309.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP60624.
PRIDEiP60624.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76334; AAC76334; b3309.
BAE77982; BAE77982; BAE77982.
GeneIDi12934409.
947810.
KEGGiecj:Y75_p3867.
eco:b3309.
PATRICi32122050. VBIEscCol129921_3402.

Organism-specific databases

EchoBASEiEB0877.
EcoGeneiEG10884. rplX.

Phylogenomic databases

eggNOGiCOG0198.
HOGENOMiHOG000039892.
InParanoidiP60624.
KOiK02895.
OMAiDIEAPIH.
OrthoDBiEOG6FFSDM.
PhylomeDBiP60624.

Enzyme and pathway databases

BioCyciEcoCyc:EG10884-MONOMER.
ECOL316407:JW3271-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60624.
PROiP60624.

Gene expression databases

GenevestigatoriP60624.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
HAMAPiMF_01326_B. Ribosomal_L24_B.
InterProiIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR003256. Ribosomal_L24.
IPR005825. Ribosomal_L24/26_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR12903. PTHR12903. 1 hit.
PfamiPF00467. KOW. 1 hit.
[Graphical view]
SMARTiSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
TIGRFAMsiTIGR01079. rplX_bact. 1 hit.
PROSITEiPS01108. RIBOSOMAL_L24. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
    Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
    Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "Primary structure of protein L24 from the Escherichia coli ribosome."
    Wittmann-Liebold B.
    FEBS Lett. 108:75-80(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-104.
    Strain: K12.
  5. "Translational regulation by ribosomal protein S8 in Escherichia coli: structural homology between rRNA binding site and feedback target on mRNA."
    Olins P.O., Nomura M.
    Nucleic Acids Res. 9:1757-1764(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 86-104.
    Strain: K12 / JM105 / ATCC 47016.
  6. "The ribosomal protein L24 of Escherichia coli is an assembly protein."
    Spillmann S., Nierhaus K.H.
    J. Biol. Chem. 253:7047-7050(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SUBUNIT ASSEMBLY.
    Strain: K12 / A19.
  7. "Initiator proteins for the assembly of the 50S subunit from Escherichia coli ribosomes."
    Nowotny V., Nierhaus K.H.
    Proc. Natl. Acad. Sci. U.S.A. 79:7238-7242(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS AN ASSEMBLY INITIATOR PROTEIN.
  8. "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.
  9. "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.
  10. "Structure of the E. coli protein-conducting channel bound to a translating ribosome."
    Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III, Ban N., Frank J.
    Nature 438:318-324(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE CONTACT WITH THE SECYEG TRANSLOCATION COMPLEX.
    Strain: MRE-600.
  11. "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.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL24_ECOLI
AccessioniPrimary (citable) accession number: P60624
Secondary accession number(s): P02425, P37438, Q2M6X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 125 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.