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P60624 (RL24_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L24
Gene names
Name:rplX
Ordered Locus Names:b3309, JW3271
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length104 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Ref.6

Subunit structure

Part of the 50S ribosomal subunit. Might contact the SecYEG translocation complex when it is docked with the ribosome. Ref.8

Sequence similarities

Belongs to the ribosomal protein L24P family.

Mass spectrometry

Molecular mass is 11186.5 Da from positions 2 - 104. Determined by MALDI. Ref.9

Binary interactions

With

Entry

#Exp.

IntAct

Notes

phoBP0AFJ51EBI-546481,EBI-1116564

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 10410350S ribosomal protein L24 HAMAP-Rule MF_01326_B
PRO_0000130654

Secondary structure

............................ 104
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60624 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0ABF7DD305FA07F5

FASTA10411,316
        10         20         30         40         50         60 
MAAKIRRDDE VIVLTGKDKG KRGKVKNVLS SGKVIVEGIN LVKKHQKPVP ALNQPGGIVE 

        70         80         90        100 
KEAAIQVSNV AIFNAATGKA DRVGFRFEDG KKVRFFKSNS ETIK 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Structures of the bacterial ribosome at 3.5 A resolution."
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.
Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRR5EC24. H65123.
RefSeqNP_417768.1. NC_000913.3.
YP_492123.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00u2-104[»]
1P85electron microscopy12.30S2-104[»]
1P86electron microscopy11.50S2-104[»]
1VS6X-ray3.46U1-104[»]
1VS8X-ray3.46U1-104[»]
1VT2X-ray3.30U1-104[»]
2AW4X-ray3.46U2-104[»]
2AWBX-ray3.46U2-104[»]
2GYAelectron microscopy15.00S4-102[»]
2GYCelectron microscopy15.00S4-102[»]
2I2TX-ray3.22U2-104[»]
2I2VX-ray3.22U2-104[»]
2J28electron microscopy8.00U2-103[»]
2QAMX-ray3.21U2-104[»]
2QAOX-ray3.21U2-104[»]
2QBAX-ray3.54U2-104[»]
2QBCX-ray3.54U2-104[»]
2QBEX-ray3.30U2-104[»]
2QBGX-ray3.30U2-104[»]
2QBIX-ray4.00U2-104[»]
2QBKX-ray4.00U2-104[»]
2QOVX-ray3.93U2-104[»]
2QOXX-ray3.93U2-104[»]
2QOZX-ray3.50U2-104[»]
2QP1X-ray3.50U2-104[»]
2RDOelectron microscopy9.10U2-104[»]
2VHMX-ray3.74U2-104[»]
2VHNX-ray3.74U2-104[»]
2VRHelectron microscopy19.00C2-104[»]
2WWQelectron microscopy5.80U2-103[»]
2Z4LX-ray4.45U2-104[»]
2Z4NX-ray4.45U2-104[»]
3BBXelectron microscopy10.00U2-104[»]
3DF2X-ray3.50U2-103[»]
3DF4X-ray3.50U2-103[»]
3E1Belectron microscopy-O1-103[»]
3E1Delectron microscopy-O1-103[»]
3FIKelectron microscopy6.70U2-103[»]
3I1NX-ray3.19U1-104[»]
3I1PX-ray3.19U1-104[»]
3I1RX-ray3.81U1-104[»]
3I1TX-ray3.81U1-104[»]
3I20X-ray3.71U1-104[»]
3I22X-ray3.71U1-104[»]
3IZTelectron microscopy-V1-104[»]
3IZUelectron microscopy-V1-104[»]
3J01electron microscopy-U2-104[»]
3J0Telectron microscopy12.10W2-104[»]
3J0Welectron microscopy14.70W2-104[»]
3J0Yelectron microscopy13.50W2-104[»]
3J11electron microscopy13.10W2-104[»]
3J12electron microscopy11.50W2-104[»]
3J14electron microscopy11.50W2-104[»]
3J19electron microscopy8.30U2-103[»]
3J37electron microscopy9.80Y2-104[»]
3J45electron microscopy9.50U2-104[»]
3J46electron microscopy10.10U2-104[»]
3J4Xelectron microscopy12.00U1-103[»]
3J50electron microscopy20.00U1-103[»]
3J51electron microscopy17.00U1-103[»]
3J52electron microscopy12.00U1-103[»]
3J54electron microscopy13.00U1-103[»]
3J56electron microscopy15.00U1-103[»]
3J58electron microscopy17.00U1-103[»]
3J5Aelectron microscopy12.00U1-103[»]
3J5Celectron microscopy17.00U1-103[»]
3J5Eelectron microscopy17.00U1-103[»]
3J5Gelectron microscopy20.00U1-103[»]
3J5Ielectron microscopy15.00U1-103[»]
3J5Kelectron microscopy9.00U1-103[»]
3J5Lelectron microscopy6.60U2-103[»]
3J5Oelectron microscopy6.80U1-104[»]
3J5Uelectron microscopy7.60W2-104[»]
3J5Welectron microscopy7.60X2-104[»]
3KCRelectron microscopy-U1-104[»]
3OASX-ray3.25U2-103[»]
3OATX-ray3.25U2-103[»]
3OFCX-ray3.19U2-103[»]
3OFDX-ray3.19U2-103[»]
3OFQX-ray3.10U2-103[»]
3OFRX-ray3.10U2-103[»]
3OFZX-ray3.29U2-103[»]
3OG0X-ray3.29U2-103[»]
3ORBX-ray3.30U1-104[»]
3R8SX-ray3.00U2-103[»]
3R8TX-ray3.00U2-103[»]
3SGFX-ray3.20Y1-104[»]
3UOSX-ray3.70Y1-104[»]
4GARX-ray3.30U1-104[»]
4GAUX-ray3.30U1-104[»]
4KIXX-ray2.90U1-104[»]
4KIZX-ray2.90U1-104[»]
4KJ1X-ray2.90U1-104[»]
4KJ3X-ray2.90U1-104[»]
4KJ5X-ray2.90U1-104[»]
4KJ7X-ray2.90U1-104[»]
4KJ9X-ray2.90U1-104[»]
4KJBX-ray2.90U1-104[»]
ProteinModelPortalP60624.
SMRP60624. Positions 2-103.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47846N.
IntActP60624. 51 interactions.
MINTMINT-1294921.
STRING511145.b3309.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP60624.
PRIDEP60624.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76334; AAC76334; b3309.
BAE77982; BAE77982; BAE77982.
GeneID12934409.
947810.
KEGGecj:Y75_p3867.
eco:b3309.
PATRIC32122050. VBIEscCol129921_3402.

Organism-specific databases

EchoBASEEB0877.
EcoGeneEG10884. rplX.

Phylogenomic databases

eggNOGCOG0198.
HOGENOMHOG000039892.
KOK02895.
OMAINEHAYL.
OrthoDBEOG6FFSDM.
PhylomeDBP60624.

Enzyme and pathway databases

BioCycEcoCyc:EG10884-MONOMER.
ECOL316407:JW3271-MONOMER.

Gene expression databases

GenevestigatorP60624.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
HAMAPMF_01326_B. Ribosomal_L24_B.
InterProIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR003256. Ribosomal_L24.
IPR005825. Ribosomal_L24/26_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERPTHR12903. PTHR12903. 1 hit.
PfamPF00467. KOW. 1 hit.
[Graphical view]
SMARTSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMSSF50104. SSF50104. 1 hit.
TIGRFAMsTIGR01079. rplX_bact. 1 hit.
PROSITEPS01108. RIBOSOMAL_L24. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP60624.
PROP60624.

Entry information

Entry nameRL24_ECOLI
AccessionPrimary (citable) accession number: P60624
Secondary accession number(s): P02425, P37438, Q2M6X4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene