50S ribosomal protein L24 - Escherichia coli (strain K12)

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P60624 (RL24_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
50S ribosomal protein L24

Gene names

Name:	rplX
Ordered Locus Names:	b3309, JW3271

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	104 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.6 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

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: InterPro
Cellular component	cytosolic large ribosomal subunit Inferred from direct assay. Source: EcoliWiki
Molecular function	rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosome Inferred from direct assay. Source: EcoliWiki
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
phoB	P0AFJ5	1	EBI-546481,EBI-1116564

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 104

103

50S ribosomal protein L24 HAMAP MF_01326_B

PRO_0000130654

Secondary structure

104

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P60624 [UniParc].

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

104

11,316

        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' referencesShow '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: 6222285] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 391595] [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: 6262737] [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: 357435] [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: 6760192] [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: 3298242] [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: 10094780] [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: 16292303] [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: 12809609] [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: 16272117] [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.

PIR

R5EC24. H65123.

RefSeq

NP_417768.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	S	2-104	[»]
1P86	electron microscopy	11.50	S	2-104	[»]
1VS6	X-ray	3.46	U	1-104	[»]
1VS8	X-ray	3.46	U	1-104	[»]
1VT2	X-ray	3.30	U	1-104	[»]
2AW4	X-ray	3.46	U	2-104	[»]
2AWB	X-ray	3.46	U	2-104	[»]
2GYA	electron microscopy	15.00	S	4-101	[»]
2GYC	electron microscopy	15.00	S	4-102	[»]
2I2T	X-ray	3.22	U	2-103	[»]
2I2V	X-ray	3.22	U	2-103	[»]
2J28	electron microscopy	8.00	U	2-102	[»]
2QAM	X-ray	3.21	U	2-104	[»]
2QAO	X-ray	3.21	U	2-104	[»]
2QBA	X-ray	3.54	U	2-104	[»]
2QBC	X-ray	3.54	U	2-104	[»]
2QBE	X-ray	3.30	U	2-104	[»]
2QBG	X-ray	3.30	U	2-104	[»]
2QBI	X-ray	4.00	U	2-104	[»]
2QBK	X-ray	4.00	U	2-104	[»]
2QOV	X-ray	3.93	U	2-104	[»]
2QOX	X-ray	3.93	U	2-104	[»]
2QOZ	X-ray	3.50	U	2-104	[»]
2QP1	X-ray	3.50	U	2-104	[»]
2RDO	electron microscopy	9.10	U	2-104	[»]
2VHM	X-ray	3.74	U	2-104	[»]
2VHN	X-ray	3.74	U	2-104	[»]
2VRH	electron microscopy	19.00	C	2-104	[»]
2WWQ	electron microscopy	5.80	U	2-103	[»]
2Z4L	X-ray	4.45	U	2-104	[»]
2Z4N	X-ray	4.45	U	2-104	[»]
3BBX	electron microscopy	10.00	U	2-104	[»]
3DF2	X-ray	3.50	U	2-103	[»]
3DF4	X-ray	3.50	U	2-103	[»]
3E1B	electron microscopy	-	O	1-103	[»]
3E1D	electron microscopy	-	O	1-103	[»]
3FIK	electron microscopy	6.70	U	2-103	[»]
3I1N	X-ray	3.19	U	1-104	[»]
3I1P	X-ray	3.19	U	1-104	[»]
3I1R	X-ray	3.81	U	1-104	[»]
3I1T	X-ray	3.81	U	1-104	[»]
3I20	X-ray	3.71	U	1-104	[»]
3I22	X-ray	3.71	U	1-104	[»]
3IZT	electron microscopy	-	V	1-104	[»]
3IZU	electron microscopy	-	V	1-104	[»]
3J01	electron microscopy	-	U	2-104	[»]
3KCR	electron microscopy	-	U	1-104	[»]
3OAS	X-ray	3.25	U	2-103	[»]
3OAT	X-ray	3.25	U	2-103	[»]
3OFC	X-ray	3.19	U	2-103	[»]
3OFD	X-ray	3.19	U	2-103	[»]
3OFQ	X-ray	3.10	U	2-103	[»]
3OFR	X-ray	3.10	U	2-103	[»]
3OFZ	X-ray	3.29	U	2-103	[»]
3OG0	X-ray	3.29	U	2-103	[»]
3ORB	X-ray	3.30	U	1-104	[»]
3R8S	X-ray	3.00	U	2-103	[»]
3R8T	X-ray	3.00	U	2-103	[»]

ProteinModelPortal

P60624.

SMR

P60624. Positions 2-103.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47846N.

IntAct

P60624. 51 interactions.

MINT

MINT-1294921.

Proteomic databases

PRIDE

P60624.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001889; EBESCP00000001889; EBESCG00000001551.
EBESCT00000015488; EBESCP00000014779; EBESCG00000014548.

GeneID

947810.

GenomeReviews

Gene locus JW3271 in contig AP009048_GR.
Gene locus b3309 in contig U00096_GR.

KEGG

ecj:JW3271.
eco:b3309.

PATRIC

32122050. VBIEscCol129921_3402.

Organism-specific databases

EchoBASE

EB0877.

EcoGene

EG10884. rplX.

Phylogenomic databases

eggNOG

COG0198.

GeneTree

EBGT00050000010431.

HOGENOM

HBG588578.

OMA

VEQEAPI.

PhylomeDB

P60624.

ProtClustDB

PRK00004.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10884-MONOMER.

Gene expression databases

Genevestigator

P60624.

Family and domain databases

HAMAP

MF_01326_B. Ribosomal_L24_B.
[Tree]

InterPro

IPR005824. KOW.
IPR003256. Ribosomal_L24.
IPR005825. Ribosomal_L24/26_CS.
IPR014723. Ribosomal_L24_SH3-like.
IPR008991. Translation_prot_SH3-like.
[Graphical view]

Gene3D

G3DSA:2.30.30.200. Ribosomal_L24_SH3-like. 1 hit.

K02895.

PANTHER

PTHR12903. Ribosomal_L24. 1 hit.

Pfam

PF00467. KOW. 1 hit.
[Graphical view]

SMART

SM00739. KOW. 1 hit.
[Graphical view]

SUPFAM

SSF50104. Transl_SH3_like. 1 hit.

TIGRFAMs

TIGR01079. RplX_bact. 1 hit.

PROSITE

PS01108. RIBOSOMAL_L24. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RL24_ECOLI

Accession

Primary (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:	January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents