50S ribosomal protein L18 - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0C018 (RL18_ECOLI)

Last modified June 16, 2009. Version 49. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
50S ribosomal protein L18

Gene names

Name:	rplR
Ordered Locus Names:	b3304, JW3266

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	117 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. Ref.6
Subunit structure	Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs. Ref.9
Domain	The basic N-terminus is not necessary for binding to 5S rRNA. It is however required for cooperative binding of L5 and L18 to 5S rRNA as well as for binding of the 5S rRNA/L5/L18 complex to the 23S rRNA. HAMAP MF_01337
Post-translational modification	The protein has been shown to contain a phosphoserine, which was required for the protein to bind to 5S rRNA (Ref.11). However the presence of this phosphoserine is controversial, and it has not been seen by mass spectrometry. HAMAP MF_01337
Sequence similarities	Belongs to the ribosomal protein L18P family.
Mass spectrometry	Molecular mass is 12769.8 Da from positions 1 - 117. Determined by MALDI. Ref.12

Ontologies

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

117

50S ribosomal protein L18 HAMAP MF_01337

PRO_0000131258

Regions

Region

17

Required for binding of the 5S rRNA/L5/L18 complex to the 23S rRNA HAMAP MF_01337

Secondary structure

1

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117

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P0C018-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: CA1082FF9B5D9697
Show »

117

12,770

        10         20         30         40         50         60 
MDKKSARIRR ATRARRKLQE LGATRLVVHR TPRHIYAQVI APNGSEVLVA ASTVEKAIAE 

        70         80         90        100        110 
QLKYTGNKDA AAAVGKAVAE RALEKGIKDV SFDRSGFQYH GRVQALADAA REAGLQF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of the 5S RNA binding protein L18 from Escherichia coli ribosomes." Brosius J., Schiltz E., Chen R. FEBS Lett. 56:359-361(1975) [PubMed: 1098937] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: K.
[2]	"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.
[3]	"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.
[4]	"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.
[5]	"Stoichiometry, cooperativity, and stability of interactions between 5S RNA and proteins L5, L18, and L25 from the 50S ribosomal subunit of Escherichia coli." Spierer P., Zimmermann R.A. Biochemistry 17:2474-2479(1978) [PubMed: 354687] [Abstract] Cited for: FORMATION OF THE 5S RRNA/L5/L18/L25 SUBCOMPLEX.
[6]	"Fragment of protein L18 from the Escherichia coli ribosome that contains the 5S RNA binding site." Newberry V., Brosius J., Garrett R. Nucleic Acids Res. 5:1753-1766(1978) [PubMed: 353728] [Abstract] Cited for: FUNCTION OF THE BASIC N-TERMINUS.
[7]	"Cooperative interactions among protein and RNA components of the 50S ribosomal subunit of Escherichia coli." Spierer P., Wang C.-C., Marsh T.L., Zimmermann R.A. Nucleic Acids Res. 6:1669-1682(1979) [PubMed: 109811] [Abstract] Cited for: ASSOCIATION OF 5S RRNA/L5/L18 WITH 23S RRNA. Strain: MRE-600.
[8]	"The role of the basic N-terminal region of protein L18 in 5S RNA-23S RNA complex formation." Newberry V., Garrett R.A. Nucleic Acids Res. 8:4131-4142(1980) [PubMed: 6159586] [Abstract] Cited for: REQUIREMENT OF N-TERMINUS FOR FORMATION OF 5S RRNA-23S RRNA COMPLEX. Strain: MRE-600.
[9]	"Assembly map of the large subunit (50S) of Escherichia coli ribosomes." Rohl R., Nierhaus K.H. Proc. Natl. Acad. Sci. U.S.A. 79:729-733(1982) [PubMed: 7038683] [Abstract] Cited for: REQUIREMENT FOR INCORPORATION OF 5S RRNA INTO THE 50S SUBUNIT. Strain: MRE-600.
[10]	"5S rRNA sugar-phosphate backbone protection in complexes with specific ribosomal proteins." Shpanchenko O.V., Zvereva M.I., Dontsova O.A., Nierhaus K.H., Bogdanov A.A. FEBS Lett. 394:71-75(1996) [PubMed: 8925931] [Abstract] Cited for: CHARACTERIZATION OF A 5S RRNA/L5/L18/L25 SUBCOMPLEX. Strain: K12 / A19.
[11]	"Phosphorylation of ribosomal protein L18 is required for its folding and binding to 5S rRNA." Bloemink M.J., Moore P.B. Biochemistry 38:13385-13390(1999) [PubMed: 10529214] [Abstract] Cited for: PHOSPHORYLATION.
[12]	"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.
[13]	"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.
[14]	"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

X01563 Genomic DNA. Translation: CAA25721.1.
U18997 Genomic DNA. Translation: AAA58101.1.
U00096 Genomic DNA. Translation: AAC76329.1.
AP009048 Genomic DNA. Translation: BAE77987.1.

PIR

R5EC18. A02803.

RefSeq

AP_004486.1.
NP_417763.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	M	1-117	[»]
1P86	electron microscopy	11.50	M	1-117	[»]
1VS6	X-ray	3.46	O	1-117	[»]
1VS8	X-ray	3.46	O	1-117	[»]
2AW4	X-ray	3.46	O	1-117	[»]
2AWB	X-ray	3.46	O	1-117	[»]
2GYA	electron microscopy	2.00	M	3-115	[»]
2GYC	electron microscopy	2.00	M	3-115	[»]
2I2T	X-ray	3.22	O	1-117	[»]
2I2V	X-ray	3.22	O	1-117	[»]
2J28	electron microscopy	8.00	O	1-117	[»]
2QAM	X-ray	3.21	O	1-117	[»]
2QAO	X-ray	3.21	O	1-117	[»]
2QBA	X-ray	3.54	O	1-117	[»]
2QBC	X-ray	3.54	O	1-117	[»]
2QBE	X-ray	3.30	O	1-117	[»]
2QBG	X-ray	3.30	O	1-117	[»]
2QBI	X-ray	4.00	O	1-117	[»]
2QBK	X-ray	4.00	O	1-117	[»]
2QOV	X-ray	3.93	O	1-117	[»]
2QOX	X-ray	3.93	O	1-117	[»]
2QOZ	X-ray	3.50	O	1-117	[»]
2QP1	X-ray	3.50	O	1-117	[»]
2RDO	electron microscopy	9.10	O	1-117	[»]
2VHM	X-ray	3.74	O	1-117	[»]
2VHN	X-ray	3.74	O	1-117	[»]
2Z4L	X-ray	4.45	O	1-117	[»]
2Z4N	X-ray	4.45	O	1-117	[»]
3BBX	electron microscopy	10.00	O	1-117	[»]
3DF2	X-ray	3.50	O	1-117	[»]
3DF4	X-ray	3.50	O	1-117	[»]
3FIK	electron microscopy	-	O	2-117	[»]

ModBase

Genome annotation databases

GeneID

GenomeReviews

Gene locus JW3266 in contig AP009048_GR.
Gene locus b3304 in contig U00096_GR.

KEGG

ecj:JW3266.
eco:b3304.

Organism-specific databases

EchoBASE

EcoGene

EG10879. rplR.

CMR

Phylogenomic databases

HOGENOM

OMA

P0C018. QVVFDRG.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10879-MON.

Family and domain databases

HAMAP

MF_01337.
[Tree]

InterPro

IPR005484. Ribosomal_L18/L5.
IPR004389. Ribosomal_L18_bac.
[Graphical view]

Pfam

PF00861. Ribosomal_L18p. 1 hit.
[Graphical view]

ProDom

PD001394. Ribosomal_L18p. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00060. L18_bact. 1 hit.

ProtoNet

Entry information

Entry name

RL18_ECOLI

Accession

Primary (citable) accession number: P0C018
Secondary accession number(s): P02419, Q2M6W9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents