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

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P0C018 (RL18_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. History...

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

Documents (4) |

Third-party data

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

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	117 AA.
Sequence status	Complete.
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-Rule MF_01337_B
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-Rule MF_01337_B
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 Reference proteome
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

1 – 117

117

50S ribosomal protein L18 HAMAP-Rule MF_01337_B

PRO_0000131258

Regions

Region

1 – 17

Required for binding of the 5S rRNA/L5/L18 complex to the 23S rRNA HAMAP-Rule MF_01337_B

Secondary structure

117

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0C018 [UniParc].

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

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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [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: CAA25721.1.
U18997 Genomic DNA. Translation: AAA58101.1.
U00096 Genomic DNA. Translation: AAC76329.1.
AP009048 Genomic DNA. Translation: BAE77987.1.

PIR

R5EC18. A02803.

RefSeq

NP_417763.1. NC_000913.2.
YP_492128.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ML5	electron microscopy	14.00	q	2-117	[»]
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	[»]
1VT2	X-ray	3.30	O	1-117	[»]
2AW4	X-ray	3.46	O	1-117	[»]
2AWB	X-ray	3.46	O	1-117	[»]
2GYA	electron microscopy	15.00	M	3-115	[»]
2GYC	electron microscopy	15.00	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	[»]
2WWQ	electron microscopy	5.80	O	2-117	[»]
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	[»]
3E1B	electron microscopy	-	H	1-117	[»]
3E1D	electron microscopy	-	H	1-117	[»]
3FIK	electron microscopy	6.70	O	2-117	[»]
3I1N	X-ray	3.19	O	1-117	[»]
3I1P	X-ray	3.19	O	1-117	[»]
3I1R	X-ray	3.81	O	1-117	[»]
3I1T	X-ray	3.81	O	1-117	[»]
3I20	X-ray	3.71	O	1-117	[»]
3I22	X-ray	3.71	O	1-117	[»]
3IZT	electron microscopy	-	P	1-117	[»]
3IZU	electron microscopy	-	P	1-117	[»]
3J01	electron microscopy	-	O	1-117	[»]
3J0T	electron microscopy	12.10	Q	1-117	[»]
3J0W	electron microscopy	14.70	Q	1-117	[»]
3J0Y	electron microscopy	13.50	Q	1-117	[»]
3J11	electron microscopy	13.10	Q	1-117	[»]
3J12	electron microscopy	11.50	Q	1-117	[»]
3J14	electron microscopy	11.50	Q	1-117	[»]
3J19	electron microscopy	8.30	O	2-117	[»]
3KCR	electron microscopy	-	O	1-117	[»]
3OAS	X-ray	3.25	O	2-117	[»]
3OAT	X-ray	3.25	O	2-117	[»]
3OFC	X-ray	3.19	O	2-117	[»]
3OFD	X-ray	3.19	O	2-117	[»]
3OFQ	X-ray	3.10	O	2-117	[»]
3OFR	X-ray	3.10	O	2-117	[»]
3OFZ	X-ray	3.29	O	2-117	[»]
3OG0	X-ray	3.29	O	2-117	[»]
3ORB	X-ray	3.30	O	1-117	[»]
3R8S	X-ray	3.00	O	2-117	[»]
3R8T	X-ray	3.00	O	2-117	[»]
3SGF	X-ray	3.20	S	1-117	[»]
3UOS	X-ray	3.70	S	1-117	[»]
4GAR	X-ray	3.30	O	1-117	[»]
4GAU	X-ray	3.30	O	1-117	[»]

ProteinModelPortal

P0C018.

SMR

P0C018. Positions 2-117.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47908N.

IntAct

P0C018. 31 interactions.

MINT

MINT-1293631.

STRING

511145.b3304.

Proteomic databases

PaxDb

P0C018.

PRIDE

P0C018.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76329; AAC76329; b3304.
BAE77987; BAE77987; BAE77987.

GeneID

12934402.
947804.

KEGG

ecj:Y75_p3872.
eco:b3304.

PATRIC

32122040. VBIEscCol129921_3397.

Organism-specific databases

EchoBASE

EB0872.

EcoGene

EG10879. rplR.

Phylogenomic databases

eggNOG

COG0256.

HOGENOM

HOG000248742.

K02881.

OMA

GNKYHGR.

ProtClustDB

PRK05593.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10879-MONOMER.
ECOL316407:JW3266-MONOMER.

Gene expression databases

Genevestigator

P0C018.

Family and domain databases

HAMAP

MF_01337_B. Ribosomal_L18_B.

InterPro

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

Pfam

PF00861. Ribosomal_L18p. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00060. L18_bact. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0C018.

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:	May 1, 2013
This is version 82 of the entry and version 1 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

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

Other

Entry information

Relevant documents