50S ribosomal protein L23 - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P0ADZ0 (RL23_ECOLI)

Last modified June 16, 2009. Version 41. History...

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

Documents (4) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

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

Hide | Top

Names and origin

Protein names

Recommended name:
50S ribosomal protein L23

Gene names

Name:	rplW
Ordered Locus Names:	b3318, JW3280

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length	100 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	One of the early assembly protein, it binds 23S rRNA; is essential for growth. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (Ref.8) for Ffh binding to the ribosome (SRP54, Ref.9 and Ref.10) and to nascent polypeptide chains (Ref.9). HAMAP MF_01369
Subunit structure	Part of the 50S ribosomal subunit. Contacts protein L29 and trigger factor. Ref.6
Sequence similarities	Belongs to the ribosomal protein L23P family.
Mass spectrometry	Molecular mass is 11198.0 Da from positions 1 - 100. Determined by MALDI. Ref.11

Hide | Top

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
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	nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct rRNA binding Inferred from electronic annotation. Source: HAMAP structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct
rpsE	P0A7W1	1	EBI-542264,EBI-543949
ybgC	P0A8Z3	1	EBI-542264,EBI-543276
yjgL	P39336	1	EBI-542264,EBI-549937

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 100

100

50S ribosomal protein L23 HAMAP MF_01369

PRO_0000129407

Experimental info

Mutagenesis

16 – 18

VSE → AAA: Strongly reduces trigger factor binding. Ref.8

Mutagenesis

E → A: Binds normally to ribosomes; strongly reduces trigger factor binding. Ref.8

Mutagenesis

E → Q: Strongly reduces trigger factor binding. Ref.8

Mutagenesis

51 – 53

FEV → AAA: No effect on trigger factor binding. Ref.8

Mutagenesis

E → K: No effect on trigger factor binding. Ref.8

Sequence conflict

Missing AA sequence Ref.1

Secondary structure

100

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P0ADZ0-1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 30CD1D77CC7CF9EB
Show »

FASTA

100

11,199

        10         20         30         40         50         60 
MIREERLLKV LRAPHVSEKA STAMEKSNTI VLKVAKDATK AEIKAAVQKL FEVEVEVVNT 

        70         80         90        100 
LVVKGKVKRH GQRIGRRSDW KKAYVTLKEG QNLDFVGGAE

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of protein L23 from the Escherichia coli ribosome." Wittmann-Liebold B., Greuer B. FEBS Lett. 108:69-74(1979) [PubMed: 391594] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: K12.
[2]	"Structure of the Escherichia coli S10 ribosomal protein operon." Zurawski G., Zurawski S.M. Nucleic Acids Res. 13:4521-4526(1985) [PubMed: 3892488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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]	"The use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29." Wower I., Wower J., Meinke M., Brimacombe R. Nucleic Acids Res. 9:4285-4302(1981) [PubMed: 6170935] [Abstract] Cited for: CROSS-LINKING TO 23S RRNA. Strain: MRE-600.
[6]	"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.
[7]	"Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli." Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G. Biochemistry 28:4099-4105(1989) [PubMed: 2665813] [Abstract] Cited for: CROSS-LINKING TO L29.
[8]	"L23 protein functions as a chaperone docking site on the ribosome." Kramer G., Rauch T., Rist W., Vorderwuelbecke S., Patzelt H., Schulze-Specking A., Ban N., Deuerling E., Bukau B. Nature 419:171-174(2002) [PubMed: 12226666] [Abstract] Cited for: BINDING TO TRIGGER FACTOR, MUTAGENESIS OF 16-VAL--GLU-18; GLU-18; 51-PHE--VAL-53 AND GLU-52. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[9]	"Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome." Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J. J. Cell Biol. 161:679-684(2003) [PubMed: 12756233] [Abstract] Cited for: CROSS-LINKS TO FFH (SRP54); TRIGGER FACTOR AND TO NASCENT PROTEIN CHAINS. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[10]	"The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome." Gu S.-Q., Peske F., Wieden H.-J., Rodnina M.V., Wintermeyer W. RNA 9:566-573(2003) [PubMed: 12702815] [Abstract] Cited for: IDENTIFICATION OF RIBOSOMAL PROTEIN L23 AS THE DOCKING SITE FOR SIGNAL RECOGNITION PARTICLE. Strain: MRE-600.
[11]	"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.
[12]	"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.
[13]	"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.

Hide | Top

Cross-references

Sequence databases

X02613 Genomic DNA. Translation: CAA26462.1.
U18997 Genomic DNA. Translation: AAA58115.1.
U00096 Genomic DNA. Translation: AAC76343.1.
AP009048 Genomic DNA. Translation: BAE77973.1.

PIR

R5EC23. A65125.

RefSeq

AP_004472.1.
NP_417777.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	R	1-100	[»]
1P86	electron microscopy	11.50	R	1-100	[»]
1VS6	X-ray	3.46	T	1-100	[»]
1VS8	X-ray	3.46	T	1-100	[»]
2AW4	X-ray	3.46	T	1-100	[»]
2AWB	X-ray	3.46	T	1-100	[»]
2GYA	electron microscopy	2.00	R	7-98	[»]
2GYC	electron microscopy	-	R	7-98	[»]
2I2T	X-ray	3.22	T	1-100	[»]
2I2V	X-ray	3.22	T	1-100	[»]
2J28	electron microscopy	8.00	T	1-99	[»]
2QAM	X-ray	3.21	T	1-100	[»]
2QAO	X-ray	3.21	T	1-100	[»]
2QBA	X-ray	3.54	T	1-100	[»]
2QBC	X-ray	3.54	T	1-100	[»]
2QBE	X-ray	3.30	T	1-100	[»]
2QBG	X-ray	3.30	T	1-100	[»]
2QBI	X-ray	4.00	T	1-100	[»]
2QBK	X-ray	4.00	T	1-100	[»]
2QOV	X-ray	3.93	T	1-100	[»]
2QOX	X-ray	3.93	T	1-100	[»]
2QOZ	X-ray	3.50	T	1-100	[»]
2QP1	X-ray	3.50	T	1-100	[»]
2RDO	electron microscopy	9.10	T	1-100	[»]
2Z4L	X-ray	4.45	T	1-100	[»]
2Z4N	X-ray	4.45	T	1-100	[»]
3BBX	electron microscopy	-	T	1-100	[»]
3FIK	electron microscopy	-	T	1-93	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0ADZ0. 73 interactions.

2-D gel databases

ECO2DBASE

I013.0. 6TH EDITION.

Genome annotation databases

GeneID

947819.

GenomeReviews

Gene locus JW3280 in contig AP009048_GR.
Gene locus b3318 in contig U00096_GR.

KEGG

ecj:JW3280.
eco:b3318.

Organism-specific databases

EchoBASE

EB0876.

EcoGene

EG10883. rplW.

CMR

Search...

Phylogenomic databases

HOGENOM

P0ADZ0.

OMA

P0ADZ0. VSEKATM.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10883-MON.

Family and domain databases

HAMAP

MF_01369.
[Tree]

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR001014. Ribosomal_L23/L25_CS.
IPR013025. Ribosomal_L25/23.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.

Pfam

PF00276. Ribosomal_L23. 1 hit.
[Graphical view]

ProDom

PD001141. Ribosomal_L23. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00050. RIBOSOMAL_L23. 1 hit.
[Graphical view]

ProtoNet

Search...

Hide | Top

Entry information

Entry name

RL23_ECOLI

Accession

Primary (citable) accession number: P0ADZ0
Secondary accession number(s): P02424, Q2M6Y3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	December 6, 2005
Last modified:	June 16, 2009
This is version 41 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)

Hide | Top

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents