P0ADZ0 (RL23_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	100 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (Ref.9) for Ffh binding to the ribosome (SRP54, Ref.10 and Ref.11) and to nascent polypeptide chains (Ref.10). HAMAP-Rule MF_01369
Subunit structure	Part of the 50S ribosomal subunit. Contacts protein L29 and trigger factor. Might also contact SecE and probably does contact SecG and SecY when the SecYEG translocation complex is docked with the ribosome. 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.12

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: HAMAP
Cellular_component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro rRNA binding Inferred from electronic annotation. Source: HAMAP structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 100

100

50S ribosomal protein L23 HAMAP-Rule MF_01369

PRO_0000129407

Experimental info

Mutagenesis

16 – 18

3

VSE → AAA: Strongly reduces trigger factor binding. Ref.9

Mutagenesis

18

1

E → A: Binds normally to ribosomes; strongly reduces trigger factor binding. Ref.9

Mutagenesis

18

1

E → Q: Strongly reduces trigger factor binding. Ref.9

Mutagenesis

51 – 53

3

FEV → AAA: No effect on trigger factor binding. Ref.9

Mutagenesis

52

1

E → K: No effect on trigger factor binding. Ref.9

Sequence conflict

80

1

Missing AA sequence Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

100

Helix Strand Turn

Details...

Helix

4 – 10

7

Beta strand

11 – 14

4

Helix

18 – 25

8

Beta strand

28 – 34

7

Turn

35 – 37

3

Helix

40 – 50

11

Beta strand

57 – 63

7

Beta strand

70 – 73

4

Beta strand

80 – 86

7

Beta strand

88 – 90

3

Sequences

	Sequence		Length	Mass (Da)
	P0ADZ0 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 30CD1D77CC7CF9EB	FASTA	100	11,199
	10 20 30 40 50 60 MIREERLLKV LRAPHVSEKA STAMEKSNTI VLKVAKDATK AEIKAAVQKL FEVEVEVVNT 70 80 90 100 LVVKGKVKRH GQRIGRRSDW KKAYVTLKEG QNLDFVGGAE

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] [Europe PMC] [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] [Europe PMC] [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] [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]	"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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO L29.
[8]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[9]	"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] [Europe PMC] [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.
[10]	"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] [Europe PMC] [Abstract] Cited for: CROSS-LINKS TO FFH (SRP54); TRIGGER FACTOR AND TO NASCENT PROTEIN CHAINS. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[11]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF RIBOSOMAL PROTEIN L23 AS THE DOCKING SITE FOR SIGNAL RECOGNITION PARTICLE. Strain: MRE-600.
[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]	"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.
[14]	"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.
[15]	"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.
[16]	"Cryo-EM structure of the ribosome-SecYE complex in the membrane environment." Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M., Beatrix B., Mielke T., Berninghausen O., Becker T., Schulten K., Beckmann R. Nat. Struct. Mol. Biol. 18:614-621(2011) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH SECYE AND A NASCENT POLYPEPTIDE CHAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_417777.1. NC_000913.2.
YP_492114.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ML5	electron microscopy	14.00	t	2-85	[»]
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	[»]
1VT2	X-ray	3.30	T	1-100	[»]
2AW4	X-ray	3.46	T	1-100	[»]
2AWB	X-ray	3.46	T	1-100	[»]
2GYA	electron microscopy	15.00	R	7-98	[»]
2GYC	electron microscopy	15.00	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	[»]
2VRH	electron microscopy	19.00	B	1-100	[»]
2WWQ	electron microscopy	5.80	T	1-93	[»]
2Z4L	X-ray	4.45	T	1-100	[»]
2Z4N	X-ray	4.45	T	1-100	[»]
3BBX	electron microscopy	10.00	T	1-100	[»]
3E1B	electron microscopy	-	M	1-99	[»]
3E1D	electron microscopy	-	M	1-99	[»]
3FIK	electron microscopy	6.70	T	1-93	[»]
3I1N	X-ray	3.19	T	1-100	[»]
3I1P	X-ray	3.19	T	1-100	[»]
3I1R	X-ray	3.81	T	1-100	[»]
3I1T	X-ray	3.81	T	1-100	[»]
3I20	X-ray	3.71	T	1-100	[»]
3I22	X-ray	3.71	T	1-100	[»]
3IZT	electron microscopy	-	U	1-100	[»]
3IZU	electron microscopy	-	U	1-100	[»]
3J01	electron microscopy	-	T	1-100	[»]
3J0T	electron microscopy	12.10	V	1-100	[»]
3J0W	electron microscopy	14.70	V	1-100	[»]
3J0Y	electron microscopy	13.50	V	1-100	[»]
3J11	electron microscopy	13.10	V	1-100	[»]
3J12	electron microscopy	11.50	V	1-100	[»]
3J14	electron microscopy	11.50	V	1-100	[»]
3J19	electron microscopy	8.30	T	1-93	[»]
3J37	electron microscopy	9.80	X	1-100	[»]
3KCR	electron microscopy	-	T	1-100	[»]
3OAS	X-ray	3.25	T	1-93	[»]
3OAT	X-ray	3.25	T	1-93	[»]
3OFC	X-ray	3.19	T	1-93	[»]
3OFD	X-ray	3.19	T	1-93	[»]
3OFQ	X-ray	3.10	T	1-93	[»]
3OFR	X-ray	3.10	T	1-93	[»]
3OFZ	X-ray	3.29	T	1-93	[»]
3OG0	X-ray	3.29	T	1-93	[»]
3ORB	X-ray	3.30	T	1-100	[»]
3R8S	X-ray	3.00	T	1-93	[»]
3R8T	X-ray	3.00	T	1-93	[»]
3SGF	X-ray	3.20	X	1-100	[»]
3UOS	X-ray	3.70	X	1-100	[»]
4GAR	X-ray	3.30	T	1-100	[»]
4GAU	X-ray	3.30	T	1-100	[»]

ProteinModelPortal

P0ADZ0.

SMR

P0ADZ0. Positions 7-98.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35972N.

IntAct

P0ADZ0. 73 interactions.

MINT

MINT-1225825.

STRING

511145.b3318.

Proteomic databases

PaxDb

P0ADZ0.

PRIDE

P0ADZ0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76343; AAC76343; b3318.
BAE77973; BAE77973; BAE77973.

GeneID

12932296.
947819.

KEGG

ecj:Y75_p3858.
eco:b3318.

PATRIC

32122068. VBIEscCol129921_3411.

Organism-specific databases

EchoBASE

EB0876.

EcoGene

EG10883. rplW.

Phylogenomic databases

eggNOG

COG0089.

HOGENOM

HOG000231364.

KO

K02892.

OMA

HRAAKPD.

ProtClustDB

PRK05738.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10883-MONOMER.
ECOL316407:JW3280-MONOMER.

Gene expression databases

Genevestigator

P0ADZ0.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

HAMAP

MF_01369_B. Ribosomal_L23_B.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001014. Ribosomal_L23/L25_CS.
IPR013025. Ribosomal_L25/23.
[Graphical view]

Pfam

PF00276. Ribosomal_L23. 1 hit.
[Graphical view]

SUPFAM

SSF54189. L23_L15e_core. 1 hit.

PROSITE

PS00050. RIBOSOMAL_L23. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ADZ0.

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:	May 29, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program