Reviewed, UniProtKB/Swiss-Prot P0A7R1 (RL9_ECOLI)

Names and origin

Protein names

Recommended name:
    50S ribosomal protein L9

Gene names

Name:	rplI
Ordered Locus Names:	b4203, JW4161

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	149 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	One of the primary rRNA binding proteins, it binds very close to the 3' end of the 23S rRNA. HAMAP MF_00503
Subunit structure	Part of the 50S ribosomal subunit. Ref.9
Sequence similarities	Belongs to the ribosomal protein L9P family.
Mass spectrometry	Molecular mass is 15769.7 Da from positions 1 - 149. Determined by MALDI. Ref.10

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation
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

1 – 149

149

50S ribosomal protein L9 HAMAP MF_00503

PRO_0000176636

Amino acid modifications

Modified residue

89

1

N6-acetyllysine Ref.11

Experimental info

Sequence conflict

106

1

A → AD AA sequence Ref.1

Sequence conflict

125 – 128

4

TGEH → HGE AA sequence Ref.1

Sequence conflict

136

1

Missing AA sequence Ref.1

Secondary structure

1

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149

Helix Strand Turn

Details...

Beta strand

10 – 12

3

Beta strand

23 – 25

3

Helix

26 – 34

9

Helix

42 – 45

4

Helix

48 – 51

4

Turn

52 – 54

3

Helix

56 – 58

3

Helix

60 – 63

4

Helix

68 – 71

4

Beta strand

72 – 74

3

Turn

86 – 88

3

Helix

97 – 100

4

Turn

101 – 103

3

Beta strand

105 – 107

3

Beta strand

128 – 132

5

Beta strand

142 – 144

3

Sequences

	Sequence		Length	Mass (Da)
	P0A7R1-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: F8FF527DBB9458CA	FASTA	149	15,769
	10 20 30 40 50 60 MQVILLDKVA NLGSLGDQVN VKAGYARNFL VPQGKAVPAT KKNIEFFEAR RAELEAKLAE 70 80 90 100 110 120 VLAAANARAE KINALETVTI ASKAGDEGKL FGSIGTRDIA DAVTAAGVEV AKSEVRLPNG 130 140 VLRTTGEHEV SFQVHSEVFA KVIVNVVAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of protein L9 from the Escherichia coli ribosome." Kamp R.M., Wittmann-Liebold B. FEBS Lett. 149:313-319(1982) Cited for: PROTEIN SEQUENCE.
[2]	"The nucleotide sequence of an Escherichia coli chromosomal region containing the genes for ribosomal proteins S6, S18, L9 and an open reading frame." Schnier J., Kitakawa M., Isono K. Mol. Gen. Genet. 204:126-132(1986) [PubMed: 3528756] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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.
[5]	"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.
[6]	Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. Submitted (SEP-1994) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-13. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[8]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed: 9600841] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]	"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.
[10]	"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.
[11]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89, MASS SPECTROMETRY.
[12]	"The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 A resolution." Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J., Goerlach M., van Heel M., Brimacombe R. J. Mol. Biol. 298:35-59(2000) [PubMed: 10756104] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[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

EMBLGenBankDDBJ

X04022 Genomic DNA. Translation: CAA27655.1.
U14003 Genomic DNA. Translation: AAA97099.1.
U00096 Genomic DNA. Translation: AAC77160.1.
AP009048 Genomic DNA. Translation: BAE78204.1.

PIR

R5EC9. F65231.

RefSeq

AP_004703.1.
NP_418624.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	F	1-149	[»]
1P86	electron microscopy	11.50	F	1-149	[»]
1VS6	X-ray	3.46	H	1-149	[»]
1VS8	X-ray	3.46	H	1-149	[»]
2AW4	X-ray	3.46	H	1-149	[»]
2AWB	X-ray	3.46	H	1-149	[»]
2GYA	electron microscopy	2.00	F	1-149	[»]
2GYC	electron microscopy	2.00	F	1-149	[»]
2I2T	X-ray	3.22	H	1-149	[»]
2I2V	X-ray	3.22	H	1-149	[»]
2J28	electron microscopy	8.00	H	1-149	[»]
2QAM	X-ray	3.21	H	1-149	[»]
2QAO	X-ray	3.21	H	1-149	[»]
2QBA	X-ray	3.54	H	1-149	[»]
2QBC	X-ray	3.54	H	1-149	[»]
2QBE	X-ray	3.30	H	1-149	[»]
2QBG	X-ray	3.30	H	1-149	[»]
2QBI	X-ray	4.00	H	1-149	[»]
2QBK	X-ray	4.00	H	1-149	[»]
2QOV	X-ray	3.93	H	1-149	[»]
2QOX	X-ray	3.93	H	1-149	[»]
2QOZ	X-ray	3.50	H	1-149	[»]
2QP1	X-ray	3.50	H	1-149	[»]
2RDO	electron microscopy	9.10	H	1-149	[»]
2VHM	X-ray	3.74	H	1-149	[»]
2VHN	X-ray	3.74	H	1-149	[»]
2Z4L	X-ray	4.45	H	1-149	[»]
2Z4N	X-ray	4.45	H	1-149	[»]
3BBX	electron microscopy	10.00	H	1-149	[»]
3DF2	X-ray	3.50	H	1-149	[»]
3DF4	X-ray	3.50	H	1-149	[»]
3FIK	electron microscopy	-	H	1-149	[»]
487D	electron microscopy	7.50	K	24-123	[»]

ModBase

Search...

2-D gel databases

SWISS-2DPAGE

P0A7R1.

ECO2DBASE

H014.0. 6TH EDITION.

Genome annotation databases

GeneID

948720.

GenomeReviews

Gene locus JW4161 in contig AP009048_GR.
Gene locus b4203 in contig U00096_GR.

KEGG

ecj:JW4161.
eco:b4203.

Organism-specific databases

EchoBASE

EB0863.

EcoGene

EG10870. rplI.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A7R1.

OMA

P0A7R1. EKVVNLG.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10870-MON.

Family and domain databases

HAMAP

MF_00503.
[Tree]

InterPro

IPR000244. Ribosomal_L9.
[Graphical view]

PANTHER

PTHR21368. Ribosomal_L9. 1 hit.

TIGRFAMs

TIGR00158. L9. 1 hit.

PROSITE

PS00651. RIBOSOMAL_L9. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RL9_ECOLI

Accession

Primary (citable) accession number: P0A7R1
Secondary accession number(s): P02418, Q2M6A2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1988
Last modified:	June 16, 2009
This is version 51 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)