P0A7R1 (RL9_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	149 AA.
Sequence status	Complete.
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-Rule 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.11

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation
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 – 149

149

50S ribosomal protein L9 HAMAP-Rule MF_00503

PRO_0000176636

Amino acid modifications

Modified residue

71

1

N6-succinyllysine Ref.13

Modified residue

83

1

N6-succinyllysine Ref.13

Modified residue

89

1

N6-acetyllysine Ref.12

Modified residue

112

1

N6-succinyllysine Ref.13

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

4 – 7

4

Turn

10 – 12

3

Beta strand

15 – 18

4

Helix

23 – 26

4

Turn

27 – 30

4

Beta strand

31 – 37

7

Helix

42 – 73

32

Beta strand

74 – 76

3

Beta strand

78 – 82

5

Beta strand

88 – 94

7

Helix

96 – 104

9

Beta strand

106 – 108

3

Beta strand

114 – 116

3

Beta strand

118 – 121

4

Beta strand

122 – 132

11

Beta strand

134 – 137

4

Beta strand

142 – 148

7

Sequences

	Sequence		Length	Mass (Da)
	P0A7R1 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT. Strain: K12.
[10]	"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.
[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] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[12]	"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] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[13]	"Identification of lysine succinylation as a new post-translational modification." Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y. Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUCCINYLATION AT LYS-71; LYS-83 AND LYS-112. Strain: K12.
[14]	"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] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[15]	"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.
[16]	"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

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

NP_418624.1. NC_000913.2.
YP_492345.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
1VT2	X-ray	3.30	H	1-149	[»]
2AW4	X-ray	3.46	H	1-149	[»]
2AWB	X-ray	3.46	H	1-149	[»]
2GYA	electron microscopy	15.00	F	1-149	[»]
2GYC	electron microscopy	15.00	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	[»]
2WWQ	electron microscopy	5.80	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	[»]
3E1B	electron microscopy	-	4	1-149	[»]
3E1D	electron microscopy	-	4	1-149	[»]
3FIK	electron microscopy	6.70	H	1-149	[»]
3I1N	X-ray	3.19	H	1-149	[»]
3I1P	X-ray	3.19	H	1-149	[»]
3I1R	X-ray	3.81	H	1-149	[»]
3I1T	X-ray	3.81	H	1-149	[»]
3I20	X-ray	3.71	H	1-149	[»]
3I22	X-ray	3.71	H	1-149	[»]
3IZT	electron microscopy	-	I	1-149	[»]
3IZU	electron microscopy	-	I	1-149	[»]
3J01	electron microscopy	-	H	1-149	[»]
3J0T	electron microscopy	12.10	I	1-149	[»]
3J0W	electron microscopy	14.70	I	1-149	[»]
3J0Y	electron microscopy	13.50	I	1-149	[»]
3J11	electron microscopy	13.10	I	1-149	[»]
3J12	electron microscopy	11.50	I	1-149	[»]
3J14	electron microscopy	11.50	I	1-149	[»]
3J19	electron microscopy	8.30	H	1-149	[»]
3KCR	electron microscopy	-	H	1-149	[»]
3OAS	X-ray	3.25	H	1-149	[»]
3OAT	X-ray	3.25	H	1-149	[»]
3OFC	X-ray	3.19	H	1-149	[»]
3OFD	X-ray	3.19	H	1-149	[»]
3OFQ	X-ray	3.10	H	1-149	[»]
3OFR	X-ray	3.10	H	1-149	[»]
3OFZ	X-ray	3.29	H	1-149	[»]
3OG0	X-ray	3.29	H	1-149	[»]
3ORB	X-ray	3.30	H	1-149	[»]
3R8S	X-ray	3.00	H	1-149	[»]
3R8T	X-ray	3.00	H	1-149	[»]
487D	electron microscopy	7.50	K	24-123	[»]
4GAR	X-ray	3.30	H	1-149	[»]
4GAU	X-ray	3.30	H	1-149	[»]

ProteinModelPortal

P0A7R1.

SMR

P0A7R1. Positions 1-149.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35748N.

IntAct

P0A7R1. 59 interactions.

MINT

MINT-1228834.

STRING

511145.b4203.

2D gel databases

SWISS-2DPAGE

P0A7R1.

Proteomic databases

PaxDb

P0A7R1.

PRIDE

P0A7R1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77160; AAC77160; b4203.
BAE78204; BAE78204; BAE78204.

GeneID

12930641.
948720.

KEGG

ecj:Y75_p4089.
eco:b4203.

PATRIC

32123981. VBIEscCol129921_4335.

Organism-specific databases

EchoBASE

EB0863.

EcoGene

EG10870. rplI.

Phylogenomic databases

eggNOG

COG0359.

HOGENOM

HOG000040337.

KO

K02939.

OMA

TGIYEIE.

ProtClustDB

PRK00137.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10870-MONOMER.
ECOL316407:JW4161-MONOMER.

Gene expression databases

Genevestigator

P0A7R1.

Family and domain databases

Gene3D

3.10.430.100. 1 hit.
3.40.5.10. 1 hit.

HAMAP

MF_00503. Ribosomal_L9.

InterPro

IPR000244. Ribosomal_L9.
IPR009027. Ribosomal_L9/RNase_H1_N.
IPR020594. Ribosomal_L9_bac/chp.
IPR020069. Ribosomal_L9_C.
IPR020070. Ribosomal_L9_N.
[Graphical view]

PANTHER

PTHR21368. PTHR21368. 1 hit.

Pfam

PF03948. Ribosomal_L9_C. 1 hit.
PF01281. Ribosomal_L9_N. 1 hit.
[Graphical view]

SUPFAM

SSF55658. L9_N_like. 1 hit.
SSF55653. Ribosomal_L9. 1 hit.

TIGRFAMs

TIGR00158. L9. 1 hit.

PROSITE

PS00651. RIBOSOMAL_L9. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7R1.

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:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program