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P0A7R1 (RL9_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L9
Gene names
Name:rplI
Ordered Locus Names:b4203, JW4161
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14914950S ribosomal protein L9 HAMAP-Rule MF_00503
PRO_0000176636

Amino acid modifications

Modified residue711N6-succinyllysine Ref.13
Modified residue831N6-succinyllysine Ref.13
Modified residue891N6-acetyllysine Ref.12
Modified residue1121N6-succinyllysine Ref.13

Experimental info

Sequence conflict1061A → AD AA sequence Ref.1
Sequence conflict125 – 1284TGEH → HGE AA sequence Ref.1
Sequence conflict1361Missing AA sequence Ref.1

Secondary structure

......................................... 149
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7R1 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: F8FF527DBB9458CA

FASTA14915,769
        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 

« Hide

References

« Hide '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 277:1453-1462(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, IDENTIFICATION BY 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.
PIRR5EC9. F65231.
RefSeqNP_418624.1. NC_000913.3.
YP_492345.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30F1-149[»]
1P86electron microscopy11.50F1-149[»]
1VS6X-ray3.46H1-149[»]
1VS8X-ray3.46H1-149[»]
1VT2X-ray3.30H1-149[»]
2AW4X-ray3.46H1-149[»]
2AWBX-ray3.46H1-149[»]
2GYAelectron microscopy15.00F1-149[»]
2GYCelectron microscopy15.00F1-149[»]
2I2TX-ray3.22H1-149[»]
2I2VX-ray3.22H1-149[»]
2J28electron microscopy8.00H1-149[»]
2QAMX-ray3.21H1-149[»]
2QAOX-ray3.21H1-149[»]
2QBAX-ray3.54H1-149[»]
2QBCX-ray3.54H1-149[»]
2QBEX-ray3.30H1-149[»]
2QBGX-ray3.30H1-149[»]
2QBIX-ray4.00H1-149[»]
2QBKX-ray4.00H1-149[»]
2QOVX-ray3.93H1-149[»]
2QOXX-ray3.93H1-149[»]
2QOZX-ray3.50H1-149[»]
2QP1X-ray3.50H1-149[»]
2RDOelectron microscopy9.10H1-149[»]
2VHMX-ray3.74H1-149[»]
2VHNX-ray3.74H1-149[»]
2WWQelectron microscopy5.80H1-149[»]
2Z4LX-ray4.45H1-149[»]
2Z4NX-ray4.45H1-149[»]
3BBXelectron microscopy10.00H1-149[»]
3DF2X-ray3.50H1-149[»]
3DF4X-ray3.50H1-149[»]
3E1Belectron microscopy-41-149[»]
3E1Delectron microscopy-41-149[»]
3FIKelectron microscopy6.70H1-149[»]
3I1NX-ray3.19H1-149[»]
3I1PX-ray3.19H1-149[»]
3I1RX-ray3.81H1-149[»]
3I1TX-ray3.81H1-149[»]
3I20X-ray3.71H1-149[»]
3I22X-ray3.71H1-149[»]
3IZTelectron microscopy-I1-149[»]
3IZUelectron microscopy-I1-149[»]
3J01electron microscopy-H1-149[»]
3J0Telectron microscopy12.10I1-149[»]
3J0Welectron microscopy14.70I1-149[»]
3J0Yelectron microscopy13.50I1-149[»]
3J11electron microscopy13.10I1-149[»]
3J12electron microscopy11.50I1-149[»]
3J14electron microscopy11.50I1-149[»]
3J19electron microscopy8.30H1-149[»]
3J37electron microscopy9.80L1-149[»]
3J4Xelectron microscopy12.00H1-149[»]
3J50electron microscopy20.00H1-149[»]
3J51electron microscopy17.00H1-149[»]
3J52electron microscopy12.00H1-149[»]
3J54electron microscopy13.00H1-149[»]
3J56electron microscopy15.00H1-149[»]
3J58electron microscopy17.00H1-149[»]
3J5Aelectron microscopy12.00H1-149[»]
3J5Celectron microscopy17.00H1-149[»]
3J5Eelectron microscopy17.00H1-149[»]
3J5Gelectron microscopy20.00H1-149[»]
3J5Ielectron microscopy15.00H1-149[»]
3J5Kelectron microscopy9.00H1-149[»]
3J5Lelectron microscopy6.60H1-56[»]
3J5Oelectron microscopy6.80H1-50[»]
3J5Uelectron microscopy7.60I1-149[»]
3J5Welectron microscopy7.60I1-149[»]
3KCRelectron microscopy-H1-149[»]
3OASX-ray3.25H1-149[»]
3OATX-ray3.25H1-149[»]
3OFCX-ray3.19H1-149[»]
3OFDX-ray3.19H1-149[»]
3OFQX-ray3.10H1-149[»]
3OFRX-ray3.10H1-149[»]
3OFZX-ray3.29H1-149[»]
3OG0X-ray3.29H1-149[»]
3ORBX-ray3.30H1-149[»]
3R8SX-ray3.00H1-149[»]
3R8TX-ray3.00H1-149[»]
487Delectron microscopy7.50K24-123[»]
4GARX-ray3.30H1-149[»]
4GAUX-ray3.30H1-149[»]
4KIXX-ray2.90H1-50[»]
4KIZX-ray2.90H1-50[»]
4KJ1X-ray2.90H1-50[»]
4KJ3X-ray2.90H1-50[»]
4KJ5X-ray2.90H1-50[»]
4KJ7X-ray2.90H1-50[»]
4KJ9X-ray2.90H1-50[»]
4KJBX-ray2.90H1-50[»]
ProteinModelPortalP0A7R1.
SMRP0A7R1. Positions 1-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35748N.
IntActP0A7R1. 59 interactions.
MINTMINT-1228834.
STRING511145.b4203.

2D gel databases

SWISS-2DPAGEP0A7R1.

Proteomic databases

PaxDbP0A7R1.
PRIDEP0A7R1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77160; AAC77160; b4203.
BAE78204; BAE78204; BAE78204.
GeneID12930641.
948720.
KEGGecj:Y75_p4089.
eco:b4203.
PATRIC32123981. VBIEscCol129921_4335.

Organism-specific databases

EchoBASEEB0863.
EcoGeneEG10870. rplI.

Phylogenomic databases

eggNOGCOG0359.
HOGENOMHOG000040337.
KOK02939.
OMAAKSEVRM.
OrthoDBEOG6D8BH0.
PhylomeDBP0A7R1.

Enzyme and pathway databases

BioCycEcoCyc:EG10870-MONOMER.
ECOL316407:JW4161-MONOMER.

Gene expression databases

GenevestigatorP0A7R1.

Family and domain databases

Gene3D3.10.430.100. 1 hit.
3.40.5.10. 1 hit.
HAMAPMF_00503. Ribosomal_L9.
InterProIPR000244. Ribosomal_L9.
IPR009027. Ribosomal_L9/RNase_H1_N.
IPR020594. Ribosomal_L9_bac/chp.
IPR020069. Ribosomal_L9_C.
IPR020070. Ribosomal_L9_N.
[Graphical view]
PANTHERPTHR21368. PTHR21368. 1 hit.
PfamPF03948. Ribosomal_L9_C. 1 hit.
PF01281. Ribosomal_L9_N. 1 hit.
[Graphical view]
SUPFAMSSF55653. SSF55653. 1 hit.
SSF55658. SSF55658. 1 hit.
TIGRFAMsTIGR00158. L9. 1 hit.
PROSITEPS00651. RIBOSOMAL_L9. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7R1.
PROP0A7R1.

Entry information

Entry nameRL9_ECOLI
AccessionPrimary (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 14, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene