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P0A7X3 (RS9_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 95. 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:
30S ribosomal protein S9
Gene names
Name:rpsI
Ordered Locus Names:b3230, JW3199
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length130 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. Mutations that decrease this affinity are suppressed in the 70S ribosome. Ref.9

Subunit structure

Part of the 30S ribosomal subunit. Cross-links to the P site tRNA and weakly to the A site tRNA.

Sequence similarities

Belongs to the ribosomal protein S9P family.

Mass spectrometry

Molecular mass is 14723.3 Da from positions 2 - 130. Determined by MALDI. Ref.10

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 13012930S ribosomal protein S9 HAMAP-Rule MF_00532_B
PRO_0000111354

Experimental info

Mutagenesis105 – 13026Missing: Cold sensitive for growth at 30 degrees Celsius. 350-fold reduced affinity of the 30S subunit P site for certain tRNAs in vitro.
Mutagenesis128 – 1303Missing: Very cold sensitive for growth at 30 degrees Celsius. Almost no P site binding of certain tRNAs in vitro.
Sequence conflict561D → N AA sequence Ref.4
Sequence conflict1241Missing AA sequence Ref.4
Sequence conflict1261Q → E AA sequence Ref.4

Secondary structure

............................ 130
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7X3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 757D599168812806

FASTA13014,856
        10         20         30         40         50         60 
MAENQYYGTG RRKSSAARVF IKPGNGKIVI NQRSLEQYFG RETARMVVRQ PLELVDMVEK 

        70         80         90        100        110        120 
LDLYITVKGG GISGQAGAIR HGITRALMEY DESLRSELRK AGFVTRDARQ VERKKVGLRK 

       130 
ARRRPQFSKR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequencing of the genes for ribosomal proteins S9 (rpsI) and L13 (rplM) of Escherichia coli."
Isono S., Thamm S., Kitakawa M., Isono K.
Mol. Gen. Genet. 198:279-282(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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.
[3]"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.
[4]"The primary structure of protein S9 from the 30S subunit of Escherichia coli ribosomes."
Chen R., Wittmann-Liebold B.
FEBS Lett. 52:139-140(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-130.
Strain: K.
[5]"Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 121-130, CROSS-LINKING TO RRNA.
Strain: MRE-600.
[6]"Requirement of proteins S5 and S9 from 30S subunits for the ribosome-dependent GTPase activity of elongation factor G."
Marsh R.C., Parmeggiani A.
Proc. Natl. Acad. Sci. U.S.A. 70:151-155(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FORMATION OF THE EF-G/RIBOSOME COMPLEX.
Strain: B/2.
[7]"The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
Osswald M., Doering T., Brimacombe R.
Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
Strain: MRE-600.
[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]"Creating ribosomes with an all-RNA 30S subunit P site."
Hoang L., Fredrick K., Noller H.F.
Proc. Natl. Acad. Sci. U.S.A. 101:12439-12443(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN P SITE TRNA-BINDING, MUTAGENESIS.
Strain: CSH142.
[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] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[11]"All-atom homology model of the Escherichia coli 30S ribosomal subunit."
Tung C.-S., Joseph S., Sanbonmatsu K.Y.
Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[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] [Europe PMC] [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] [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
X02130 Genomic DNA. Translation: CAA26042.1.
U18997 Genomic DNA. Translation: AAA58032.1.
U00096 Genomic DNA. Translation: AAC76262.1.
AP009048 Genomic DNA. Translation: BAE77273.1.
PIRR3EC9. H65114.
RefSeqNP_417697.1. NC_000913.3.
YP_491414.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-I4-130[»]
1P6Gelectron microscopy12.30I2-130[»]
1P87electron microscopy11.50I2-130[»]
1VS5X-ray3.46I1-130[»]
1VS7X-ray3.46I1-130[»]
2AVYX-ray3.46I2-130[»]
2AW7X-ray3.46I2-130[»]
2GY9electron microscopy15.00I5-129[»]
2GYBelectron microscopy15.00I5-129[»]
2I2PX-ray3.22I2-129[»]
2I2UX-ray3.22I2-129[»]
2QALX-ray3.21I2-130[»]
2QANX-ray3.21I2-130[»]
2QB9X-ray3.54I2-130[»]
2QBBX-ray3.54I2-130[»]
2QBDX-ray3.30I2-130[»]
2QBFX-ray3.30I2-130[»]
2QBHX-ray4.00I2-130[»]
2QBJX-ray4.00I2-130[»]
2QOUX-ray3.93I2-130[»]
2QOWX-ray3.93I2-130[»]
2QOYX-ray3.50I2-130[»]
2QP0X-ray3.50I2-130[»]
2VHOX-ray3.74I2-130[»]
2VHPX-ray3.74I2-130[»]
2WWLelectron microscopy5.80I4-130[»]
2YKRelectron microscopy9.80I4-130[»]
2Z4KX-ray4.45I2-130[»]
2Z4MX-ray4.45I2-130[»]
3DF1X-ray3.50I2-129[»]
3DF3X-ray3.50I2-129[»]
3E1Aelectron microscopy-W1-130[»]
3E1Celectron microscopy-W1-130[»]
3FIHelectron microscopy6.70I4-130[»]
3I1MX-ray3.19I1-130[»]
3I1OX-ray3.19I1-130[»]
3I1QX-ray3.81I1-130[»]
3I1SX-ray3.81I1-130[»]
3I1ZX-ray3.71I1-130[»]
3I21X-ray3.71I1-130[»]
3IZVelectron microscopy-M1-130[»]
3IZWelectron microscopy-M1-130[»]
3J00electron microscopy-I2-130[»]
3J0Uelectron microscopy12.10L2-130[»]
3J0Velectron microscopy14.70L2-130[»]
3J0Xelectron microscopy13.50L2-130[»]
3J0Zelectron microscopy11.50L2-130[»]
3J10electron microscopy11.50L2-130[»]
3J13electron microscopy13.10K2-130[»]
3J18electron microscopy8.30I4-130[»]
3J36electron microscopy9.80I2-130[»]
3J4Velectron microscopy12.00I4-130[»]
3J4Welectron microscopy12.00I4-130[»]
3J4Yelectron microscopy17.00I4-130[»]
3J4Zelectron microscopy20.00I4-130[»]
3J53electron microscopy13.00I4-130[»]
3J55electron microscopy15.00I4-130[»]
3J57electron microscopy17.00I4-130[»]
3J59electron microscopy12.00I4-130[»]
3J5Belectron microscopy17.00I4-130[»]
3J5Delectron microscopy17.00I4-130[»]
3J5Felectron microscopy20.00I4-130[»]
3J5Helectron microscopy15.00I4-130[»]
3J5Jelectron microscopy9.00I4-130[»]
3J5Nelectron microscopy6.80I1-130[»]
3J5Telectron microscopy7.60I2-130[»]
3J5Xelectron microscopy7.60I2-130[»]
3KC4electron microscopy-I1-130[»]
3OAQX-ray3.25I4-130[»]
3OARX-ray3.25I4-130[»]
3OFAX-ray3.19I4-130[»]
3OFBX-ray3.19I4-130[»]
3OFOX-ray3.10I4-130[»]
3OFPX-ray3.10I4-130[»]
3OFXX-ray3.29I4-130[»]
3OFYX-ray3.29I4-130[»]
3OR9X-ray3.30I1-130[»]
3ORAX-ray3.30I1-130[»]
3SFSX-ray3.20I1-130[»]
3UOQX-ray3.70I1-130[»]
4A2Ielectron microscopy16.50I4-130[»]
4ADVelectron microscopy13.50I2-130[»]
4GAQX-ray3.30I1-130[»]
4GASX-ray3.30I1-130[»]
4GD1X-ray3.00I4-130[»]
4GD2X-ray3.00I4-130[»]
4KIYX-ray2.90I1-130[»]
4KJ0X-ray2.90I1-130[»]
4KJ2X-ray2.90I1-130[»]
4KJ4X-ray2.90I1-130[»]
4KJ6X-ray2.90I1-130[»]
4KJ8X-ray2.90I1-130[»]
4KJAX-ray2.90I1-130[»]
4KJCX-ray2.90I1-130[»]
ProteinModelPortalP0A7X3.
SMRP0A7X3. Positions 4-130.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35799N.
IntActP0A7X3. 147 interactions.
MINTMINT-1290939.
STRING511145.b3230.

Chemistry

ChEMBLCHEMBL2363135.
DrugBankDB00453. Clomocycline.
DB00618. Demeclocycline.
DB00254. Doxycycline.
DB00256. Lymecycline.
DB01017. Minocycline.
DB00595. Oxytetracycline.
DB00759. Tetracycline.
DB00560. Tigecycline.

Proteomic databases

PaxDbP0A7X3.
PRIDEP0A7X3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76262; AAC76262; b3230.
BAE77273; BAE77273; BAE77273.
GeneID12933452.
949000.
KEGGecj:Y75_p3150.
eco:b3230.
PATRIC32121886. VBIEscCol129921_3327.

Organism-specific databases

EchoBASEEB0901.
EcoGeneEG10908. rpsI.

Phylogenomic databases

eggNOGCOG0103.
HOGENOMHOG000019802.
KOK02996.
OMAIKQGAAR.
OrthoDBEOG6MWNH0.
ProtClustDBPRK00132.

Enzyme and pathway databases

BioCycEcoCyc:EG10908-MONOMER.
ECOL316407:JW3199-MONOMER.

Gene expression databases

GenevestigatorP0A7X3.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
HAMAPMF_00532_B. Ribosomal_S9_B.
InterProIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000754. Ribosomal_S9.
IPR023035. Ribosomal_S9_bac/plastid.
IPR020574. Ribosomal_S9_CS.
[Graphical view]
PANTHERPTHR21569. PTHR21569. 1 hit.
PfamPF00380. Ribosomal_S9. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
PROSITEPS00360. RIBOSOMAL_S9. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7X3.
PROP0A7X3.

Entry information

Entry nameRS9_ECOLI
AccessionPrimary (citable) accession number: P0A7X3
Secondary accession number(s): P02363, Q2M8Y3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 95 of the entry and version 2 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