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Reviewed, UniProtKB/Swiss-Prot P0A7X3 (RS9_ECOLI)

Last modified June 16, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    30S ribosomal protein S9
Gene names
Name: rpsI
Ordered Locus Names: b3230, JW3199
OrganismEscherichia coli (strain K12) [Complete 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.8

Subunit structure

Part of the 30S ribosomal subunit. Cross-links to the P site tRNA and weakly to the A site tRNA. HAMAP MF_00532

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.9

Binary interactions

With

Entry

#Exp.

IntAct

Notes

frvAP321551EBI-546072,EBI-1133990

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 13012930S ribosomal protein S9 HAMAP MF_00532
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. HAMAP MF_00532
Mutagenesis128 – 1303Missing: Very cold sensitive for growth at 30 degrees Celsius. Almost no P site binding of certain tRNAs in vitro. HAMAP MF_00532
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
P0A7X3-1 [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: 3884974] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 1091515] [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: 7556101] [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: 4346030] [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: 8524654] [Abstract]
Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
Strain: MRE-600.
[8]"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: 15308780] [Abstract]
Cited for: ROLE IN P SITE TRNA BINDING, MUTAGENESIS.
Strain: CSH142.
[9]"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.
[10]"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: 12244297] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[11]"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.
[12]"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

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.
RefSeqAP_003772.1.
NP_417697.1.

3D structure databases

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 microscopy-I5-129[»]
2GYBelectron microscopy-I5-129[»]
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[»]
2Z4KX-ray4.45I2-130[»]
2Z4MX-ray4.45I2-130[»]
3DF1X-ray3.50I2-129[»]
3DF3X-ray3.50I2-129[»]
3FIHelectron microscopy-I4-130[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP0A7X3. 147 interactions.

2-D gel databases

ECO2DBASEI014.6. 6TH EDITION.

Genome annotation databases

GeneID949000.
GenomeReviewsGene locus JW3199 in contig AP009048_GR.
Gene locus b3230 in contig U00096_GR.
KEGGecj:JW3199.
eco:b3230.

Organism-specific databases

EchoBASEEB0901.
EcoGeneEG10908. rpsI.
CMRSearch...

Phylogenomic databases

HOGENOMP0A7X3.
OMAP0A7X3. VYFARPV.

Enzyme and pathway databases

BioCycEcoCyc:EG10908-MON.

Family and domain databases

HAMAPMF_00532.
[Tree]
InterProIPR014721. Ribosomal_S5_D2-type_fold.
IPR000754. Ribosomal_S9.
[Graphical view]
Gene3DG3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
PANTHERPTHR21569. Ribosomal_S9. 1 hit.
PfamPF00380. Ribosomal_S9. 1 hit.
[Graphical view]
ProDomPD001627. Ribosomal_S9. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00360. RIBOSOMAL_S9. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

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

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: June 16, 2009
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents