Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

30S ribosomal protein S9

Gene

rpsI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. structural constituent of ribosome Source: InterPro
  2. tRNA binding Source: UniProtKB-KW

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10908-MONOMER.
ECOL316407:JW3199-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S9
Gene namesi
Name:rpsI
Ordered Locus Names:b3230, JW3199
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10908. rpsI.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 13026Missing : Cold sensitive for growth at 30 degrees Celsius. 350-fold reduced affinity of the 30S subunit P site for certain tRNAs in vitro. 1 PublicationAdd
BLAST
Mutagenesisi128 – 1303Missing : Very cold sensitive for growth at 30 degrees Celsius. Almost no P site binding of certain tRNAs in vitro. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 13012930S ribosomal protein S9PRO_0000111354Add
BLAST

Proteomic databases

PaxDbiP0A7X3.
PRIDEiP0A7X3.

Expressioni

Gene expression databases

GenevestigatoriP0A7X3.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-35799N.
IntActiP0A7X3. 148 interactions.
MINTiMINT-1290939.
STRINGi511145.b3230.

Structurei

Secondary structure

1
130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Beta strandi11 – 144Combined sources
Beta strandi15 – 2410Combined sources
Beta strandi28 – 303Combined sources
Helixi35 – 395Combined sources
Beta strandi40 – 423Combined sources
Helixi45 – 495Combined sources
Beta strandi52 – 554Combined sources
Beta strandi58 – 7013Combined sources
Helixi72 – 8615Combined sources
Helixi87 – 904Combined sources
Beta strandi92 – 965Combined sources
Helixi97 – 1015Combined sources
Turni102 – 1043Combined sources
Beta strandi118 – 1203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-I4-130[»]
2YKRelectron microscopy9.80I4-130[»]
4A2Ielectron microscopy16.50I4-130[»]
4ADVelectron microscopy13.50I2-130[»]
4U1UX-ray2.95AI/CI4-130[»]
4U1VX-ray3.00AI/CI4-130[»]
4U20X-ray2.90AI/CI4-130[»]
4U24X-ray2.90AI/CI4-130[»]
4U25X-ray2.90AI/CI4-130[»]
4U26X-ray2.80AI/CI4-130[»]
4U27X-ray2.80AI/CI4-130[»]
4V47electron microscopy12.30BI2-130[»]
4V48electron microscopy11.50BI2-130[»]
4V4HX-ray3.46AI/CI1-130[»]
4V4QX-ray3.46AI/CI2-130[»]
4V4Velectron microscopy15.00AI5-130[»]
4V4Welectron microscopy15.00AI5-130[»]
4V50X-ray3.22AI/CI2-130[»]
4V52X-ray3.21AI/CI2-130[»]
4V53X-ray3.54AI/CI2-130[»]
4V54X-ray3.30AI/CI2-130[»]
4V55X-ray4.00AI/CI2-130[»]
4V56X-ray3.93AI/CI2-130[»]
4V57X-ray3.50AI/CI2-130[»]
4V5BX-ray3.74BI/DI2-130[»]
4V5Helectron microscopy5.80AI4-130[»]
4V5YX-ray4.45AI/CI2-130[»]
4V64X-ray3.50AI/CI2-130[»]
4V65electron microscopy9.00AW1-130[»]
4V66electron microscopy9.00AW1-130[»]
4V69electron microscopy6.70AI4-130[»]
4V6CX-ray3.19AI/CI1-130[»]
4V6DX-ray3.81AI/CI1-130[»]
4V6EX-ray3.71AI/CI1-130[»]
4V6Kelectron microscopy8.25BM1-130[»]
4V6Lelectron microscopy13.20AM1-130[»]
4V6Melectron microscopy7.10AI2-130[»]
4V6Nelectron microscopy12.10BL2-130[»]
4V6Oelectron microscopy14.70AL2-130[»]
4V6Pelectron microscopy13.50AL2-130[»]
4V6Qelectron microscopy11.50AL2-130[»]
4V6Relectron microscopy11.50AL2-130[»]
4V6Selectron microscopy13.10BK2-130[»]
4V6Telectron microscopy8.30AI4-130[»]
4V6Velectron microscopy9.80I2-130[»]
4V6Yelectron microscopy12.00AI4-130[»]
4V6Zelectron microscopy12.00AI4-130[»]
4V70electron microscopy17.00AI4-130[»]
4V71electron microscopy20.00AI4-130[»]
4V72electron microscopy13.00AI4-130[»]
4V73electron microscopy15.00AI4-130[»]
4V74electron microscopy17.00AI4-130[»]
4V75electron microscopy12.00AI4-130[»]
4V76electron microscopy17.00AI4-130[»]
4V77electron microscopy17.00AI4-130[»]
4V78electron microscopy20.00AI4-130[»]
4V79electron microscopy15.00AI4-130[»]
4V7Aelectron microscopy9.00AI4-130[»]
4V7Belectron microscopy6.80AI1-130[»]
4V7Celectron microscopy7.60AI2-130[»]
4V7Delectron microscopy7.60BI2-130[»]
4V7Ielectron microscopy9.60BI1-130[»]
4V7SX-ray3.25AI/CI4-130[»]
4V7TX-ray3.19AI/CI4-130[»]
4V7UX-ray3.10AI/CI4-130[»]
4V7VX-ray3.29AI/CI4-130[»]
4V85X-ray3.20I1-130[»]
4V89X-ray3.70AI1-130[»]
4V9CX-ray3.30AI/CI1-130[»]
4V9DX-ray3.00AI/BI4-130[»]
4V9OX-ray2.90BI/DI/FI/HI1-130[»]
4V9PX-ray2.90BI/DI/FI/HI1-130[»]
4WF1X-ray3.09AI/CI4-130[»]
4WWWX-ray3.10QI/XI4-130[»]
ProteinModelPortaliP0A7X3.
SMRiP0A7X3. Positions 4-130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7X3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S9P family.Curated

Phylogenomic databases

eggNOGiCOG0103.
HOGENOMiHOG000019802.
InParanoidiP0A7X3.
KOiK02996.
OMAiIKQGAAR.
OrthoDBiEOG6MWNH0.
PhylomeDBiP0A7X3.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00532_B. Ribosomal_S9_B.
InterProiIPR020568. 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]
PANTHERiPTHR21569. PTHR21569. 1 hit.
PfamiPF00380. Ribosomal_S9. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7X3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENQYYGTG RRKSSAARVF IKPGNGKIVI NQRSLEQYFG RETARMVVRQ
60 70 80 90 100
PLELVDMVEK LDLYITVKGG GISGQAGAIR HGITRALMEY DESLRSELRK
110 120 130
AGFVTRDARQ VERKKVGLRK ARRRPQFSKR
Length:130
Mass (Da):14,856
Last modified:January 22, 2007 - v2
Checksum:i757D599168812806
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561D → N AA sequence (PubMed:1091515).Curated
Sequence conflicti124 – 1241Missing AA sequence (PubMed:1091515).Curated
Sequence conflicti126 – 1261Q → E AA sequence (PubMed:1091515).Curated

Mass spectrometryi

Molecular mass is 14723.3 Da from positions 2 - 130. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02130 Genomic DNA. Translation: CAA26042.1.
U18997 Genomic DNA. Translation: AAA58032.1.
U00096 Genomic DNA. Translation: AAC76262.1.
AP009048 Genomic DNA. Translation: BAE77273.1.
PIRiH65114. R3EC9.
RefSeqiNP_417697.1. NC_000913.3.
YP_491414.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76262; AAC76262; b3230.
BAE77273; BAE77273; BAE77273.
GeneIDi12933452.
949000.
KEGGiecj:Y75_p3150.
eco:b3230.
PATRICi32121886. VBIEscCol129921_3327.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02130 Genomic DNA. Translation: CAA26042.1.
U18997 Genomic DNA. Translation: AAA58032.1.
U00096 Genomic DNA. Translation: AAC76262.1.
AP009048 Genomic DNA. Translation: BAE77273.1.
PIRiH65114. R3EC9.
RefSeqiNP_417697.1. NC_000913.3.
YP_491414.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-I4-130[»]
2YKRelectron microscopy9.80I4-130[»]
4A2Ielectron microscopy16.50I4-130[»]
4ADVelectron microscopy13.50I2-130[»]
4U1UX-ray2.95AI/CI4-130[»]
4U1VX-ray3.00AI/CI4-130[»]
4U20X-ray2.90AI/CI4-130[»]
4U24X-ray2.90AI/CI4-130[»]
4U25X-ray2.90AI/CI4-130[»]
4U26X-ray2.80AI/CI4-130[»]
4U27X-ray2.80AI/CI4-130[»]
4V47electron microscopy12.30BI2-130[»]
4V48electron microscopy11.50BI2-130[»]
4V4HX-ray3.46AI/CI1-130[»]
4V4QX-ray3.46AI/CI2-130[»]
4V4Velectron microscopy15.00AI5-130[»]
4V4Welectron microscopy15.00AI5-130[»]
4V50X-ray3.22AI/CI2-130[»]
4V52X-ray3.21AI/CI2-130[»]
4V53X-ray3.54AI/CI2-130[»]
4V54X-ray3.30AI/CI2-130[»]
4V55X-ray4.00AI/CI2-130[»]
4V56X-ray3.93AI/CI2-130[»]
4V57X-ray3.50AI/CI2-130[»]
4V5BX-ray3.74BI/DI2-130[»]
4V5Helectron microscopy5.80AI4-130[»]
4V5YX-ray4.45AI/CI2-130[»]
4V64X-ray3.50AI/CI2-130[»]
4V65electron microscopy9.00AW1-130[»]
4V66electron microscopy9.00AW1-130[»]
4V69electron microscopy6.70AI4-130[»]
4V6CX-ray3.19AI/CI1-130[»]
4V6DX-ray3.81AI/CI1-130[»]
4V6EX-ray3.71AI/CI1-130[»]
4V6Kelectron microscopy8.25BM1-130[»]
4V6Lelectron microscopy13.20AM1-130[»]
4V6Melectron microscopy7.10AI2-130[»]
4V6Nelectron microscopy12.10BL2-130[»]
4V6Oelectron microscopy14.70AL2-130[»]
4V6Pelectron microscopy13.50AL2-130[»]
4V6Qelectron microscopy11.50AL2-130[»]
4V6Relectron microscopy11.50AL2-130[»]
4V6Selectron microscopy13.10BK2-130[»]
4V6Telectron microscopy8.30AI4-130[»]
4V6Velectron microscopy9.80I2-130[»]
4V6Yelectron microscopy12.00AI4-130[»]
4V6Zelectron microscopy12.00AI4-130[»]
4V70electron microscopy17.00AI4-130[»]
4V71electron microscopy20.00AI4-130[»]
4V72electron microscopy13.00AI4-130[»]
4V73electron microscopy15.00AI4-130[»]
4V74electron microscopy17.00AI4-130[»]
4V75electron microscopy12.00AI4-130[»]
4V76electron microscopy17.00AI4-130[»]
4V77electron microscopy17.00AI4-130[»]
4V78electron microscopy20.00AI4-130[»]
4V79electron microscopy15.00AI4-130[»]
4V7Aelectron microscopy9.00AI4-130[»]
4V7Belectron microscopy6.80AI1-130[»]
4V7Celectron microscopy7.60AI2-130[»]
4V7Delectron microscopy7.60BI2-130[»]
4V7Ielectron microscopy9.60BI1-130[»]
4V7SX-ray3.25AI/CI4-130[»]
4V7TX-ray3.19AI/CI4-130[»]
4V7UX-ray3.10AI/CI4-130[»]
4V7VX-ray3.29AI/CI4-130[»]
4V85X-ray3.20I1-130[»]
4V89X-ray3.70AI1-130[»]
4V9CX-ray3.30AI/CI1-130[»]
4V9DX-ray3.00AI/BI4-130[»]
4V9OX-ray2.90BI/DI/FI/HI1-130[»]
4V9PX-ray2.90BI/DI/FI/HI1-130[»]
4WF1X-ray3.09AI/CI4-130[»]
4WWWX-ray3.10QI/XI4-130[»]
ProteinModelPortaliP0A7X3.
SMRiP0A7X3. Positions 4-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35799N.
IntActiP0A7X3. 148 interactions.
MINTiMINT-1290939.
STRINGi511145.b3230.

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB00453. Clomocycline.
DB00618. Demeclocycline.
DB00254. Doxycycline.
DB00256. Lymecycline.
DB01017. Minocycline.
DB00595. Oxytetracycline.
DB01301. Rolitetracycline.
DB00560. Tigecycline.

Proteomic databases

PaxDbiP0A7X3.
PRIDEiP0A7X3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76262; AAC76262; b3230.
BAE77273; BAE77273; BAE77273.
GeneIDi12933452.
949000.
KEGGiecj:Y75_p3150.
eco:b3230.
PATRICi32121886. VBIEscCol129921_3327.

Organism-specific databases

EchoBASEiEB0901.
EcoGeneiEG10908. rpsI.

Phylogenomic databases

eggNOGiCOG0103.
HOGENOMiHOG000019802.
InParanoidiP0A7X3.
KOiK02996.
OMAiIKQGAAR.
OrthoDBiEOG6MWNH0.
PhylomeDBiP0A7X3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10908-MONOMER.
ECOL316407:JW3199-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7X3.
PROiP0A7X3.

Gene expression databases

GenevestigatoriP0A7X3.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00532_B. Ribosomal_S9_B.
InterProiIPR020568. 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]
PANTHERiPTHR21569. PTHR21569. 1 hit.
PfamiPF00380. Ribosomal_S9. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. 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(2005) [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(1974) [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(1994) [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(1972) [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(1994) [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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. 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(1998) [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(2001) [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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
    Strain: MRE-600.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS9_ECOLI
AccessioniPrimary (citable) accession number: P0A7X3
Secondary accession number(s): P02363, Q2M8Y3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.