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Protein

30S ribosomal protein S8

Gene

rpsH

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

Functioni

One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.By similarity
Protein S8 is a translational repressor protein, it controls the translation of the spc operon by binding to its mRNA.

GO - Molecular functioni

  • rRNA binding Source: EcoliWiki
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

  • regulation of mRNA stability Source: EcoliWiki
  • regulation of translation Source: UniProtKB-KW
  • translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10907-MONOMER.
ECOL316407:JW3268-MONOMER.

Protein family/group databases

MoonProtiP0A7W7.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S8
Gene namesi
Name:rpsH
Ordered Locus Names:b3306, JW3268
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10907. rpsH.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: EcoliWiki
Complete GO annotation...

Pathology & Biotechi

Chemistry

DrugBankiDB00759. Tetracycline.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 13012930S ribosomal protein S8PRO_0000126405Add
BLAST

Proteomic databases

PaxDbiP0A7W7.
PRIDEiP0A7W7.

Expressioni

Gene expression databases

GenevestigatoriP0A7W7.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts proteins S5 and S12 (By similarity).By similarity

Protein-protein interaction databases

BioGridi852114. 1 interaction.
DIPiDIP-47901N.
IntActiP0A7W7. 38 interactions.
MINTiMINT-1318565.
STRINGi511145.b3306.

Structurei

Secondary structure

1
130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1914Combined sources
Beta strandi23 – 286Combined sources
Helixi31 – 4212Combined sources
Beta strandi45 – 528Combined sources
Beta strandi54 – 563Combined sources
Beta strandi58 – 636Combined sources
Beta strandi65 – 717Combined sources
Beta strandi75 – 773Combined sources
Helixi89 – 913Combined sources
Beta strandi97 – 993Combined sources
Beta strandi101 – 1066Combined sources
Beta strandi109 – 1124Combined sources
Helixi113 – 1197Combined sources
Beta strandi123 – 1297Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50E1-130[»]
1M5Gmodel-H2-130[»]
1S03X-ray2.70G/H2-130[»]
2YKRelectron microscopy9.80H2-130[»]
4A2Ielectron microscopy16.50H2-130[»]
4ADVelectron microscopy13.50H2-130[»]
4U1UX-ray2.95AH/CH2-130[»]
4U1VX-ray3.00AH/CH2-130[»]
4U20X-ray2.90AH/CH2-130[»]
4U24X-ray2.90AH/CH2-130[»]
4U25X-ray2.90AH/CH2-130[»]
4U26X-ray2.80AH/CH2-130[»]
4U27X-ray2.80AH/CH2-130[»]
4V47electron microscopy12.30BH2-130[»]
4V48electron microscopy11.50BH2-130[»]
4V4HX-ray3.46AH/CH1-130[»]
4V4QX-ray3.46AH/CH2-130[»]
4V4Velectron microscopy15.00AH3-129[»]
4V4Welectron microscopy15.00AH3-129[»]
4V50X-ray3.22AH/CH2-130[»]
4V52X-ray3.21AH/CH2-130[»]
4V53X-ray3.54AH/CH2-130[»]
4V54X-ray3.30AH/CH2-130[»]
4V55X-ray4.00AH/CH2-130[»]
4V56X-ray3.93AH/CH2-130[»]
4V57X-ray3.50AH/CH2-130[»]
4V5BX-ray3.74BH/DH2-130[»]
4V5Helectron microscopy5.80AH2-130[»]
4V5YX-ray4.45AH/CH2-130[»]
4V64X-ray3.50AH/CH2-130[»]
4V65electron microscopy9.00AV1-130[»]
4V66electron microscopy9.00AV1-130[»]
4V69electron microscopy6.70AH2-130[»]
4V6CX-ray3.19AH/CH1-130[»]
4V6DX-ray3.81AH/CH1-130[»]
4V6EX-ray3.71AH/CH1-130[»]
4V6Kelectron microscopy8.25BL1-130[»]
4V6Lelectron microscopy13.20AL1-130[»]
4V6Melectron microscopy7.10AH2-130[»]
4V6Nelectron microscopy12.10BK2-130[»]
4V6Oelectron microscopy14.70AK2-130[»]
4V6Pelectron microscopy13.50AK2-130[»]
4V6Qelectron microscopy11.50AK2-130[»]
4V6Relectron microscopy11.50AK2-130[»]
4V6Selectron microscopy13.10BJ2-130[»]
4V6Telectron microscopy8.30AH2-130[»]
4V6Yelectron microscopy12.00AH1-130[»]
4V6Zelectron microscopy12.00AH1-130[»]
4V70electron microscopy17.00AH1-130[»]
4V71electron microscopy20.00AH1-130[»]
4V72electron microscopy13.00AH1-130[»]
4V73electron microscopy15.00AH1-130[»]
4V74electron microscopy17.00AH1-130[»]
4V75electron microscopy12.00AH1-130[»]
4V76electron microscopy17.00AH1-130[»]
4V77electron microscopy17.00AH1-130[»]
4V78electron microscopy20.00AH1-130[»]
4V79electron microscopy15.00AH1-130[»]
4V7Aelectron microscopy9.00AH1-130[»]
4V7Belectron microscopy6.80AH1-130[»]
4V7Celectron microscopy7.60AH2-130[»]
4V7Delectron microscopy7.60BH2-130[»]
4V7Ielectron microscopy9.60BH1-130[»]
4V7SX-ray3.25AH/CH2-130[»]
4V7TX-ray3.19AH/CH2-130[»]
4V7UX-ray3.10AH/CH2-130[»]
4V7VX-ray3.29AH/CH2-130[»]
4V85X-ray3.20H1-130[»]
4V89X-ray3.70AH1-130[»]
4V9CX-ray3.30AH/CH1-130[»]
4V9DX-ray3.00AH/BH2-130[»]
4V9OX-ray2.90BH/DH/FH/HH1-130[»]
4V9PX-ray2.90BH/DH/FH/HH1-130[»]
4WF1X-ray3.09AH/CH2-130[»]
4WWWX-ray3.10QH/XH2-130[»]
4YBBX-ray2.10AH/BH2-130[»]
5AFIelectron microscopy2.90h1-130[»]
ProteinModelPortaliP0A7W7.
SMRiP0A7W7. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7W7.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S8P family.Curated

Phylogenomic databases

eggNOGiCOG0096.
HOGENOMiHOG000204095.
InParanoidiP0A7W7.
KOiK02994.
OMAiRIYKNTR.
OrthoDBiEOG6Z0QH1.
PhylomeDBiP0A7W7.

Family and domain databases

HAMAPiMF_01302_B. Ribosomal_S8_B.
InterProiIPR000630. Ribosomal_S8.
[Graphical view]
PANTHERiPTHR11758. PTHR11758. 1 hit.
PfamiPF00410. Ribosomal_S8. 1 hit.
[Graphical view]
SUPFAMiSSF56047. SSF56047. 1 hit.
PROSITEiPS00053. RIBOSOMAL_S8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7W7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMQDPIADM LTRIRNGQAA NKAAVTMPSS KLKVAIANVL KEEGFIEDFK
60 70 80 90 100
VEGDTKPELE LTLKYFQGKA VVESIQRVSR PGLRIYKRKD ELPKVMAGLG
110 120 130
IAVVSTSKGV MTDRAARQAG LGGEIICYVA
Length:130
Mass (Da):14,127
Last modified:January 23, 2007 - v2
Checksum:i74641BC5021DA651
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911E → Q in CAA25719 (PubMed:6222285).Curated

Mass spectrometryi

Molecular mass is 13993.2 Da from positions 2 - 130. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25719.1.
U18997 Genomic DNA. Translation: AAA58103.1.
U00096 Genomic DNA. Translation: AAC76331.1.
AP009048 Genomic DNA. Translation: BAE77985.1.
PIRiE65123. R3EC8.
RefSeqiNP_417765.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76331; AAC76331; b3306.
BAE77985; BAE77985; BAE77985.
GeneIDi947802.
KEGGiecj:Y75_p3870.
eco:b3306.
PATRICi32122044. VBIEscCol129921_3399.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25719.1.
U18997 Genomic DNA. Translation: AAA58103.1.
U00096 Genomic DNA. Translation: AAC76331.1.
AP009048 Genomic DNA. Translation: BAE77985.1.
PIRiE65123. R3EC8.
RefSeqiNP_417765.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50E1-130[»]
1M5Gmodel-H2-130[»]
1S03X-ray2.70G/H2-130[»]
2YKRelectron microscopy9.80H2-130[»]
4A2Ielectron microscopy16.50H2-130[»]
4ADVelectron microscopy13.50H2-130[»]
4U1UX-ray2.95AH/CH2-130[»]
4U1VX-ray3.00AH/CH2-130[»]
4U20X-ray2.90AH/CH2-130[»]
4U24X-ray2.90AH/CH2-130[»]
4U25X-ray2.90AH/CH2-130[»]
4U26X-ray2.80AH/CH2-130[»]
4U27X-ray2.80AH/CH2-130[»]
4V47electron microscopy12.30BH2-130[»]
4V48electron microscopy11.50BH2-130[»]
4V4HX-ray3.46AH/CH1-130[»]
4V4QX-ray3.46AH/CH2-130[»]
4V4Velectron microscopy15.00AH3-129[»]
4V4Welectron microscopy15.00AH3-129[»]
4V50X-ray3.22AH/CH2-130[»]
4V52X-ray3.21AH/CH2-130[»]
4V53X-ray3.54AH/CH2-130[»]
4V54X-ray3.30AH/CH2-130[»]
4V55X-ray4.00AH/CH2-130[»]
4V56X-ray3.93AH/CH2-130[»]
4V57X-ray3.50AH/CH2-130[»]
4V5BX-ray3.74BH/DH2-130[»]
4V5Helectron microscopy5.80AH2-130[»]
4V5YX-ray4.45AH/CH2-130[»]
4V64X-ray3.50AH/CH2-130[»]
4V65electron microscopy9.00AV1-130[»]
4V66electron microscopy9.00AV1-130[»]
4V69electron microscopy6.70AH2-130[»]
4V6CX-ray3.19AH/CH1-130[»]
4V6DX-ray3.81AH/CH1-130[»]
4V6EX-ray3.71AH/CH1-130[»]
4V6Kelectron microscopy8.25BL1-130[»]
4V6Lelectron microscopy13.20AL1-130[»]
4V6Melectron microscopy7.10AH2-130[»]
4V6Nelectron microscopy12.10BK2-130[»]
4V6Oelectron microscopy14.70AK2-130[»]
4V6Pelectron microscopy13.50AK2-130[»]
4V6Qelectron microscopy11.50AK2-130[»]
4V6Relectron microscopy11.50AK2-130[»]
4V6Selectron microscopy13.10BJ2-130[»]
4V6Telectron microscopy8.30AH2-130[»]
4V6Yelectron microscopy12.00AH1-130[»]
4V6Zelectron microscopy12.00AH1-130[»]
4V70electron microscopy17.00AH1-130[»]
4V71electron microscopy20.00AH1-130[»]
4V72electron microscopy13.00AH1-130[»]
4V73electron microscopy15.00AH1-130[»]
4V74electron microscopy17.00AH1-130[»]
4V75electron microscopy12.00AH1-130[»]
4V76electron microscopy17.00AH1-130[»]
4V77electron microscopy17.00AH1-130[»]
4V78electron microscopy20.00AH1-130[»]
4V79electron microscopy15.00AH1-130[»]
4V7Aelectron microscopy9.00AH1-130[»]
4V7Belectron microscopy6.80AH1-130[»]
4V7Celectron microscopy7.60AH2-130[»]
4V7Delectron microscopy7.60BH2-130[»]
4V7Ielectron microscopy9.60BH1-130[»]
4V7SX-ray3.25AH/CH2-130[»]
4V7TX-ray3.19AH/CH2-130[»]
4V7UX-ray3.10AH/CH2-130[»]
4V7VX-ray3.29AH/CH2-130[»]
4V85X-ray3.20H1-130[»]
4V89X-ray3.70AH1-130[»]
4V9CX-ray3.30AH/CH1-130[»]
4V9DX-ray3.00AH/BH2-130[»]
4V9OX-ray2.90BH/DH/FH/HH1-130[»]
4V9PX-ray2.90BH/DH/FH/HH1-130[»]
4WF1X-ray3.09AH/CH2-130[»]
4WWWX-ray3.10QH/XH2-130[»]
4YBBX-ray2.10AH/BH2-130[»]
5AFIelectron microscopy2.90h1-130[»]
ProteinModelPortaliP0A7W7.
SMRiP0A7W7. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852114. 1 interaction.
DIPiDIP-47901N.
IntActiP0A7W7. 38 interactions.
MINTiMINT-1318565.
STRINGi511145.b3306.

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB00759. Tetracycline.

Protein family/group databases

MoonProtiP0A7W7.

Proteomic databases

PaxDbiP0A7W7.
PRIDEiP0A7W7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76331; AAC76331; b3306.
BAE77985; BAE77985; BAE77985.
GeneIDi947802.
KEGGiecj:Y75_p3870.
eco:b3306.
PATRICi32122044. VBIEscCol129921_3399.

Organism-specific databases

EchoBASEiEB0900.
EcoGeneiEG10907. rpsH.

Phylogenomic databases

eggNOGiCOG0096.
HOGENOMiHOG000204095.
InParanoidiP0A7W7.
KOiK02994.
OMAiRIYKNTR.
OrthoDBiEOG6Z0QH1.
PhylomeDBiP0A7W7.

Enzyme and pathway databases

BioCyciEcoCyc:EG10907-MONOMER.
ECOL316407:JW3268-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7W7.
PROiP0A7W7.

Gene expression databases

GenevestigatoriP0A7W7.

Family and domain databases

HAMAPiMF_01302_B. Ribosomal_S8_B.
InterProiIPR000630. Ribosomal_S8.
[Graphical view]
PANTHERiPTHR11758. PTHR11758. 1 hit.
PfamiPF00410. Ribosomal_S8. 1 hit.
[Graphical view]
SUPFAMiSSF56047. SSF56047. 1 hit.
PROSITEiPS00053. RIBOSOMAL_S8. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
    Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
    Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The amino acid sequence of the ribosomal protein S8 of Escherichia coli."
    Allen G., Wittmann-Liebold B.
    Hoppe-Seyler's Z. Physiol. Chem. 359:1509-1525(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-130.
    Strain: K.
  5. "Translational regulation by ribosomal protein S8 in Escherichia coli: structural homology between rRNA binding site and feedback target on mRNA."
    Olins P.O., Nomura M.
    Nucleic Acids Res. 9:1757-1764(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: MECHANISM OF TRANSLATION REGULATION.
  6. "Mutagenesis of ribosomal protein S8 from Escherichia coli: defects in regulation of the spc operon."
    Wower I., Kowaleski M.P., Sears L.E., Zimmermann R.A.
    J. Bacteriol. 174:1213-1221(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS8_ECOLI
AccessioniPrimary (citable) accession number: P0A7W7
Secondary accession number(s): P02361, Q2M6X1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 100 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.