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P0A7W7

- RS8_ECOLI

UniProt

P0A7W7 - RS8_ECOLI

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Protein
30S ribosomal protein S8
Gene
rpsH, b3306, JW3268
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.UniRule annotation
Protein S8 is a translational repressor protein, it controls the translation of the spc operon by binding to its mRNA.UniRule annotation

GO - Molecular functioni

  1. rRNA binding Source: EcoliWiki
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. regulation of mRNA stability Source: EcoliWiki
  2. regulation of translation Source: UniProtKB-KW
  3. translation Source: InterPro
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.

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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10907. rpsH.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 13012930S ribosomal protein S8UniRule annotation
PRO_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.

Protein-protein interaction databases

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

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1914
Beta strandi23 – 286
Helixi31 – 4212
Beta strandi45 – 528
Beta strandi54 – 563
Beta strandi58 – 636
Beta strandi65 – 717
Beta strandi75 – 773
Beta strandi81 – 833
Helixi89 – 913
Beta strandi97 – 993
Beta strandi101 – 1066
Beta strandi109 – 1124
Helixi113 – 1197
Beta strandi123 – 1297

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50E1-130[»]
1M5Gmodel-H2-130[»]
1P6Gelectron microscopy12.30H2-130[»]
1P87electron microscopy11.50H2-130[»]
1S03X-ray2.70G/H2-130[»]
1VS5X-ray3.46H1-130[»]
1VS7X-ray3.46H1-130[»]
2AVYX-ray3.46H2-130[»]
2AW7X-ray3.46H2-130[»]
2GY9electron microscopy15.00H3-129[»]
2GYBelectron microscopy15.00H3-129[»]
2I2PX-ray3.22H2-130[»]
2I2UX-ray3.22H2-130[»]
2QALX-ray3.21H2-130[»]
2QANX-ray3.21H2-130[»]
2QB9X-ray3.54H2-130[»]
2QBBX-ray3.54H2-130[»]
2QBDX-ray3.30H2-130[»]
2QBFX-ray3.30H2-130[»]
2QBHX-ray4.00H2-130[»]
2QBJX-ray4.00H2-130[»]
2QOUX-ray3.93H2-130[»]
2QOWX-ray3.93H2-130[»]
2QOYX-ray3.50H2-130[»]
2QP0X-ray3.50H2-130[»]
2VHOX-ray3.74H2-130[»]
2VHPX-ray3.74H2-130[»]
2WWLelectron microscopy5.80H2-130[»]
2YKRelectron microscopy9.80H2-130[»]
2Z4KX-ray4.45H2-130[»]
2Z4MX-ray4.45H2-130[»]
3DF1X-ray3.50H2-129[»]
3DF3X-ray3.50H2-129[»]
3E1Aelectron microscopy9.00V1-130[»]
3E1Celectron microscopy9.00V1-130[»]
3FIHelectron microscopy6.70H2-130[»]
3I1MX-ray3.19H1-130[»]
3I1OX-ray3.19H1-130[»]
3I1QX-ray3.81H1-130[»]
3I1SX-ray3.81H1-130[»]
3I1ZX-ray3.71H1-130[»]
3I21X-ray3.71H1-130[»]
3IZVelectron microscopy-L1-130[»]
3IZWelectron microscopy-L1-130[»]
3J00electron microscopy-H2-130[»]
3J0Uelectron microscopy12.10K2-130[»]
3J0Velectron microscopy14.70K2-130[»]
3J0Xelectron microscopy13.50K2-130[»]
3J0Zelectron microscopy11.50K2-130[»]
3J10electron microscopy11.50K2-130[»]
3J13electron microscopy13.10J2-130[»]
3J18electron microscopy8.30H2-130[»]
3J36electron microscopy9.80H2-130[»]
3J4Velectron microscopy12.00H1-130[»]
3J4Welectron microscopy12.00H1-130[»]
3J4Yelectron microscopy17.00H1-130[»]
3J4Zelectron microscopy20.00H1-130[»]
3J53electron microscopy13.00H1-130[»]
3J55electron microscopy15.00H1-130[»]
3J57electron microscopy17.00H1-130[»]
3J59electron microscopy12.00H1-130[»]
3J5Belectron microscopy17.00H1-130[»]
3J5Delectron microscopy17.00H1-130[»]
3J5Felectron microscopy20.00H1-130[»]
3J5Helectron microscopy15.00H1-130[»]
3J5Jelectron microscopy9.00H1-130[»]
3J5Nelectron microscopy6.80H1-130[»]
3J5Telectron microscopy7.60H2-130[»]
3J5Xelectron microscopy7.60H2-130[»]
3KC4electron microscopy-H1-130[»]
3OAQX-ray3.25H2-130[»]
3OARX-ray3.25H2-130[»]
3OFAX-ray3.19H2-130[»]
3OFBX-ray3.19H2-130[»]
3OFOX-ray3.10H2-130[»]
3OFPX-ray3.10H2-130[»]
3OFXX-ray3.29H2-130[»]
3OFYX-ray3.29H2-130[»]
3OR9X-ray3.30H1-130[»]
3ORAX-ray3.30H1-130[»]
3SFSX-ray3.20H1-130[»]
3UOQX-ray3.70H1-130[»]
4A2Ielectron microscopy16.50H2-130[»]
4ADVelectron microscopy13.50H2-130[»]
4GAQX-ray3.30H1-130[»]
4GASX-ray3.30H1-130[»]
4GD1X-ray3.00H2-130[»]
4GD2X-ray3.00H2-130[»]
4KIYX-ray2.90H1-130[»]
4KJ0X-ray2.90H1-130[»]
4KJ2X-ray2.90H1-130[»]
4KJ4X-ray2.90H1-130[»]
4KJ6X-ray2.90H1-130[»]
4KJ8X-ray2.90H1-130[»]
4KJAX-ray2.90H1-130[»]
4KJCX-ray2.90H1-130[»]
ProteinModelPortaliP0A7W7.
SMRiP0A7W7. Positions 3-129.

Miscellaneous databases

EvolutionaryTraceiP0A7W7.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0096.
HOGENOMiHOG000204095.
KOiK02994.
OMAiTRVRNGQ.
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

MSMQDPIADM LTRIRNGQAA NKAAVTMPSS KLKVAIANVL KEEGFIEDFK    50
VEGDTKPELE LTLKYFQGKA VVESIQRVSR PGLRIYKRKD ELPKVMAGLG 100
IAVVSTSKGV MTDRAARQAG LGGEIICYVA 130
Length:130
Mass (Da):14,127
Last modified:January 23, 2007 - v2
Checksum:i74641BC5021DA651
GO

Mass spectrometryi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911E → Q in CAA25719. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_492126.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76331; AAC76331; b3306.
BAE77985; BAE77985; BAE77985.
GeneIDi12934408.
947802.
KEGGiecj:Y75_p3870.
eco:b3306.
PATRICi32122044. VBIEscCol129921_3399.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi E65123. R3EC8.
RefSeqi NP_417765.1. NC_000913.3.
YP_492126.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EG0 electron microscopy 11.50 E 1-130 [» ]
1M5G model - H 2-130 [» ]
1P6G electron microscopy 12.30 H 2-130 [» ]
1P87 electron microscopy 11.50 H 2-130 [» ]
1S03 X-ray 2.70 G/H 2-130 [» ]
1VS5 X-ray 3.46 H 1-130 [» ]
1VS7 X-ray 3.46 H 1-130 [» ]
2AVY X-ray 3.46 H 2-130 [» ]
2AW7 X-ray 3.46 H 2-130 [» ]
2GY9 electron microscopy 15.00 H 3-129 [» ]
2GYB electron microscopy 15.00 H 3-129 [» ]
2I2P X-ray 3.22 H 2-130 [» ]
2I2U X-ray 3.22 H 2-130 [» ]
2QAL X-ray 3.21 H 2-130 [» ]
2QAN X-ray 3.21 H 2-130 [» ]
2QB9 X-ray 3.54 H 2-130 [» ]
2QBB X-ray 3.54 H 2-130 [» ]
2QBD X-ray 3.30 H 2-130 [» ]
2QBF X-ray 3.30 H 2-130 [» ]
2QBH X-ray 4.00 H 2-130 [» ]
2QBJ X-ray 4.00 H 2-130 [» ]
2QOU X-ray 3.93 H 2-130 [» ]
2QOW X-ray 3.93 H 2-130 [» ]
2QOY X-ray 3.50 H 2-130 [» ]
2QP0 X-ray 3.50 H 2-130 [» ]
2VHO X-ray 3.74 H 2-130 [» ]
2VHP X-ray 3.74 H 2-130 [» ]
2WWL electron microscopy 5.80 H 2-130 [» ]
2YKR electron microscopy 9.80 H 2-130 [» ]
2Z4K X-ray 4.45 H 2-130 [» ]
2Z4M X-ray 4.45 H 2-130 [» ]
3DF1 X-ray 3.50 H 2-129 [» ]
3DF3 X-ray 3.50 H 2-129 [» ]
3E1A electron microscopy 9.00 V 1-130 [» ]
3E1C electron microscopy 9.00 V 1-130 [» ]
3FIH electron microscopy 6.70 H 2-130 [» ]
3I1M X-ray 3.19 H 1-130 [» ]
3I1O X-ray 3.19 H 1-130 [» ]
3I1Q X-ray 3.81 H 1-130 [» ]
3I1S X-ray 3.81 H 1-130 [» ]
3I1Z X-ray 3.71 H 1-130 [» ]
3I21 X-ray 3.71 H 1-130 [» ]
3IZV electron microscopy - L 1-130 [» ]
3IZW electron microscopy - L 1-130 [» ]
3J00 electron microscopy - H 2-130 [» ]
3J0U electron microscopy 12.10 K 2-130 [» ]
3J0V electron microscopy 14.70 K 2-130 [» ]
3J0X electron microscopy 13.50 K 2-130 [» ]
3J0Z electron microscopy 11.50 K 2-130 [» ]
3J10 electron microscopy 11.50 K 2-130 [» ]
3J13 electron microscopy 13.10 J 2-130 [» ]
3J18 electron microscopy 8.30 H 2-130 [» ]
3J36 electron microscopy 9.80 H 2-130 [» ]
3J4V electron microscopy 12.00 H 1-130 [» ]
3J4W electron microscopy 12.00 H 1-130 [» ]
3J4Y electron microscopy 17.00 H 1-130 [» ]
3J4Z electron microscopy 20.00 H 1-130 [» ]
3J53 electron microscopy 13.00 H 1-130 [» ]
3J55 electron microscopy 15.00 H 1-130 [» ]
3J57 electron microscopy 17.00 H 1-130 [» ]
3J59 electron microscopy 12.00 H 1-130 [» ]
3J5B electron microscopy 17.00 H 1-130 [» ]
3J5D electron microscopy 17.00 H 1-130 [» ]
3J5F electron microscopy 20.00 H 1-130 [» ]
3J5H electron microscopy 15.00 H 1-130 [» ]
3J5J electron microscopy 9.00 H 1-130 [» ]
3J5N electron microscopy 6.80 H 1-130 [» ]
3J5T electron microscopy 7.60 H 2-130 [» ]
3J5X electron microscopy 7.60 H 2-130 [» ]
3KC4 electron microscopy - H 1-130 [» ]
3OAQ X-ray 3.25 H 2-130 [» ]
3OAR X-ray 3.25 H 2-130 [» ]
3OFA X-ray 3.19 H 2-130 [» ]
3OFB X-ray 3.19 H 2-130 [» ]
3OFO X-ray 3.10 H 2-130 [» ]
3OFP X-ray 3.10 H 2-130 [» ]
3OFX X-ray 3.29 H 2-130 [» ]
3OFY X-ray 3.29 H 2-130 [» ]
3OR9 X-ray 3.30 H 1-130 [» ]
3ORA X-ray 3.30 H 1-130 [» ]
3SFS X-ray 3.20 H 1-130 [» ]
3UOQ X-ray 3.70 H 1-130 [» ]
4A2I electron microscopy 16.50 H 2-130 [» ]
4ADV electron microscopy 13.50 H 2-130 [» ]
4GAQ X-ray 3.30 H 1-130 [» ]
4GAS X-ray 3.30 H 1-130 [» ]
4GD1 X-ray 3.00 H 2-130 [» ]
4GD2 X-ray 3.00 H 2-130 [» ]
4KIY X-ray 2.90 H 1-130 [» ]
4KJ0 X-ray 2.90 H 1-130 [» ]
4KJ2 X-ray 2.90 H 1-130 [» ]
4KJ4 X-ray 2.90 H 1-130 [» ]
4KJ6 X-ray 2.90 H 1-130 [» ]
4KJ8 X-ray 2.90 H 1-130 [» ]
4KJA X-ray 2.90 H 1-130 [» ]
4KJC X-ray 2.90 H 1-130 [» ]
ProteinModelPortali P0A7W7.
SMRi P0A7W7. Positions 3-129.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852114. 1 interaction.
DIPi DIP-47901N.
IntActi P0A7W7. 38 interactions.
MINTi MINT-1318565.
STRINGi 511145.b3306.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7W7.
PRIDEi P0A7W7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76331 ; AAC76331 ; b3306 .
BAE77985 ; BAE77985 ; BAE77985 .
GeneIDi 12934408.
947802.
KEGGi ecj:Y75_p3870.
eco:b3306.
PATRICi 32122044. VBIEscCol129921_3399.

Organism-specific databases

EchoBASEi EB0900.
EcoGenei EG10907. rpsH.

Phylogenomic databases

eggNOGi COG0096.
HOGENOMi HOG000204095.
KOi K02994.
OMAi TRVRNGQ.
OrthoDBi EOG6Z0QH1.
PhylomeDBi P0A7W7.

Enzyme and pathway databases

BioCyci EcoCyc:EG10907-MONOMER.
ECOL316407:JW3268-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7W7.
PROi P0A7W7.

Gene expression databases

Genevestigatori P0A7W7.

Family and domain databases

HAMAPi MF_01302_B. Ribosomal_S8_B.
InterProi IPR000630. Ribosomal_S8.
[Graphical view ]
PANTHERi PTHR11758. PTHR11758. 1 hit.
Pfami PF00410. Ribosomal_S8. 1 hit.
[Graphical view ]
SUPFAMi SSF56047. SSF56047. 1 hit.
PROSITEi PS00053. RIBOSOMAL_S8. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 91 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

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