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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.
MetaCyc:EG10907-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10907. rpsH.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

DrugBankiDB00759. Tetracycline.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001264052 – 13030S ribosomal protein S8Add BLAST129

Proteomic databases

EPDiP0A7W7.
PaxDbiP0A7W7.
PRIDEiP0A7W7.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi852114. 1 interactor.
DIPiDIP-47901N.
IntActiP0A7W7. 38 interactors.
MINTiMINT-1318565.
STRINGi511145.b3306.

Structurei

Secondary structure

1130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 19Combined sources14
Beta strandi23 – 28Combined sources6
Helixi31 – 42Combined sources12
Beta strandi45 – 52Combined sources8
Beta strandi54 – 56Combined sources3
Beta strandi58 – 63Combined sources6
Beta strandi65 – 71Combined sources7
Beta strandi75 – 77Combined sources3
Helixi89 – 91Combined sources3
Beta strandi97 – 99Combined sources3
Beta strandi101 – 106Combined sources6
Beta strandi109 – 112Combined sources4
Helixi113 – 119Combined sources7
Beta strandi123 – 129Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50E1-130[»]
1M5Gmodel-H2-130[»]
1S03X-ray2.70G/H2-130[»]
2YKRelectron microscopy9.80H2-130[»]
3J9Yelectron microscopy3.90h1-130[»]
3J9Zelectron microscopy3.60SH2-130[»]
3JA1electron microscopy3.60SH2-130[»]
3JBUelectron microscopy3.64H1-130[»]
3JBVelectron microscopy3.32H1-130[»]
3JCDelectron microscopy3.70h1-130[»]
3JCEelectron microscopy3.20h1-130[»]
3JCJelectron microscopy3.70p1-130[»]
3JCNelectron microscopy4.60k1-130[»]
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[»]
4V6Velectron microscopy9.80AH2-130[»]
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[»]
4WOIX-ray3.00AH/DH1-130[»]
4WWWX-ray3.10QH/XH2-130[»]
4YBBX-ray2.10AH/BH2-130[»]
5AFIelectron microscopy2.90h1-130[»]
5IQRelectron microscopy3.00m1-130[»]
5IT8X-ray3.12AH/BH2-130[»]
5J5BX-ray2.80AH/BH2-130[»]
5J7LX-ray3.00AH/BH2-130[»]
5J88X-ray3.32AH/BH2-130[»]
5J8AX-ray3.10AH/BH2-130[»]
5J91X-ray2.96AH/BH2-130[»]
5JC9X-ray3.03AH/BH2-130[»]
5JTEelectron microscopy3.60AH1-130[»]
5JU8electron microscopy3.60AH1-130[»]
5KCRelectron microscopy3.601h1-130[»]
5KCSelectron microscopy3.901h1-130[»]
5KPSelectron microscopy3.90131-130[»]
5KPVelectron microscopy4.10121-130[»]
5KPWelectron microscopy3.90121-130[»]
5KPXelectron microscopy3.90121-130[»]
5L3Pelectron microscopy3.70h1-130[»]
ProteinModelPortaliP0A7W7.
SMRiP0A7W7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7W7.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S8P family.Curated

Phylogenomic databases

eggNOGiCOG0096. LUCA.
HOGENOMiHOG000204095.
InParanoidiP0A7W7.
KOiK02994.
OMAiRIYKNTR.
PhylomeDBiP0A7W7.

Family and domain databases

HAMAPiMF_01302_B. Ribosomal_S8_B. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti91E → Q in CAA25719 (PubMed:6222285).Curated1

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.
WP_000062611.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76331; AAC76331; b3306.
BAE77985; BAE77985; BAE77985.
GeneIDi947802.
KEGGiecj:JW3268.
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.
WP_000062611.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50E1-130[»]
1M5Gmodel-H2-130[»]
1S03X-ray2.70G/H2-130[»]
2YKRelectron microscopy9.80H2-130[»]
3J9Yelectron microscopy3.90h1-130[»]
3J9Zelectron microscopy3.60SH2-130[»]
3JA1electron microscopy3.60SH2-130[»]
3JBUelectron microscopy3.64H1-130[»]
3JBVelectron microscopy3.32H1-130[»]
3JCDelectron microscopy3.70h1-130[»]
3JCEelectron microscopy3.20h1-130[»]
3JCJelectron microscopy3.70p1-130[»]
3JCNelectron microscopy4.60k1-130[»]
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[»]
4V6Velectron microscopy9.80AH2-130[»]
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[»]
4WOIX-ray3.00AH/DH1-130[»]
4WWWX-ray3.10QH/XH2-130[»]
4YBBX-ray2.10AH/BH2-130[»]
5AFIelectron microscopy2.90h1-130[»]
5IQRelectron microscopy3.00m1-130[»]
5IT8X-ray3.12AH/BH2-130[»]
5J5BX-ray2.80AH/BH2-130[»]
5J7LX-ray3.00AH/BH2-130[»]
5J88X-ray3.32AH/BH2-130[»]
5J8AX-ray3.10AH/BH2-130[»]
5J91X-ray2.96AH/BH2-130[»]
5JC9X-ray3.03AH/BH2-130[»]
5JTEelectron microscopy3.60AH1-130[»]
5JU8electron microscopy3.60AH1-130[»]
5KCRelectron microscopy3.601h1-130[»]
5KCSelectron microscopy3.901h1-130[»]
5KPSelectron microscopy3.90131-130[»]
5KPVelectron microscopy4.10121-130[»]
5KPWelectron microscopy3.90121-130[»]
5KPXelectron microscopy3.90121-130[»]
5L3Pelectron microscopy3.70h1-130[»]
ProteinModelPortaliP0A7W7.
SMRiP0A7W7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852114. 1 interactor.
DIPiDIP-47901N.
IntActiP0A7W7. 38 interactors.
MINTiMINT-1318565.
STRINGi511145.b3306.

Chemistry databases

DrugBankiDB00759. Tetracycline.

Protein family/group databases

MoonProtiP0A7W7.

Proteomic databases

EPDiP0A7W7.
PaxDbiP0A7W7.
PRIDEiP0A7W7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76331; AAC76331; b3306.
BAE77985; BAE77985; BAE77985.
GeneIDi947802.
KEGGiecj:JW3268.
eco:b3306.
PATRICi32122044. VBIEscCol129921_3399.

Organism-specific databases

EchoBASEiEB0900.
EcoGeneiEG10907. rpsH.

Phylogenomic databases

eggNOGiCOG0096. LUCA.
HOGENOMiHOG000204095.
InParanoidiP0A7W7.
KOiK02994.
OMAiRIYKNTR.
PhylomeDBiP0A7W7.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7W7.
PROiP0A7W7.

Family and domain databases

HAMAPiMF_01302_B. Ribosomal_S8_B. 1 hit.
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...

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: November 30, 2016
This is version 113 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

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 one 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.