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Protein

30S ribosomal protein S17

Gene

rpsQ

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

Functioni

One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. Also plays a role in translational accuracy; neamine-resistant ribosomes show reduced neamine-induced misreading in vitro.

GO - Molecular functioni

  • rRNA binding Source: EcoliWiki
  • small ribosomal subunit rRNA binding Source: EcoliWiki
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

  • response to antibiotic Source: EcoliWiki
  • translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10916-MONOMER.
ECOL316407:JW3273-MONOMER.
MetaCyc:EG10916-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S17UniRule annotation
Gene namesi
Name:rpsQUniRule annotation
Synonyms:neaA
Ordered Locus Names:b3311, JW3273
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10916. rpsQ.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001284562 – 8430S ribosomal protein S17Add BLAST83

Proteomic databases

EPDiP0AG63.
PaxDbiP0AG63.
PRIDEiP0AG63.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit.

Protein-protein interaction databases

DIPiDIP-47952N.
IntActiP0AG63. 1 interactor.
STRINGi511145.b3311.

Structurei

Secondary structure

184
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 11Combined sources4
Beta strandi17 – 19Combined sources3
Beta strandi22 – 25Combined sources4
Beta strandi28 – 30Combined sources3
Turni32 – 34Combined sources3
Beta strandi37 – 39Combined sources3
Beta strandi42 – 47Combined sources6
Helixi49 – 51Combined sources3
Beta strandi58 – 63Combined sources6
Beta strandi68 – 70Combined sources3
Beta strandi71 – 79Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50G2-84[»]
1M5Gmodel-Q4-84[»]
2YKRelectron microscopy9.80Q4-83[»]
3J9Yelectron microscopy3.90q1-84[»]
3J9Zelectron microscopy3.60SQ2-84[»]
3JA1electron microscopy3.60SQ2-84[»]
3JBUelectron microscopy3.64Q1-84[»]
3JBVelectron microscopy3.32Q1-84[»]
3JCDelectron microscopy3.70q1-84[»]
3JCEelectron microscopy3.20q1-84[»]
3JCJelectron microscopy3.70x1-84[»]
3JCNelectron microscopy4.60r1-84[»]
4A2Ielectron microscopy16.50Q4-83[»]
4ADVelectron microscopy13.50Q2-84[»]
4U1UX-ray2.95AQ/CQ4-83[»]
4U1VX-ray3.00AQ/CQ4-83[»]
4U20X-ray2.90AQ/CQ4-83[»]
4U24X-ray2.90AQ/CQ4-83[»]
4U25X-ray2.90AQ/CQ4-83[»]
4U26X-ray2.80AQ/CQ4-83[»]
4U27X-ray2.80AQ/CQ4-83[»]
4V47electron microscopy12.30BQ2-84[»]
4V48electron microscopy11.50BQ2-84[»]
4V4HX-ray3.46AQ/CQ1-84[»]
4V4QX-ray3.46AQ/CQ2-84[»]
4V4Velectron microscopy15.00AQ6-84[»]
4V4Welectron microscopy15.00AQ6-84[»]
4V50X-ray3.22AQ/CQ2-84[»]
4V52X-ray3.21AQ/CQ2-84[»]
4V53X-ray3.54AQ/CQ2-84[»]
4V54X-ray3.30AQ/CQ2-84[»]
4V55X-ray4.00AQ/CQ2-84[»]
4V56X-ray3.93AQ/CQ2-84[»]
4V57X-ray3.50AQ/CQ2-84[»]
4V5BX-ray3.74BQ/DQ2-84[»]
4V5Helectron microscopy5.80AQ4-83[»]
4V5YX-ray4.45AQ/CQ2-84[»]
4V64X-ray3.50AQ/CQ2-84[»]
4V65electron microscopy9.00AJ1-84[»]
4V66electron microscopy9.00AJ1-84[»]
4V69electron microscopy6.70AQ4-83[»]
4V6CX-ray3.19AQ/CQ1-84[»]
4V6DX-ray3.81AQ/CQ1-84[»]
4V6EX-ray3.71AQ/CQ1-84[»]
4V6Kelectron microscopy8.25BU1-84[»]
4V6Lelectron microscopy13.20AU1-84[»]
4V6Melectron microscopy7.10AQ2-84[»]
4V6Nelectron microscopy12.10BT2-84[»]
4V6Oelectron microscopy14.70AT2-84[»]
4V6Pelectron microscopy13.50AT2-84[»]
4V6Qelectron microscopy11.50AT2-84[»]
4V6Relectron microscopy11.50AT2-84[»]
4V6Selectron microscopy13.10BS2-84[»]
4V6Telectron microscopy8.30AQ4-83[»]
4V6Velectron microscopy9.80AQ2-84[»]
4V6Yelectron microscopy12.00AQ4-83[»]
4V6Zelectron microscopy12.00AQ4-83[»]
4V70electron microscopy17.00AQ4-83[»]
4V71electron microscopy20.00AQ4-83[»]
4V72electron microscopy13.00AQ4-83[»]
4V73electron microscopy15.00AQ4-83[»]
4V74electron microscopy17.00AQ4-83[»]
4V75electron microscopy12.00AQ4-83[»]
4V76electron microscopy17.00AQ4-83[»]
4V77electron microscopy17.00AQ4-83[»]
4V78electron microscopy20.00AQ4-83[»]
4V79electron microscopy15.00AQ4-83[»]
4V7Aelectron microscopy9.00AQ4-83[»]
4V7Belectron microscopy6.80AQ1-84[»]
4V7Celectron microscopy7.60AQ2-84[»]
4V7Delectron microscopy7.60BQ2-84[»]
4V7Ielectron microscopy9.60BQ1-84[»]
4V7SX-ray3.25AQ/CQ4-83[»]
4V7TX-ray3.19AQ/CQ4-83[»]
4V7UX-ray3.10AQ/CQ4-83[»]
4V7VX-ray3.29AQ/CQ4-83[»]
4V85X-ray3.20Q1-84[»]
4V89X-ray3.70AQ1-84[»]
4V9CX-ray3.30AQ/CQ1-84[»]
4V9DX-ray3.00AQ/BQ4-83[»]
4V9OX-ray2.90BQ/DQ/FQ/HQ1-84[»]
4V9PX-ray2.90BQ/DQ/FQ/HQ1-84[»]
4WF1X-ray3.09AQ/CQ4-83[»]
4WOIX-ray3.00AQ/DQ1-84[»]
4WWWX-ray3.10QQ/XQ4-83[»]
4YBBX-ray2.10AQ/BQ4-83[»]
5AFIelectron microscopy2.90q1-84[»]
5IQRelectron microscopy3.00v1-84[»]
5IT8X-ray3.12AQ/BQ4-83[»]
5J5BX-ray2.80AQ/BQ4-83[»]
5J7LX-ray3.00AQ/BQ4-83[»]
5J88X-ray3.32AQ/BQ4-83[»]
5J8AX-ray3.10AQ/BQ4-83[»]
5J91X-ray2.96AQ/BQ4-83[»]
5JC9X-ray3.03AQ/BQ4-83[»]
5JTEelectron microscopy3.60AQ1-84[»]
5JU8electron microscopy3.60AQ1-84[»]
5KCRelectron microscopy3.601q1-84[»]
5KCSelectron microscopy3.901q1-84[»]
5KPSelectron microscopy3.90221-84[»]
5KPVelectron microscopy4.10211-84[»]
5KPWelectron microscopy3.90211-84[»]
5KPXelectron microscopy3.90211-84[»]
5L3Pelectron microscopy3.70q1-84[»]
DisProtiDP00242.
ProteinModelPortaliP0AG63.
SMRiP0AG63.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG63.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S17P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0186. LUCA.
HOGENOMiHOG000231339.
InParanoidiP0AG63.
KOiK02961.
OMAiLKAHDEQ.
PhylomeDBiP0AG63.

Family and domain databases

HAMAPiMF_01345_B. Ribosomal_S17_B. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR000266. Ribosomal_S17/S11.
IPR019984. Ribosomal_S17_bac-type.
IPR019979. Ribosomal_S17_CS.
[Graphical view]
PANTHERiPTHR10744. PTHR10744. 1 hit.
PfamiPF00366. Ribosomal_S17. 1 hit.
[Graphical view]
PRINTSiPR00973. RIBOSOMALS17.
ProDomiPD001295. Ribosomal_S17. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR03635. uS17_bact. 1 hit.
PROSITEiPS00056. RIBOSOMAL_S17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0AG63-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDKIRTLQG RVVSDKMEKS IVVAIERFVK HPIYGKFIKR TTKLHVHDEN
60 70 80
NECGIGDVVE IRECRPLSKT KSWTLVRVVE KAVL
Length:84
Mass (Da):9,704
Last modified:January 23, 2007 - v2
Checksum:iFC64AF04841842F6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53 – 59CGIGDVV → GIGDVVC AA sequence (PubMed:344065).Curated7
Sequence conflicti64 – 66CRP → RPC (PubMed:151587).Curated3

Mass spectrometryi

Molecular mass is 9573.0 Da from positions 2 - 84. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti31H → P in neamine-resistant mutant nea301. 1
Natural varianti68S → F Prevents 30S subunit assembly at 42 degrees Celsius. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26469.1.
U18997 Genomic DNA. Translation: AAA58108.1.
U00096 Genomic DNA. Translation: AAC76336.1.
AP009048 Genomic DNA. Translation: BAE77980.1.
V00357 Genomic DNA. Translation: CAA23652.1.
X01563 Genomic DNA. Translation: CAA25714.1.
PIRiA37519. R3EC17.
RefSeqiNP_417770.1. NC_000913.3.
WP_000130100.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76336; AAC76336; b3311.
BAE77980; BAE77980; BAE77980.
GeneIDi5552384.
947808.
KEGGiecj:JW3273.
eco:b3311.
PATRICi32122054. VBIEscCol129921_3404.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26469.1.
U18997 Genomic DNA. Translation: AAA58108.1.
U00096 Genomic DNA. Translation: AAC76336.1.
AP009048 Genomic DNA. Translation: BAE77980.1.
V00357 Genomic DNA. Translation: CAA23652.1.
X01563 Genomic DNA. Translation: CAA25714.1.
PIRiA37519. R3EC17.
RefSeqiNP_417770.1. NC_000913.3.
WP_000130100.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50G2-84[»]
1M5Gmodel-Q4-84[»]
2YKRelectron microscopy9.80Q4-83[»]
3J9Yelectron microscopy3.90q1-84[»]
3J9Zelectron microscopy3.60SQ2-84[»]
3JA1electron microscopy3.60SQ2-84[»]
3JBUelectron microscopy3.64Q1-84[»]
3JBVelectron microscopy3.32Q1-84[»]
3JCDelectron microscopy3.70q1-84[»]
3JCEelectron microscopy3.20q1-84[»]
3JCJelectron microscopy3.70x1-84[»]
3JCNelectron microscopy4.60r1-84[»]
4A2Ielectron microscopy16.50Q4-83[»]
4ADVelectron microscopy13.50Q2-84[»]
4U1UX-ray2.95AQ/CQ4-83[»]
4U1VX-ray3.00AQ/CQ4-83[»]
4U20X-ray2.90AQ/CQ4-83[»]
4U24X-ray2.90AQ/CQ4-83[»]
4U25X-ray2.90AQ/CQ4-83[»]
4U26X-ray2.80AQ/CQ4-83[»]
4U27X-ray2.80AQ/CQ4-83[»]
4V47electron microscopy12.30BQ2-84[»]
4V48electron microscopy11.50BQ2-84[»]
4V4HX-ray3.46AQ/CQ1-84[»]
4V4QX-ray3.46AQ/CQ2-84[»]
4V4Velectron microscopy15.00AQ6-84[»]
4V4Welectron microscopy15.00AQ6-84[»]
4V50X-ray3.22AQ/CQ2-84[»]
4V52X-ray3.21AQ/CQ2-84[»]
4V53X-ray3.54AQ/CQ2-84[»]
4V54X-ray3.30AQ/CQ2-84[»]
4V55X-ray4.00AQ/CQ2-84[»]
4V56X-ray3.93AQ/CQ2-84[»]
4V57X-ray3.50AQ/CQ2-84[»]
4V5BX-ray3.74BQ/DQ2-84[»]
4V5Helectron microscopy5.80AQ4-83[»]
4V5YX-ray4.45AQ/CQ2-84[»]
4V64X-ray3.50AQ/CQ2-84[»]
4V65electron microscopy9.00AJ1-84[»]
4V66electron microscopy9.00AJ1-84[»]
4V69electron microscopy6.70AQ4-83[»]
4V6CX-ray3.19AQ/CQ1-84[»]
4V6DX-ray3.81AQ/CQ1-84[»]
4V6EX-ray3.71AQ/CQ1-84[»]
4V6Kelectron microscopy8.25BU1-84[»]
4V6Lelectron microscopy13.20AU1-84[»]
4V6Melectron microscopy7.10AQ2-84[»]
4V6Nelectron microscopy12.10BT2-84[»]
4V6Oelectron microscopy14.70AT2-84[»]
4V6Pelectron microscopy13.50AT2-84[»]
4V6Qelectron microscopy11.50AT2-84[»]
4V6Relectron microscopy11.50AT2-84[»]
4V6Selectron microscopy13.10BS2-84[»]
4V6Telectron microscopy8.30AQ4-83[»]
4V6Velectron microscopy9.80AQ2-84[»]
4V6Yelectron microscopy12.00AQ4-83[»]
4V6Zelectron microscopy12.00AQ4-83[»]
4V70electron microscopy17.00AQ4-83[»]
4V71electron microscopy20.00AQ4-83[»]
4V72electron microscopy13.00AQ4-83[»]
4V73electron microscopy15.00AQ4-83[»]
4V74electron microscopy17.00AQ4-83[»]
4V75electron microscopy12.00AQ4-83[»]
4V76electron microscopy17.00AQ4-83[»]
4V77electron microscopy17.00AQ4-83[»]
4V78electron microscopy20.00AQ4-83[»]
4V79electron microscopy15.00AQ4-83[»]
4V7Aelectron microscopy9.00AQ4-83[»]
4V7Belectron microscopy6.80AQ1-84[»]
4V7Celectron microscopy7.60AQ2-84[»]
4V7Delectron microscopy7.60BQ2-84[»]
4V7Ielectron microscopy9.60BQ1-84[»]
4V7SX-ray3.25AQ/CQ4-83[»]
4V7TX-ray3.19AQ/CQ4-83[»]
4V7UX-ray3.10AQ/CQ4-83[»]
4V7VX-ray3.29AQ/CQ4-83[»]
4V85X-ray3.20Q1-84[»]
4V89X-ray3.70AQ1-84[»]
4V9CX-ray3.30AQ/CQ1-84[»]
4V9DX-ray3.00AQ/BQ4-83[»]
4V9OX-ray2.90BQ/DQ/FQ/HQ1-84[»]
4V9PX-ray2.90BQ/DQ/FQ/HQ1-84[»]
4WF1X-ray3.09AQ/CQ4-83[»]
4WOIX-ray3.00AQ/DQ1-84[»]
4WWWX-ray3.10QQ/XQ4-83[»]
4YBBX-ray2.10AQ/BQ4-83[»]
5AFIelectron microscopy2.90q1-84[»]
5IQRelectron microscopy3.00v1-84[»]
5IT8X-ray3.12AQ/BQ4-83[»]
5J5BX-ray2.80AQ/BQ4-83[»]
5J7LX-ray3.00AQ/BQ4-83[»]
5J88X-ray3.32AQ/BQ4-83[»]
5J8AX-ray3.10AQ/BQ4-83[»]
5J91X-ray2.96AQ/BQ4-83[»]
5JC9X-ray3.03AQ/BQ4-83[»]
5JTEelectron microscopy3.60AQ1-84[»]
5JU8electron microscopy3.60AQ1-84[»]
5KCRelectron microscopy3.601q1-84[»]
5KCSelectron microscopy3.901q1-84[»]
5KPSelectron microscopy3.90221-84[»]
5KPVelectron microscopy4.10211-84[»]
5KPWelectron microscopy3.90211-84[»]
5KPXelectron microscopy3.90211-84[»]
5L3Pelectron microscopy3.70q1-84[»]
DisProtiDP00242.
ProteinModelPortaliP0AG63.
SMRiP0AG63.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47952N.
IntActiP0AG63. 1 interactor.
STRINGi511145.b3311.

Proteomic databases

EPDiP0AG63.
PaxDbiP0AG63.
PRIDEiP0AG63.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76336; AAC76336; b3311.
BAE77980; BAE77980; BAE77980.
GeneIDi5552384.
947808.
KEGGiecj:JW3273.
eco:b3311.
PATRICi32122054. VBIEscCol129921_3404.

Organism-specific databases

EchoBASEiEB0909.
EcoGeneiEG10916. rpsQ.

Phylogenomic databases

eggNOGiCOG0186. LUCA.
HOGENOMiHOG000231339.
InParanoidiP0AG63.
KOiK02961.
OMAiLKAHDEQ.
PhylomeDBiP0AG63.

Enzyme and pathway databases

BioCyciEcoCyc:EG10916-MONOMER.
ECOL316407:JW3273-MONOMER.
MetaCyc:EG10916-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AG63.
PROiP0AG63.

Family and domain databases

HAMAPiMF_01345_B. Ribosomal_S17_B. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR000266. Ribosomal_S17/S11.
IPR019984. Ribosomal_S17_bac-type.
IPR019979. Ribosomal_S17_CS.
[Graphical view]
PANTHERiPTHR10744. PTHR10744. 1 hit.
PfamiPF00366. Ribosomal_S17. 1 hit.
[Graphical view]
PRINTSiPR00973. RIBOSOMALS17.
ProDomiPD001295. Ribosomal_S17. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR03635. uS17_bact. 1 hit.
PROSITEiPS00056. RIBOSOMAL_S17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRS17_ECOLI
AccessioniPrimary (citable) accession number: P0AG63
Secondary accession number(s): P02373, Q2M6X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The strain missing both S17 and L29 grows very slowly and has a rather unstable temperature-sensitive phenotype.

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.