Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0AG63 (RS17_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
30S ribosomal protein S17
Gene names
Name:rpsQ
Synonyms:neaA
Ordered Locus Names:b3311, JW3273
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length84 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_01345

Subunit structure

Part of the 30S ribosomal subunit. Ref.8

Miscellaneous

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

Sequence similarities

Belongs to the ribosomal protein S17P family.

Mass spectrometry

Molecular mass is 9573.0 Da from positions 2 - 84. Determined by MALDI. Ref.12

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.6
Chain2 – 848330S ribosomal protein S17 HAMAP-Rule MF_01345
PRO_0000128456

Natural variations

Natural variant311H → P in neamine-resistant mutant nea301.
Natural variant681S → F Prevents 30S subunit assembly at 42 degrees Celsius. Ref.10

Experimental info

Sequence conflict53 – 597CGIGDVV → GIGDVVC AA sequence Ref.4
Sequence conflict64 – 663CRP → RPC Ref.5

Secondary structure

................... 84
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AG63 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: FC64AF04841842F6

FASTA849,704
        10         20         30         40         50         60 
MTDKIRTLQG RVVSDKMEKS IVVAIERFVK HPIYGKFIKR TTKLHVHDEN NECGIGDVVE 

        70         80 
IRECRPLSKT KSWTLVRVVE KAVL 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the Escherichia coli S10 ribosomal protein operon."
Zurawski G., Zurawski S.M.
Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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 primary structure of protein S17 from the small ribosomal subunit of Escherichia coli."
Yaguchi M., Wittmann H.G.
FEBS Lett. 87:37-40(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-84.
Strain: K.
[5]"DNA sequences of promoter regions for the str and spc ribosomal protein operons in E. coli."
Post L.E., Arfsten A.E., Reusser F., Nomura M.
Cell 15:215-229(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-84.
Strain: K12.
[6]"Small genes/gene-products in Escherichia coli K-12."
Wasinger V.C., Humphery-Smith I.
FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Strain: K12.
[7]"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(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-36, CROSS-LINKING TO RRNA.
Strain: MRE-600.
[8]"Assembly mapping of 30 S ribosomal proteins from Escherichia coli. Further studies."
Held W.A., Ballou B., Mizushima S., Nomura M.
J. Biol. Chem. 249:3103-3111(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A PRIMARY 16S RRNA-BINDING PROTEIN, ASSEMBLY MAP OF THE 30S SUBUNIT.
Strain: Q13.
[9]"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.
[10]"A missense mutation in the gene coding for ribosomal protein S17 (rpsQ) leading to ribosomal assembly defectivity in Escherichia coli."
Herzog A., Yaguchi M., Cabezon T., Corchuelo M.C., Petre J., Bollen A.
Mol. Gen. Genet. 171:15-22(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: THERMOSENSITIVE VARIANT PHE-68 AFFECTS ASSEMBLY.
[11]"A mutant from Escherichia coli which lacks ribosomal proteins S17 and L29 used to localize these two proteins on the ribosomal surface."
Stoeffler-Meilicke M., Dabbs E.R., Albrecht-Ehrlich R., Stoeffler G.
Eur. J. Biochem. 150:485-490(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF A STRAIN MISSING S17 AND L29.
Strain: AM111.
[12]"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.
[13]"Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli. I. General properties of neaA mutants."
Bollen A., Cabezon T., de Wilde M., Villarroel R., Herzog A.
J. Mol. Biol. 99:795-806(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOLATION, CHARACTERIZATION OF NEAMINE-RESISTANT VARIANT NEA301.
Strain: K12S.
[14]"Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli. II. Localization of the amino acid replacement in protein S17 from a meaA mutant."
Yaguchi M., Wittmann H.G., Cabezon T., DeWilde M., Villarroel R., Herzog A., Bollen A.
J. Mol. Biol. 104:617-620(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: NEAMINE-RESISTANT VARIANT NEA301.
Strain: K12S.
[15]"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.
[16]"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.
[17]"Structures of the bacterial ribosome at 3.5 A resolution."
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.
Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRR3EC17. A37519.
RefSeqNP_417770.1. NC_000913.3.
YP_492121.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50G2-84[»]
1M5Gmodel-Q4-84[»]
1P6Gelectron microscopy12.30Q2-84[»]
1P87electron microscopy11.50Q2-84[»]
1VS5X-ray3.46Q1-84[»]
1VS7X-ray3.46Q1-84[»]
2AVYX-ray3.46Q2-84[»]
2AW7X-ray3.46Q2-84[»]
2GY9electron microscopy15.00Q6-83[»]
2GYBelectron microscopy15.00Q6-83[»]
2I2PX-ray3.22Q2-83[»]
2I2UX-ray3.22Q2-83[»]
2QALX-ray3.21Q2-84[»]
2QANX-ray3.21Q2-84[»]
2QB9X-ray3.54Q2-84[»]
2QBBX-ray3.54Q2-84[»]
2QBDX-ray3.30Q2-84[»]
2QBFX-ray3.30Q2-84[»]
2QBHX-ray4.00Q2-84[»]
2QBJX-ray4.00Q2-84[»]
2QOUX-ray3.93Q2-84[»]
2QOWX-ray3.93Q2-84[»]
2QOYX-ray3.50Q2-84[»]
2QP0X-ray3.50Q2-84[»]
2WWLelectron microscopy5.80Q4-83[»]
2YKRelectron microscopy9.80Q4-83[»]
2Z4KX-ray4.45Q2-84[»]
2Z4MX-ray4.45Q2-84[»]
3E1Aelectron microscopy-J1-84[»]
3E1Celectron microscopy-J1-84[»]
3FIHelectron microscopy6.70Q4-83[»]
3I1MX-ray3.19Q1-84[»]
3I1OX-ray3.19Q1-84[»]
3I1QX-ray3.81Q1-84[»]
3I1SX-ray3.81Q1-84[»]
3I1ZX-ray3.71Q1-84[»]
3I21X-ray3.71Q1-84[»]
3IZVelectron microscopy-U1-84[»]
3IZWelectron microscopy-U1-84[»]
3J00electron microscopy-Q2-84[»]
3J0Uelectron microscopy12.10T2-84[»]
3J0Velectron microscopy14.70T2-84[»]
3J0Xelectron microscopy13.50T2-84[»]
3J0Zelectron microscopy11.50T2-84[»]
3J10electron microscopy11.50T2-84[»]
3J13electron microscopy13.10S2-84[»]
3J18electron microscopy8.30Q4-83[»]
3J36electron microscopy9.80Q2-84[»]
3J4Velectron microscopy12.00Q4-83[»]
3J4Welectron microscopy12.00Q4-83[»]
3J4Yelectron microscopy17.00Q4-83[»]
3J4Zelectron microscopy20.00Q4-83[»]
3J53electron microscopy13.00Q4-83[»]
3J55electron microscopy15.00Q4-83[»]
3J57electron microscopy17.00Q4-83[»]
3J59electron microscopy12.00Q4-83[»]
3J5Belectron microscopy17.00Q4-83[»]
3J5Delectron microscopy17.00Q4-83[»]
3J5Felectron microscopy20.00Q4-83[»]
3J5Helectron microscopy15.00Q4-83[»]
3J5Jelectron microscopy9.00Q4-83[»]
3J5Nelectron microscopy6.80Q1-84[»]
3J5Telectron microscopy7.60Q2-84[»]
3J5Xelectron microscopy7.60Q2-84[»]
3KC4electron microscopy-Q1-84[»]
3OAQX-ray3.25Q4-83[»]
3OARX-ray3.25Q4-83[»]
3OFAX-ray3.19Q4-83[»]
3OFBX-ray3.19Q4-83[»]
3OFOX-ray3.10Q4-83[»]
3OFPX-ray3.10Q4-83[»]
3OFXX-ray3.29Q4-83[»]
3OFYX-ray3.29Q4-83[»]
3OR9X-ray3.30Q1-84[»]
3ORAX-ray3.30Q1-84[»]
3SFSX-ray3.20Q1-84[»]
3UOQX-ray3.70Q1-84[»]
4A2Ielectron microscopy16.50Q4-83[»]
4ADVelectron microscopy13.50Q2-84[»]
4GAQX-ray3.30Q1-84[»]
4GASX-ray3.30Q1-84[»]
4GD1X-ray3.00Q4-83[»]
4GD2X-ray3.00Q4-83[»]
4KIYX-ray2.90Q1-84[»]
4KJ0X-ray2.90Q1-84[»]
4KJ2X-ray2.90Q1-84[»]
4KJ4X-ray2.90Q1-84[»]
4KJ6X-ray2.90Q1-84[»]
4KJ8X-ray2.90Q1-84[»]
4KJAX-ray2.90Q1-84[»]
4KJCX-ray2.90Q1-84[»]
DisProtDP00242.
ProteinModelPortalP0AG63.
SMRP0AG63. Positions 6-84.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47952N.
IntActP0AG63. 1 interaction.
STRING511145.b3311.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0AG63.
PRIDEP0AG63.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76336; AAC76336; b3311.
BAE77980; BAE77980; BAE77980.
GeneID12934391.
947808.
KEGGecj:Y75_p3865.
eco:b3311.
PATRIC32122054. VBIEscCol129921_3404.

Organism-specific databases

EchoBASEEB0909.
EcoGeneEG10916. rpsQ.

Phylogenomic databases

eggNOGCOG0186.
HOGENOMHOG000231339.
KOK02961.
OMATIRECRP.
OrthoDBEOG63JRH2.
PhylomeDBP0AG63.
ProtClustDBPRK05610.

Enzyme and pathway databases

BioCycEcoCyc:EG10916-MONOMER.
ECOL316407:JW3273-MONOMER.

Gene expression databases

GenevestigatorP0AG63.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
HAMAPMF_01345_B. Ribosomal_S17_B.
InterProIPR012340. NA-bd_OB-fold.
IPR000266. Ribosomal_S17.
IPR019984. Ribosomal_S17_bac-type.
IPR019979. Ribosomal_S17_CS.
[Graphical view]
PANTHERPTHR10744. PTHR10744. 1 hit.
PfamPF00366. Ribosomal_S17. 1 hit.
[Graphical view]
PRINTSPR00973. RIBOSOMALS17.
ProDomPD001295. Ribosomal_S17. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR03635. S17_bact. 1 hit.
PROSITEPS00056. RIBOSOMAL_S17. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AG63.
PROP0AG63.

Entry information

Entry nameRS17_ECOLI
AccessionPrimary (citable) accession number: P0AG63
Secondary accession number(s): P02373, Q2M6X6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene