Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

  1. rRNA binding Source: EcoliWiki
  2. small ribosomal subunit rRNA binding Source: EcoliWiki
  3. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. response to antibiotic Source: EcoliWiki
  2. translation Source: UniProtKB-HAMAP
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.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10916. rpsQ.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 848330S ribosomal protein S17PRO_0000128456Add
BLAST

Proteomic databases

PaxDbiP0AG63.
PRIDEiP0AG63.

Expressioni

Gene expression databases

GenevestigatoriP0AG63.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit.

Protein-protein interaction databases

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

Structurei

Secondary structure

1
84
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114Combined sources
Beta strandi17 – 193Combined sources
Beta strandi22 – 254Combined sources
Beta strandi28 – 303Combined sources
Turni32 – 343Combined sources
Beta strandi37 – 393Combined sources
Beta strandi42 – 476Combined sources
Helixi49 – 513Combined sources
Beta strandi58 – 636Combined sources
Beta strandi68 – 703Combined sources
Beta strandi71 – 799Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 microscopy15.00Q6-84[»]
2GYBelectron microscopy15.00Q6-84[»]
2I2PX-ray3.22Q2-84[»]
2I2UX-ray3.22Q2-84[»]
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[»]
4PE9X-ray2.95Q4-83[»]
4PEAX-ray2.95Q4-83[»]
4TOLX-ray3.00Q4-83[»]
4TONX-ray3.00Q4-83[»]
4TOUX-ray2.90Q4-83[»]
4TOWX-ray2.90Q4-83[»]
4TP0X-ray2.90Q4-83[»]
4TP2X-ray2.90Q4-83[»]
4TP4X-ray2.90Q4-83[»]
4TP6X-ray2.90Q4-83[»]
4TP8X-ray2.80Q4-83[»]
4TPAX-ray2.80Q4-83[»]
4TPCX-ray2.80Q4-83[»]
4TPEX-ray2.80Q4-83[»]
4WAOX-ray3.09Q4-83[»]
4WAQX-ray3.09Q4-83[»]
DisProtiDP00242.
ProteinModelPortaliP0AG63.
SMRiP0AG63. Positions 6-84.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG63.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S17P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0186.
HOGENOMiHOG000231339.
InParanoidiP0AG63.
KOiK02961.
OMAiTIRECRP.
OrthoDBiEOG63JRH2.
PhylomeDBiP0AG63.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_01345_B. Ribosomal_S17_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR000266. Ribosomal_S17.
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. S17_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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 597CGIGDVV → GIGDVVC AA sequence (PubMed:344065)Curated
Sequence conflicti64 – 663CRP → RPC(PubMed:151587)Curated

Mass spectrometryi

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311H → P in neamine-resistant mutant nea301.
Natural varianti68 – 681S → F Prevents 30S subunit assembly at 42 degrees Celsius.

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.
YP_492121.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76336; AAC76336; b3311.
BAE77980; BAE77980; BAE77980.
GeneIDi12934391.
947808.
KEGGiecj:Y75_p3865.
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.
YP_492121.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 microscopy15.00Q6-84[»]
2GYBelectron microscopy15.00Q6-84[»]
2I2PX-ray3.22Q2-84[»]
2I2UX-ray3.22Q2-84[»]
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[»]
4PE9X-ray2.95Q4-83[»]
4PEAX-ray2.95Q4-83[»]
4TOLX-ray3.00Q4-83[»]
4TONX-ray3.00Q4-83[»]
4TOUX-ray2.90Q4-83[»]
4TOWX-ray2.90Q4-83[»]
4TP0X-ray2.90Q4-83[»]
4TP2X-ray2.90Q4-83[»]
4TP4X-ray2.90Q4-83[»]
4TP6X-ray2.90Q4-83[»]
4TP8X-ray2.80Q4-83[»]
4TPAX-ray2.80Q4-83[»]
4TPCX-ray2.80Q4-83[»]
4TPEX-ray2.80Q4-83[»]
4WAOX-ray3.09Q4-83[»]
4WAQX-ray3.09Q4-83[»]
DisProtiDP00242.
ProteinModelPortaliP0AG63.
SMRiP0AG63. Positions 6-84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0AG63.
PRIDEiP0AG63.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76336; AAC76336; b3311.
BAE77980; BAE77980; BAE77980.
GeneIDi12934391.
947808.
KEGGiecj:Y75_p3865.
eco:b3311.
PATRICi32122054. VBIEscCol129921_3404.

Organism-specific databases

EchoBASEiEB0909.
EcoGeneiEG10916. rpsQ.

Phylogenomic databases

eggNOGiCOG0186.
HOGENOMiHOG000231339.
InParanoidiP0AG63.
KOiK02961.
OMAiTIRECRP.
OrthoDBiEOG63JRH2.
PhylomeDBiP0AG63.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AG63.
PROiP0AG63.

Gene expression databases

GenevestigatoriP0AG63.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_01345_B. Ribosomal_S17_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR000266. Ribosomal_S17.
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. S17_bact. 1 hit.
PROSITEiPS00056. RIBOSOMAL_S17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

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: January 7, 2015
This is version 92 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

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.