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P0A7T7

- RS18_ECOLI

UniProt

P0A7T7 - RS18_ECOLI

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Protein

30S ribosomal protein S18

Gene
rpsR, b4202, JW4160
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.UniRule annotation

GO - Molecular functioni

  1. mRNA 5'-UTR binding Source: EcoCyc
  2. protein binding Source: IntAct
  3. small ribosomal subunit rRNA binding Source: EcoCyc
  4. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10917-MONOMER.
ECOL316407:JW4160-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S18
Gene namesi
Name:rpsR
Ordered Locus Names:b4202, JW4160
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10917. rpsR.

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 – 757430S ribosomal protein S18UniRule annotationPRO_0000111153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineUniRule annotation

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A7T7.
PRIDEiP0A7T7.

Expressioni

Gene expression databases

GenevestigatoriP0A7T7.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein S6.

Binary interactionsi

WithEntry#Exp.IntActNotes
rpsFP023584EBI-548844,EBI-543068

Protein-protein interaction databases

DIPiDIP-47889N.
IntActiP0A7T7. 26 interactions.
MINTiMINT-1247424.
STRINGi511145.b4202.

Structurei

Secondary structure

1
75
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 243
Helixi26 – 294
Helixi30 – 323
Beta strandi37 – 393
Helixi42 – 454
Helixi49 – 6315
Turni64 – 663
Beta strandi70 – 723

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-R5-75[»]
1P6Gelectron microscopy12.30R2-75[»]
1P87electron microscopy11.50R2-75[»]
1VS5X-ray3.46R1-75[»]
1VS7X-ray3.46R1-75[»]
2AVYX-ray3.46R2-75[»]
2AW7X-ray3.46R2-75[»]
2GY9electron microscopy15.00R7-75[»]
2GYBelectron microscopy15.00R7-75[»]
2I2PX-ray3.22R2-75[»]
2I2UX-ray3.22R2-75[»]
2QALX-ray3.21R2-75[»]
2QANX-ray3.21R2-75[»]
2QB9X-ray3.54R2-75[»]
2QBBX-ray3.54R2-75[»]
2QBDX-ray3.30R2-75[»]
2QBFX-ray3.30R2-75[»]
2QBHX-ray4.00R2-75[»]
2QBJX-ray4.00R2-75[»]
2QOUX-ray3.93R2-75[»]
2QOWX-ray3.93R2-75[»]
2QOYX-ray3.50R2-75[»]
2QP0X-ray3.50R2-75[»]
2VHOX-ray3.74R2-75[»]
2VHPX-ray3.74R2-75[»]
2WWLelectron microscopy5.80R20-74[»]
2YKRelectron microscopy9.80R20-74[»]
2Z4KX-ray4.45R2-75[»]
2Z4MX-ray4.45R2-75[»]
3DF1X-ray3.50R2-74[»]
3DF3X-ray3.50R2-74[»]
3E1Aelectron microscopy-K1-75[»]
3E1Celectron microscopy-K1-75[»]
3FIHelectron microscopy6.70R20-74[»]
3I1MX-ray3.19R1-75[»]
3I1OX-ray3.19R1-75[»]
3I1QX-ray3.81R1-75[»]
3I1SX-ray3.81R1-75[»]
3I1ZX-ray3.71R1-75[»]
3I21X-ray3.71R1-75[»]
3IZVelectron microscopy-V1-75[»]
3IZWelectron microscopy-V1-75[»]
3J00electron microscopy-R2-75[»]
3J0Uelectron microscopy12.10U2-75[»]
3J0Velectron microscopy14.70U2-75[»]
3J0Xelectron microscopy13.50U2-75[»]
3J0Zelectron microscopy11.50U2-75[»]
3J10electron microscopy11.50U2-75[»]
3J13electron microscopy13.10T2-75[»]
3J18electron microscopy8.30R20-74[»]
3J36electron microscopy9.80R2-75[»]
3J4Velectron microscopy12.00R20-74[»]
3J4Welectron microscopy12.00R20-74[»]
3J4Yelectron microscopy17.00R20-74[»]
3J4Zelectron microscopy20.00R20-74[»]
3J53electron microscopy13.00R20-74[»]
3J55electron microscopy15.00R20-74[»]
3J57electron microscopy17.00R20-74[»]
3J59electron microscopy12.00R20-74[»]
3J5Belectron microscopy17.00R20-74[»]
3J5Delectron microscopy17.00R20-74[»]
3J5Felectron microscopy20.00R20-74[»]
3J5Helectron microscopy15.00R20-74[»]
3J5Jelectron microscopy9.00R20-74[»]
3J5Nelectron microscopy6.80R1-75[»]
3J5Telectron microscopy7.60R2-75[»]
3J5Xelectron microscopy7.60R2-75[»]
3KC4electron microscopy-R1-75[»]
3OAQX-ray3.25R20-74[»]
3OARX-ray3.25R20-74[»]
3OFAX-ray3.19R20-74[»]
3OFBX-ray3.19R20-74[»]
3OFOX-ray3.10R20-74[»]
3OFPX-ray3.10R20-74[»]
3OFXX-ray3.29R20-74[»]
3OFYX-ray3.29R20-74[»]
3OR9X-ray3.30R1-75[»]
3ORAX-ray3.30R1-75[»]
3SFSX-ray3.20R1-75[»]
3UOQX-ray3.70R1-75[»]
4A2Ielectron microscopy16.50R20-74[»]
4ADVelectron microscopy13.50R2-75[»]
4GAQX-ray3.30R1-75[»]
4GASX-ray3.30R1-75[»]
4GD1X-ray3.00R20-74[»]
4GD2X-ray3.00R20-74[»]
4KIYX-ray2.90R1-75[»]
4KJ0X-ray2.90R1-75[»]
4KJ2X-ray2.90R1-75[»]
4KJ4X-ray2.90R1-75[»]
4KJ6X-ray2.90R1-75[»]
4KJ8X-ray2.90R1-75[»]
4KJAX-ray2.90R1-75[»]
4KJCX-ray2.90R1-75[»]
DisProtiDP00146.
ProteinModelPortaliP0A7T7.
SMRiP0A7T7. Positions 2-75.

Miscellaneous databases

EvolutionaryTraceiP0A7T7.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0238.
HOGENOMiHOG000218466.
KOiK02963.
OMAiPRRIYGT.
OrthoDBiEOG6PCQ4R.
PhylomeDBiP0A7T7.

Family and domain databases

Gene3Di4.10.640.10. 1 hit.
HAMAPiMF_00270. Ribosomal_S18.
InterProiIPR001648. Ribosomal_S18.
IPR018275. Ribosomal_S18_CS.
[Graphical view]
PANTHERiPTHR13479. PTHR13479. 1 hit.
PfamiPF01084. Ribosomal_S18. 1 hit.
[Graphical view]
PRINTSiPR00974. RIBOSOMALS18.
ProDomiPD002239. Ribosomal_S18. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46911. SSF46911. 1 hit.
TIGRFAMsiTIGR00165. S18. 1 hit.
PROSITEiPS00057. RIBOSOMAL_S18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7T7-1 [UniParc]FASTAAdd to Basket

« Hide

MARYFRRRKF CRFTAEGVQE IDYKDIATLK NYITESGKIV PSRITGTRAK   50
YQRQLARAIK RARYLSLLPY TDRHQ 75
Length:75
Mass (Da):8,986
Last modified:January 23, 2007 - v2
Checksum:iAB2E8288901B73B8
GO

Mass spectrometryi

Molecular mass is 8897.0 Da from positions 2 - 75. Determined by MALDI. 1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241K → E AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04022 Genomic DNA. Translation: CAA27654.1.
U14003 Genomic DNA. Translation: AAA97098.1.
U00096 Genomic DNA. Translation: AAC77159.1.
AP009048 Genomic DNA. Translation: BAE78203.1.
PIRiS56427. R3EC18.
RefSeqiNP_418623.1. NC_000913.3.
YP_492344.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77159; AAC77159; b4202.
BAE78203; BAE78203; BAE78203.
GeneIDi12930640.
948721.
KEGGiecj:Y75_p4088.
eco:b4202.
PATRICi32123979. VBIEscCol129921_4334.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04022 Genomic DNA. Translation: CAA27654.1 .
U14003 Genomic DNA. Translation: AAA97098.1 .
U00096 Genomic DNA. Translation: AAC77159.1 .
AP009048 Genomic DNA. Translation: BAE78203.1 .
PIRi S56427. R3EC18.
RefSeqi NP_418623.1. NC_000913.3.
YP_492344.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M5G model - R 5-75 [» ]
1P6G electron microscopy 12.30 R 2-75 [» ]
1P87 electron microscopy 11.50 R 2-75 [» ]
1VS5 X-ray 3.46 R 1-75 [» ]
1VS7 X-ray 3.46 R 1-75 [» ]
2AVY X-ray 3.46 R 2-75 [» ]
2AW7 X-ray 3.46 R 2-75 [» ]
2GY9 electron microscopy 15.00 R 7-75 [» ]
2GYB electron microscopy 15.00 R 7-75 [» ]
2I2P X-ray 3.22 R 2-75 [» ]
2I2U X-ray 3.22 R 2-75 [» ]
2QAL X-ray 3.21 R 2-75 [» ]
2QAN X-ray 3.21 R 2-75 [» ]
2QB9 X-ray 3.54 R 2-75 [» ]
2QBB X-ray 3.54 R 2-75 [» ]
2QBD X-ray 3.30 R 2-75 [» ]
2QBF X-ray 3.30 R 2-75 [» ]
2QBH X-ray 4.00 R 2-75 [» ]
2QBJ X-ray 4.00 R 2-75 [» ]
2QOU X-ray 3.93 R 2-75 [» ]
2QOW X-ray 3.93 R 2-75 [» ]
2QOY X-ray 3.50 R 2-75 [» ]
2QP0 X-ray 3.50 R 2-75 [» ]
2VHO X-ray 3.74 R 2-75 [» ]
2VHP X-ray 3.74 R 2-75 [» ]
2WWL electron microscopy 5.80 R 20-74 [» ]
2YKR electron microscopy 9.80 R 20-74 [» ]
2Z4K X-ray 4.45 R 2-75 [» ]
2Z4M X-ray 4.45 R 2-75 [» ]
3DF1 X-ray 3.50 R 2-74 [» ]
3DF3 X-ray 3.50 R 2-74 [» ]
3E1A electron microscopy - K 1-75 [» ]
3E1C electron microscopy - K 1-75 [» ]
3FIH electron microscopy 6.70 R 20-74 [» ]
3I1M X-ray 3.19 R 1-75 [» ]
3I1O X-ray 3.19 R 1-75 [» ]
3I1Q X-ray 3.81 R 1-75 [» ]
3I1S X-ray 3.81 R 1-75 [» ]
3I1Z X-ray 3.71 R 1-75 [» ]
3I21 X-ray 3.71 R 1-75 [» ]
3IZV electron microscopy - V 1-75 [» ]
3IZW electron microscopy - V 1-75 [» ]
3J00 electron microscopy - R 2-75 [» ]
3J0U electron microscopy 12.10 U 2-75 [» ]
3J0V electron microscopy 14.70 U 2-75 [» ]
3J0X electron microscopy 13.50 U 2-75 [» ]
3J0Z electron microscopy 11.50 U 2-75 [» ]
3J10 electron microscopy 11.50 U 2-75 [» ]
3J13 electron microscopy 13.10 T 2-75 [» ]
3J18 electron microscopy 8.30 R 20-74 [» ]
3J36 electron microscopy 9.80 R 2-75 [» ]
3J4V electron microscopy 12.00 R 20-74 [» ]
3J4W electron microscopy 12.00 R 20-74 [» ]
3J4Y electron microscopy 17.00 R 20-74 [» ]
3J4Z electron microscopy 20.00 R 20-74 [» ]
3J53 electron microscopy 13.00 R 20-74 [» ]
3J55 electron microscopy 15.00 R 20-74 [» ]
3J57 electron microscopy 17.00 R 20-74 [» ]
3J59 electron microscopy 12.00 R 20-74 [» ]
3J5B electron microscopy 17.00 R 20-74 [» ]
3J5D electron microscopy 17.00 R 20-74 [» ]
3J5F electron microscopy 20.00 R 20-74 [» ]
3J5H electron microscopy 15.00 R 20-74 [» ]
3J5J electron microscopy 9.00 R 20-74 [» ]
3J5N electron microscopy 6.80 R 1-75 [» ]
3J5T electron microscopy 7.60 R 2-75 [» ]
3J5X electron microscopy 7.60 R 2-75 [» ]
3KC4 electron microscopy - R 1-75 [» ]
3OAQ X-ray 3.25 R 20-74 [» ]
3OAR X-ray 3.25 R 20-74 [» ]
3OFA X-ray 3.19 R 20-74 [» ]
3OFB X-ray 3.19 R 20-74 [» ]
3OFO X-ray 3.10 R 20-74 [» ]
3OFP X-ray 3.10 R 20-74 [» ]
3OFX X-ray 3.29 R 20-74 [» ]
3OFY X-ray 3.29 R 20-74 [» ]
3OR9 X-ray 3.30 R 1-75 [» ]
3ORA X-ray 3.30 R 1-75 [» ]
3SFS X-ray 3.20 R 1-75 [» ]
3UOQ X-ray 3.70 R 1-75 [» ]
4A2I electron microscopy 16.50 R 20-74 [» ]
4ADV electron microscopy 13.50 R 2-75 [» ]
4GAQ X-ray 3.30 R 1-75 [» ]
4GAS X-ray 3.30 R 1-75 [» ]
4GD1 X-ray 3.00 R 20-74 [» ]
4GD2 X-ray 3.00 R 20-74 [» ]
4KIY X-ray 2.90 R 1-75 [» ]
4KJ0 X-ray 2.90 R 1-75 [» ]
4KJ2 X-ray 2.90 R 1-75 [» ]
4KJ4 X-ray 2.90 R 1-75 [» ]
4KJ6 X-ray 2.90 R 1-75 [» ]
4KJ8 X-ray 2.90 R 1-75 [» ]
4KJA X-ray 2.90 R 1-75 [» ]
4KJC X-ray 2.90 R 1-75 [» ]
DisProti DP00146.
ProteinModelPortali P0A7T7.
SMRi P0A7T7. Positions 2-75.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47889N.
IntActi P0A7T7. 26 interactions.
MINTi MINT-1247424.
STRINGi 511145.b4202.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7T7.
PRIDEi P0A7T7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77159 ; AAC77159 ; b4202 .
BAE78203 ; BAE78203 ; BAE78203 .
GeneIDi 12930640.
948721.
KEGGi ecj:Y75_p4088.
eco:b4202.
PATRICi 32123979. VBIEscCol129921_4334.

Organism-specific databases

EchoBASEi EB0910.
EcoGenei EG10917. rpsR.

Phylogenomic databases

eggNOGi COG0238.
HOGENOMi HOG000218466.
KOi K02963.
OMAi PRRIYGT.
OrthoDBi EOG6PCQ4R.
PhylomeDBi P0A7T7.

Enzyme and pathway databases

BioCyci EcoCyc:EG10917-MONOMER.
ECOL316407:JW4160-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7T7.
PROi P0A7T7.

Gene expression databases

Genevestigatori P0A7T7.

Family and domain databases

Gene3Di 4.10.640.10. 1 hit.
HAMAPi MF_00270. Ribosomal_S18.
InterProi IPR001648. Ribosomal_S18.
IPR018275. Ribosomal_S18_CS.
[Graphical view ]
PANTHERi PTHR13479. PTHR13479. 1 hit.
Pfami PF01084. Ribosomal_S18. 1 hit.
[Graphical view ]
PRINTSi PR00974. RIBOSOMALS18.
ProDomi PD002239. Ribosomal_S18. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF46911. SSF46911. 1 hit.
TIGRFAMsi TIGR00165. S18. 1 hit.
PROSITEi PS00057. RIBOSOMAL_S18. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of an Escherichia coli chromosomal region containing the genes for ribosomal proteins S6, S18, L9 and an open reading frame."
    Schnier J., Kitakawa M., Isono K.
    Mol. Gen. Genet. 204:126-132(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Primary structure of protein S18 from the small Escherichia coli ribosomal subunit."
    Yaguchi M.
    FEBS Lett. 59:217-220(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-75.
    Strain: K.
  6. "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 31-38, CROSS-LINKING TO RRNA.
    Strain: MRE-600.
  7. "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.
  8. "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.
  9. "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.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS18_ECOLI
AccessioniPrimary (citable) accession number: P0A7T7
Secondary accession number(s): P02374, Q2M6A3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 98 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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