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Protein

30S ribosomal protein S18

Gene

rpsR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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.

GO - Molecular functioni

  • mRNA 5'-UTR binding Source: EcoCyc
  • small ribosomal subunit rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10917. rpsR.

Subcellular locationi

GO - Cellular componenti

  • 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 S18PRO_0000111153Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A7T7.
PRIDEiP0A7T7.

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 – 243Combined sources
Helixi26 – 294Combined sources
Helixi30 – 323Combined sources
Beta strandi37 – 393Combined sources
Helixi42 – 454Combined sources
Helixi49 – 6416Combined sources
Turni65 – 673Combined sources
Beta strandi70 – 723Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-R5-75[»]
2YKRelectron microscopy9.80R20-74[»]
3J9Yelectron microscopy3.90r1-75[»]
4A2Ielectron microscopy16.50R20-74[»]
4ADVelectron microscopy13.50R2-75[»]
4U1UX-ray2.95AR/CR20-74[»]
4U1VX-ray3.00AR/CR20-74[»]
4U20X-ray2.90AR/CR20-74[»]
4U24X-ray2.90AR/CR20-74[»]
4U25X-ray2.90AR/CR20-74[»]
4U26X-ray2.80AR/CR20-74[»]
4U27X-ray2.80AR/CR20-74[»]
4V47electron microscopy12.30BR2-75[»]
4V48electron microscopy11.50BR2-75[»]
4V4HX-ray3.46AR/CR1-75[»]
4V4QX-ray3.46AR/CR2-75[»]
4V4Velectron microscopy15.00AR7-75[»]
4V4Welectron microscopy15.00AR7-75[»]
4V50X-ray3.22AR/CR2-75[»]
4V52X-ray3.21AR/CR2-75[»]
4V53X-ray3.54AR/CR2-75[»]
4V54X-ray3.30AR/CR2-75[»]
4V55X-ray4.00AR/CR2-75[»]
4V56X-ray3.93AR/CR2-75[»]
4V57X-ray3.50AR/CR2-75[»]
4V5BX-ray3.74BR/DR2-75[»]
4V5Helectron microscopy5.80AR20-74[»]
4V5YX-ray4.45AR/CR2-75[»]
4V64X-ray3.50AR/CR2-75[»]
4V65electron microscopy9.00AK1-75[»]
4V66electron microscopy9.00AK1-75[»]
4V69electron microscopy6.70AR20-74[»]
4V6CX-ray3.19AR/CR1-75[»]
4V6DX-ray3.81AR/CR1-75[»]
4V6EX-ray3.71AR/CR1-75[»]
4V6Kelectron microscopy8.25BV1-75[»]
4V6Lelectron microscopy13.20AV1-75[»]
4V6Melectron microscopy7.10AR2-75[»]
4V6Nelectron microscopy12.10BU2-75[»]
4V6Oelectron microscopy14.70AU2-75[»]
4V6Pelectron microscopy13.50AU2-75[»]
4V6Qelectron microscopy11.50AU2-75[»]
4V6Relectron microscopy11.50AU2-75[»]
4V6Selectron microscopy13.10BT2-75[»]
4V6Telectron microscopy8.30AR20-74[»]
4V6Velectron microscopy9.80R2-75[»]
4V6Yelectron microscopy12.00AR20-74[»]
4V6Zelectron microscopy12.00AR20-74[»]
4V70electron microscopy17.00AR20-74[»]
4V71electron microscopy20.00AR20-74[»]
4V72electron microscopy13.00AR20-74[»]
4V73electron microscopy15.00AR20-74[»]
4V74electron microscopy17.00AR20-74[»]
4V75electron microscopy12.00AR20-74[»]
4V76electron microscopy17.00AR20-74[»]
4V77electron microscopy17.00AR20-74[»]
4V78electron microscopy20.00AR20-74[»]
4V79electron microscopy15.00AR20-74[»]
4V7Aelectron microscopy9.00AR20-74[»]
4V7Belectron microscopy6.80AR1-75[»]
4V7Celectron microscopy7.60AR2-75[»]
4V7Delectron microscopy7.60BR2-75[»]
4V7Ielectron microscopy9.60BR1-75[»]
4V7SX-ray3.25AR/CR20-74[»]
4V7TX-ray3.19AR/CR20-74[»]
4V7UX-ray3.10AR/CR20-74[»]
4V7VX-ray3.29AR/CR20-74[»]
4V85X-ray3.20R1-75[»]
4V89X-ray3.70AR1-75[»]
4V9CX-ray3.30AR/CR1-75[»]
4V9DX-ray3.00AR/BR20-74[»]
4V9OX-ray2.90BR/DR/FR/HR1-75[»]
4V9PX-ray2.90BR/DR/FR/HR1-75[»]
4WF1X-ray3.09AR/CR20-74[»]
4WWWX-ray3.10QR/XR20-74[»]
4YBBX-ray2.10AR/BR20-74[»]
5AFIelectron microscopy2.90r1-75[»]
DisProtiDP00146.
ProteinModelPortaliP0A7T7.
SMRiP0A7T7. Positions 20-74.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7T7.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S18P family.Curated

Phylogenomic databases

eggNOGiCOG0238.
HOGENOMiHOG000218466.
InParanoidiP0A7T7.
KOiK02963.
OMAiYRRRKSC.
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

        10         20         30         40         50
MARYFRRRKF CRFTAEGVQE IDYKDIATLK NYITESGKIV PSRITGTRAK
60 70
YQRQLARAIK RARYLSLLPY TDRHQ
Length:75
Mass (Da):8,986
Last modified:January 23, 2007 - v2
Checksum:iAB2E8288901B73B8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241K → E AA sequence (PubMed:776663).Curated

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Genome annotation databases

EnsemblBacteriaiAAC77159; AAC77159; b4202.
BAE78203; BAE78203; BAE78203.
GeneIDi948721.
KEGGiecj:Y75_p4088.
eco:b4202.
PATRICi32123979. VBIEscCol129921_4334.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-R5-75[»]
2YKRelectron microscopy9.80R20-74[»]
3J9Yelectron microscopy3.90r1-75[»]
4A2Ielectron microscopy16.50R20-74[»]
4ADVelectron microscopy13.50R2-75[»]
4U1UX-ray2.95AR/CR20-74[»]
4U1VX-ray3.00AR/CR20-74[»]
4U20X-ray2.90AR/CR20-74[»]
4U24X-ray2.90AR/CR20-74[»]
4U25X-ray2.90AR/CR20-74[»]
4U26X-ray2.80AR/CR20-74[»]
4U27X-ray2.80AR/CR20-74[»]
4V47electron microscopy12.30BR2-75[»]
4V48electron microscopy11.50BR2-75[»]
4V4HX-ray3.46AR/CR1-75[»]
4V4QX-ray3.46AR/CR2-75[»]
4V4Velectron microscopy15.00AR7-75[»]
4V4Welectron microscopy15.00AR7-75[»]
4V50X-ray3.22AR/CR2-75[»]
4V52X-ray3.21AR/CR2-75[»]
4V53X-ray3.54AR/CR2-75[»]
4V54X-ray3.30AR/CR2-75[»]
4V55X-ray4.00AR/CR2-75[»]
4V56X-ray3.93AR/CR2-75[»]
4V57X-ray3.50AR/CR2-75[»]
4V5BX-ray3.74BR/DR2-75[»]
4V5Helectron microscopy5.80AR20-74[»]
4V5YX-ray4.45AR/CR2-75[»]
4V64X-ray3.50AR/CR2-75[»]
4V65electron microscopy9.00AK1-75[»]
4V66electron microscopy9.00AK1-75[»]
4V69electron microscopy6.70AR20-74[»]
4V6CX-ray3.19AR/CR1-75[»]
4V6DX-ray3.81AR/CR1-75[»]
4V6EX-ray3.71AR/CR1-75[»]
4V6Kelectron microscopy8.25BV1-75[»]
4V6Lelectron microscopy13.20AV1-75[»]
4V6Melectron microscopy7.10AR2-75[»]
4V6Nelectron microscopy12.10BU2-75[»]
4V6Oelectron microscopy14.70AU2-75[»]
4V6Pelectron microscopy13.50AU2-75[»]
4V6Qelectron microscopy11.50AU2-75[»]
4V6Relectron microscopy11.50AU2-75[»]
4V6Selectron microscopy13.10BT2-75[»]
4V6Telectron microscopy8.30AR20-74[»]
4V6Velectron microscopy9.80R2-75[»]
4V6Yelectron microscopy12.00AR20-74[»]
4V6Zelectron microscopy12.00AR20-74[»]
4V70electron microscopy17.00AR20-74[»]
4V71electron microscopy20.00AR20-74[»]
4V72electron microscopy13.00AR20-74[»]
4V73electron microscopy15.00AR20-74[»]
4V74electron microscopy17.00AR20-74[»]
4V75electron microscopy12.00AR20-74[»]
4V76electron microscopy17.00AR20-74[»]
4V77electron microscopy17.00AR20-74[»]
4V78electron microscopy20.00AR20-74[»]
4V79electron microscopy15.00AR20-74[»]
4V7Aelectron microscopy9.00AR20-74[»]
4V7Belectron microscopy6.80AR1-75[»]
4V7Celectron microscopy7.60AR2-75[»]
4V7Delectron microscopy7.60BR2-75[»]
4V7Ielectron microscopy9.60BR1-75[»]
4V7SX-ray3.25AR/CR20-74[»]
4V7TX-ray3.19AR/CR20-74[»]
4V7UX-ray3.10AR/CR20-74[»]
4V7VX-ray3.29AR/CR20-74[»]
4V85X-ray3.20R1-75[»]
4V89X-ray3.70AR1-75[»]
4V9CX-ray3.30AR/CR1-75[»]
4V9DX-ray3.00AR/BR20-74[»]
4V9OX-ray2.90BR/DR/FR/HR1-75[»]
4V9PX-ray2.90BR/DR/FR/HR1-75[»]
4WF1X-ray3.09AR/CR20-74[»]
4WWWX-ray3.10QR/XR20-74[»]
4YBBX-ray2.10AR/BR20-74[»]
5AFIelectron microscopy2.90r1-75[»]
DisProtiDP00146.
ProteinModelPortaliP0A7T7.
SMRiP0A7T7. Positions 20-74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0A7T7.
PRIDEiP0A7T7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77159; AAC77159; b4202.
BAE78203; BAE78203; BAE78203.
GeneIDi948721.
KEGGiecj:Y75_p4088.
eco:b4202.
PATRICi32123979. VBIEscCol129921_4334.

Organism-specific databases

EchoBASEiEB0910.
EcoGeneiEG10917. rpsR.

Phylogenomic databases

eggNOGiCOG0238.
HOGENOMiHOG000218466.
InParanoidiP0A7T7.
KOiK02963.
OMAiYRRRKSC.
OrthoDBiEOG6PCQ4R.
PhylomeDBiP0A7T7.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7T7.
PROiP0A7T7.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 108 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

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.