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Protein

30S ribosomal protein S19

Gene

rpsS

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

Functioni

In the E.coli 70S ribosome in the initiation state (PubMed:12809609) it has been modeled to contact the 23S rRNA of the 50S subunit forming part of bridge B1a; this bridge is broken in the model with bound EF-G. The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states (PubMed:12859903), contacting alternately S13 or S19. In the 3.5 angstroms resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 bridge B1b are different, confirming the dynamic nature of this interaction. Bridge B1a is not visible in the crystallized ribosomes due to 23S rRNA disorder.3 Publications
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. Contacts the A site tRNA.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10918-MONOMER.
ECOL316407:JW3278-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S19
Gene namesi
Name:rpsS
Ordered Locus Names:b3316, JW3278
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10918. rpsS.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Chemistry

DrugBankiDB00759. Tetracycline.
DB00560. Tigecycline.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 929130S ribosomal protein S19PRO_0000129819Add
BLAST

Proteomic databases

PaxDbiP0A7U3.
PRIDEiP0A7U3.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Binds S13 and L5 and cross-links to the A site tRNA.

Protein-protein interaction databases

BioGridi852123. 1 interaction.
DIPiDIP-47904N.
IntActiP0A7U3. 30 interactions.
STRINGi511145.b3316.

Structurei

Secondary structure

1
92
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi13 – 208Combined sources
Turni21 – 255Combined sources
Beta strandi29 – 335Combined sources
Beta strandi37 – 393Combined sources
Helixi42 – 443Combined sources
Beta strandi48 – 525Combined sources
Beta strandi54 – 618Combined sources
Helixi64 – 663Combined sources
Beta strandi67 – 704Combined sources
Helixi71 – 744Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-S3-81[»]
2YKRelectron microscopy9.80S3-81[»]
3J9Yelectron microscopy3.90s1-92[»]
4A2Ielectron microscopy16.50S3-81[»]
4ADVelectron microscopy13.50S2-92[»]
4U1UX-ray2.95AS/CS3-81[»]
4U1VX-ray3.00AS/CS3-81[»]
4U20X-ray2.90AS/CS3-81[»]
4U24X-ray2.90AS/CS3-81[»]
4U25X-ray2.90AS/CS3-81[»]
4U26X-ray2.80AS/CS3-81[»]
4U27X-ray2.80AS/CS3-81[»]
4V47electron microscopy12.30BS2-92[»]
4V48electron microscopy11.50BS2-92[»]
4V4HX-ray3.46AS/CS1-92[»]
4V4QX-ray3.46AS/CS2-92[»]
4V4Velectron microscopy15.00AS2-88[»]
4V4Welectron microscopy15.00AS2-88[»]
4V50X-ray3.22AS/CS2-92[»]
4V52X-ray3.21AS/CS2-92[»]
4V53X-ray3.54AS/CS2-92[»]
4V54X-ray3.30AS/CS2-92[»]
4V55X-ray4.00AS/CS2-92[»]
4V56X-ray3.93AS/CS2-92[»]
4V57X-ray3.50AS/CS2-92[»]
4V5BX-ray3.74BS/DS2-92[»]
4V5Helectron microscopy5.80AS3-81[»]
4V5YX-ray4.45AS/CS2-92[»]
4V64X-ray3.50AS/CS2-92[»]
4V65electron microscopy9.00AL1-92[»]
4V66electron microscopy9.00AL1-92[»]
4V69electron microscopy6.70AS3-81[»]
4V6CX-ray3.19AS/CS1-92[»]
4V6DX-ray3.81AS/CS1-92[»]
4V6EX-ray3.71AS/CS1-92[»]
4V6Kelectron microscopy8.25BW1-92[»]
4V6Lelectron microscopy13.20AW1-92[»]
4V6Melectron microscopy7.10AS2-92[»]
4V6Nelectron microscopy12.10BV2-92[»]
4V6Oelectron microscopy14.70AV2-92[»]
4V6Pelectron microscopy13.50AV2-92[»]
4V6Qelectron microscopy11.50AV2-92[»]
4V6Relectron microscopy11.50AV2-92[»]
4V6Selectron microscopy13.10BU2-92[»]
4V6Telectron microscopy8.30AS3-81[»]
4V6Velectron microscopy9.80AS2-92[»]
4V6Yelectron microscopy12.00AS3-81[»]
4V6Zelectron microscopy12.00AS3-81[»]
4V70electron microscopy17.00AS3-81[»]
4V71electron microscopy20.00AS3-81[»]
4V72electron microscopy13.00AS3-81[»]
4V73electron microscopy15.00AS3-81[»]
4V74electron microscopy17.00AS3-81[»]
4V75electron microscopy12.00AS3-81[»]
4V76electron microscopy17.00AS3-81[»]
4V77electron microscopy17.00AS3-81[»]
4V78electron microscopy20.00AS3-81[»]
4V79electron microscopy15.00AS3-81[»]
4V7Aelectron microscopy9.00AS3-81[»]
4V7Belectron microscopy6.80AS1-92[»]
4V7Celectron microscopy7.60AS2-92[»]
4V7Delectron microscopy7.60BS2-92[»]
4V7Ielectron microscopy9.60BS1-92[»]
4V7SX-ray3.25AS/CS3-81[»]
4V7TX-ray3.19AS/CS3-81[»]
4V7UX-ray3.10AS/CS3-81[»]
4V7VX-ray3.29AS/CS3-81[»]
4V85X-ray3.20S1-92[»]
4V89X-ray3.70AS1-92[»]
4V9CX-ray3.30AS/CS1-92[»]
4V9DX-ray3.00AS/BS3-81[»]
4V9OX-ray2.90BS/DS/FS/HS1-92[»]
4V9PX-ray2.90BS/DS/FS/HS1-92[»]
4WF1X-ray3.09AS/CS3-81[»]
4WWWX-ray3.10QS/XS3-81[»]
4YBBX-ray2.10AS/BS3-81[»]
5AFIelectron microscopy2.90s1-92[»]
DisProtiDP00147.
ProteinModelPortaliP0A7U3.
SMRiP0A7U3. Positions 3-81.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7U3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S19P family.Curated

Phylogenomic databases

eggNOGiCOG0185.
HOGENOMiHOG000111560.
InParanoidiP0A7U3.
KOiK02965.
OMAiVHNGRQF.
OrthoDBiEOG61S365.
PhylomeDBiP0A7U3.

Family and domain databases

Gene3Di3.30.860.10. 1 hit.
HAMAPiMF_00531. Ribosomal_S19.
InterProiIPR002222. Ribosomal_S19.
IPR005732. Ribosomal_S19_bac-type.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
[Graphical view]
PANTHERiPTHR11880. PTHR11880. 1 hit.
PfamiPF00203. Ribosomal_S19. 1 hit.
[Graphical view]
PIRSFiPIRSF002144. Ribosomal_S19. 1 hit.
PRINTSiPR00975. RIBOSOMALS19.
SUPFAMiSSF54570. SSF54570. 1 hit.
TIGRFAMsiTIGR01050. rpsS_bact. 1 hit.
PROSITEiPS00323. RIBOSOMAL_S19. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7U3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRSLKKGPF IDLHLLKKVE KAVESGDKKP LRTWSRRSTI FPNMIGLTIA
60 70 80 90
VHNGRQHVPV FVTDEMVGHK LGEFAPTRTY RGHAADKKAK KK
Length:92
Mass (Da):10,430
Last modified:January 23, 2007 - v2
Checksum:i439F951848E95CB8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 437RSTIFPN → STIFPDR AA sequence (PubMed:348496).Curated
Sequence conflicti86 – 861D → N AA sequence (PubMed:348496).Curated

Mass spectrometryi

Molecular mass is 10299.6 Da from positions 2 - 92. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti83 – 831H → Y in MW145; suppresses a rimM deletion.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26464.1.
U18997 Genomic DNA. Translation: AAA58113.1.
U00096 Genomic DNA. Translation: AAC76341.1.
AP009048 Genomic DNA. Translation: BAE77975.1.
PIRiF23129. R3EC19.
RefSeqiNP_417775.1. NC_000913.3.
WP_001138117.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76341; AAC76341; b3316.
BAE77975; BAE77975; BAE77975.
GeneIDi947811.
KEGGieco:b3316.
PATRICi32122064. VBIEscCol129921_3409.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26464.1.
U18997 Genomic DNA. Translation: AAA58113.1.
U00096 Genomic DNA. Translation: AAC76341.1.
AP009048 Genomic DNA. Translation: BAE77975.1.
PIRiF23129. R3EC19.
RefSeqiNP_417775.1. NC_000913.3.
WP_001138117.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-S3-81[»]
2YKRelectron microscopy9.80S3-81[»]
3J9Yelectron microscopy3.90s1-92[»]
4A2Ielectron microscopy16.50S3-81[»]
4ADVelectron microscopy13.50S2-92[»]
4U1UX-ray2.95AS/CS3-81[»]
4U1VX-ray3.00AS/CS3-81[»]
4U20X-ray2.90AS/CS3-81[»]
4U24X-ray2.90AS/CS3-81[»]
4U25X-ray2.90AS/CS3-81[»]
4U26X-ray2.80AS/CS3-81[»]
4U27X-ray2.80AS/CS3-81[»]
4V47electron microscopy12.30BS2-92[»]
4V48electron microscopy11.50BS2-92[»]
4V4HX-ray3.46AS/CS1-92[»]
4V4QX-ray3.46AS/CS2-92[»]
4V4Velectron microscopy15.00AS2-88[»]
4V4Welectron microscopy15.00AS2-88[»]
4V50X-ray3.22AS/CS2-92[»]
4V52X-ray3.21AS/CS2-92[»]
4V53X-ray3.54AS/CS2-92[»]
4V54X-ray3.30AS/CS2-92[»]
4V55X-ray4.00AS/CS2-92[»]
4V56X-ray3.93AS/CS2-92[»]
4V57X-ray3.50AS/CS2-92[»]
4V5BX-ray3.74BS/DS2-92[»]
4V5Helectron microscopy5.80AS3-81[»]
4V5YX-ray4.45AS/CS2-92[»]
4V64X-ray3.50AS/CS2-92[»]
4V65electron microscopy9.00AL1-92[»]
4V66electron microscopy9.00AL1-92[»]
4V69electron microscopy6.70AS3-81[»]
4V6CX-ray3.19AS/CS1-92[»]
4V6DX-ray3.81AS/CS1-92[»]
4V6EX-ray3.71AS/CS1-92[»]
4V6Kelectron microscopy8.25BW1-92[»]
4V6Lelectron microscopy13.20AW1-92[»]
4V6Melectron microscopy7.10AS2-92[»]
4V6Nelectron microscopy12.10BV2-92[»]
4V6Oelectron microscopy14.70AV2-92[»]
4V6Pelectron microscopy13.50AV2-92[»]
4V6Qelectron microscopy11.50AV2-92[»]
4V6Relectron microscopy11.50AV2-92[»]
4V6Selectron microscopy13.10BU2-92[»]
4V6Telectron microscopy8.30AS3-81[»]
4V6Velectron microscopy9.80AS2-92[»]
4V6Yelectron microscopy12.00AS3-81[»]
4V6Zelectron microscopy12.00AS3-81[»]
4V70electron microscopy17.00AS3-81[»]
4V71electron microscopy20.00AS3-81[»]
4V72electron microscopy13.00AS3-81[»]
4V73electron microscopy15.00AS3-81[»]
4V74electron microscopy17.00AS3-81[»]
4V75electron microscopy12.00AS3-81[»]
4V76electron microscopy17.00AS3-81[»]
4V77electron microscopy17.00AS3-81[»]
4V78electron microscopy20.00AS3-81[»]
4V79electron microscopy15.00AS3-81[»]
4V7Aelectron microscopy9.00AS3-81[»]
4V7Belectron microscopy6.80AS1-92[»]
4V7Celectron microscopy7.60AS2-92[»]
4V7Delectron microscopy7.60BS2-92[»]
4V7Ielectron microscopy9.60BS1-92[»]
4V7SX-ray3.25AS/CS3-81[»]
4V7TX-ray3.19AS/CS3-81[»]
4V7UX-ray3.10AS/CS3-81[»]
4V7VX-ray3.29AS/CS3-81[»]
4V85X-ray3.20S1-92[»]
4V89X-ray3.70AS1-92[»]
4V9CX-ray3.30AS/CS1-92[»]
4V9DX-ray3.00AS/BS3-81[»]
4V9OX-ray2.90BS/DS/FS/HS1-92[»]
4V9PX-ray2.90BS/DS/FS/HS1-92[»]
4WF1X-ray3.09AS/CS3-81[»]
4WWWX-ray3.10QS/XS3-81[»]
4YBBX-ray2.10AS/BS3-81[»]
5AFIelectron microscopy2.90s1-92[»]
DisProtiDP00147.
ProteinModelPortaliP0A7U3.
SMRiP0A7U3. Positions 3-81.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852123. 1 interaction.
DIPiDIP-47904N.
IntActiP0A7U3. 30 interactions.
STRINGi511145.b3316.

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB00759. Tetracycline.
DB00560. Tigecycline.

Proteomic databases

PaxDbiP0A7U3.
PRIDEiP0A7U3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76341; AAC76341; b3316.
BAE77975; BAE77975; BAE77975.
GeneIDi947811.
KEGGieco:b3316.
PATRICi32122064. VBIEscCol129921_3409.

Organism-specific databases

EchoBASEiEB0911.
EcoGeneiEG10918. rpsS.

Phylogenomic databases

eggNOGiCOG0185.
HOGENOMiHOG000111560.
InParanoidiP0A7U3.
KOiK02965.
OMAiVHNGRQF.
OrthoDBiEOG61S365.
PhylomeDBiP0A7U3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10918-MONOMER.
ECOL316407:JW3278-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7U3.
PROiP0A7U3.

Family and domain databases

Gene3Di3.30.860.10. 1 hit.
HAMAPiMF_00531. Ribosomal_S19.
InterProiIPR002222. Ribosomal_S19.
IPR005732. Ribosomal_S19_bac-type.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
[Graphical view]
PANTHERiPTHR11880. PTHR11880. 1 hit.
PfamiPF00203. Ribosomal_S19. 1 hit.
[Graphical view]
PIRSFiPIRSF002144. Ribosomal_S19. 1 hit.
PRINTSiPR00975. RIBOSOMALS19.
SUPFAMiSSF54570. SSF54570. 1 hit.
TIGRFAMsiTIGR01050. rpsS_bact. 1 hit.
PROSITEiPS00323. RIBOSOMAL_S19. 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. "Primary structure of protein S19 from the small ribosomal subunit of Escherichia coli."
    Yaguchi M., Wittmann H.G.
    FEBS Lett. 88:227-230(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-92.
    Strain: K.
  5. "Identification of a cross-link in the Escherichia coli ribosomal protein pair S13-S19 at the amino acid level."
    Pohl T., Wittmann-Liebold B.
    J. Biol. Chem. 263:4293-4301(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 66-70, CROSS-LINKING TO S13.
    Strain: K12 / A19.
  6. "The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
    Osswald M., Doering T., Brimacombe R.
    Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
    Strain: MRE-600.
  7. "The PRC-barrel domain of the ribosome maturation protein RimM mediates binding to ribosomal protein S19 in the 30S ribosomal subunits."
    Loevgren J.M., Bylund G.O., Srivastava M.K., Lundberg L.A.C., Persson O.P., Wingsle G., Wikstroem P.M.
    RNA 10:1798-1812(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ABILITY OF VARIANT MW145 TO SUPPRESS A RIMM DELETION.
    Strain: MW100.
  8. "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.
  9. "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.
  10. "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), INTERSUBUNIT BRIDGE FORMATION.
    Strain: MRE-600.
  11. Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES INCLUDING BRIDGE CHANGES UPON TRANSLOCATION.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES INCLUDING THE INTERSUBUNIT BRIDGE B1B.
    Strain: MRE-600.

Entry informationi

Entry nameiRS19_ECOLI
AccessioniPrimary (citable) accession number: P0A7U3
Secondary accession number(s): P02375, Q2M6Y1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 22, 2015
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

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.