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P0A7U3 (RS19_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. 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 S19
Gene names
Name:rpsS
Ordered Locus Names:b3316, JW3278
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length92 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In the E.coli 70S ribosome in the initiation state (Ref.10) 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 (Ref.11), contacting alternately S13 or S19. In the 3.5 angstroms resolved ribosome structures (Ref.12) 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. HAMAP-Rule MF_00531

Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. Contacts the A site tRNA. HAMAP-Rule MF_00531

Subunit structure

Part of the 30S ribosomal subunit. Binds S13 and L5 and cross-links to the A site tRNA. Ref.10 Ref.12

Sequence similarities

Belongs to the ribosomal protein S19P family.

Mass spectrometry

Molecular mass is 10299.6 Da from positions 2 - 92. Determined by MALDI. Ref.8

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 929130S ribosomal protein S19 HAMAP-Rule MF_00531
PRO_0000129819

Natural variations

Natural variant831H → Y in MW145; suppresses a rimM deletion.

Experimental info

Sequence conflict37 – 437RSTIFPN → STIFPDR AA sequence Ref.4
Sequence conflict861D → N AA sequence Ref.4

Secondary structure

.................... 92
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7U3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 439F951848E95CB8

FASTA9210,430
        10         20         30         40         50         60 
MPRSLKKGPF IDLHLLKKVE KAVESGDKKP LRTWSRRSTI FPNMIGLTIA VHNGRQHVPV 

        70         80         90 
FVTDEMVGHK LGEFAPTRTY RGHAADKKAK KK 

« 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]"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]"Locking and unlocking of ribosomal motions."
Valle M., Zavialov A., Sengupta J., Rawat U., Ehrenberg M., Frank J.
Cell 114:123-134(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES INCLUDING BRIDGE CHANGES UPON TRANSLOCATION.
[12]"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 INCLUDING THE INTERSUBUNIT BRIDGE B1B.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02613 Genomic DNA. Translation: CAA26464.1.
U18997 Genomic DNA. Translation: AAA58113.1.
U00096 Genomic DNA. Translation: AAC76341.1.
AP009048 Genomic DNA. Translation: BAE77975.1.
PIRR3EC19. F23129.
RefSeqNP_417775.1. NC_000913.3.
YP_492116.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-S3-81[»]
1P6Gelectron microscopy12.30S2-92[»]
1P87electron microscopy11.50S2-92[»]
1VS5X-ray3.46S1-92[»]
1VS7X-ray3.46S1-92[»]
2AVYX-ray3.46S2-92[»]
2AW7X-ray3.46S2-92[»]
2GY9electron microscopy15.00S2-87[»]
2GYBelectron microscopy15.00S2-87[»]
2I2PX-ray3.22S2-91[»]
2I2UX-ray3.22S2-91[»]
2QALX-ray3.21S2-92[»]
2QANX-ray3.21S2-92[»]
2QB9X-ray3.54S2-92[»]
2QBBX-ray3.54S2-92[»]
2QBDX-ray3.30S2-92[»]
2QBFX-ray3.30S2-92[»]
2QBHX-ray4.00S2-92[»]
2QBJX-ray4.00S2-92[»]
2QOUX-ray3.93S2-92[»]
2QOWX-ray3.93S2-92[»]
2QOYX-ray3.50S2-92[»]
2QP0X-ray3.50S2-92[»]
2VHOX-ray3.74S2-92[»]
2VHPX-ray3.74S2-92[»]
2WWLelectron microscopy5.80S3-81[»]
2YKRelectron microscopy9.80S3-81[»]
2Z4KX-ray4.45S2-92[»]
2Z4MX-ray4.45S2-92[»]
3DF1X-ray3.50S2-91[»]
3DF3X-ray3.50S2-91[»]
3E1Aelectron microscopy-L1-92[»]
3E1Celectron microscopy-L1-92[»]
3FIHelectron microscopy6.70S3-81[»]
3I1MX-ray3.19S1-92[»]
3I1OX-ray3.19S1-92[»]
3I1QX-ray3.81S1-92[»]
3I1SX-ray3.81S1-92[»]
3I1ZX-ray3.71S1-92[»]
3I21X-ray3.71S1-92[»]
3IZVelectron microscopy-W1-92[»]
3IZWelectron microscopy-W1-92[»]
3J00electron microscopy-S2-92[»]
3J0Uelectron microscopy12.10V2-92[»]
3J0Velectron microscopy14.70V2-92[»]
3J0Xelectron microscopy13.50V2-92[»]
3J0Zelectron microscopy11.50V2-92[»]
3J10electron microscopy11.50V2-92[»]
3J13electron microscopy13.10U2-92[»]
3J18electron microscopy8.30S3-81[»]
3J36electron microscopy9.80S2-92[»]
3J4Velectron microscopy12.00S3-81[»]
3J4Welectron microscopy12.00S3-81[»]
3J4Yelectron microscopy17.00S3-81[»]
3J4Zelectron microscopy20.00S3-81[»]
3J53electron microscopy13.00S3-81[»]
3J55electron microscopy15.00S3-81[»]
3J57electron microscopy17.00S3-81[»]
3J59electron microscopy12.00S3-81[»]
3J5Belectron microscopy17.00S3-81[»]
3J5Delectron microscopy17.00S3-81[»]
3J5Felectron microscopy20.00S3-81[»]
3J5Helectron microscopy15.00S3-81[»]
3J5Jelectron microscopy9.00S3-81[»]
3J5Nelectron microscopy6.80S1-92[»]
3J5Telectron microscopy7.60S2-92[»]
3J5Xelectron microscopy7.60S2-92[»]
3KC4electron microscopy-S1-92[»]
3OAQX-ray3.25S3-81[»]
3OARX-ray3.25S3-81[»]
3OFAX-ray3.19S3-81[»]
3OFBX-ray3.19S3-81[»]
3OFOX-ray3.10S3-81[»]
3OFPX-ray3.10S3-81[»]
3OFXX-ray3.29S3-81[»]
3OFYX-ray3.29S3-81[»]
3OR9X-ray3.30S1-92[»]
3ORAX-ray3.30S1-92[»]
3SFSX-ray3.20S1-92[»]
3UOQX-ray3.70S1-92[»]
4A2Ielectron microscopy16.50S3-81[»]
4ADVelectron microscopy13.50S2-92[»]
4GAQX-ray3.30S1-92[»]
4GASX-ray3.30S1-92[»]
4GD1X-ray3.00S3-81[»]
4GD2X-ray3.00S3-81[»]
4KIYX-ray2.90S1-92[»]
4KJ0X-ray2.90S1-92[»]
4KJ2X-ray2.90S1-92[»]
4KJ4X-ray2.90S1-92[»]
4KJ6X-ray2.90S1-92[»]
4KJ8X-ray2.90S1-92[»]
4KJAX-ray2.90S1-92[»]
4KJCX-ray2.90S1-92[»]
DisProtDP00147.
ProteinModelPortalP0A7U3.
SMRP0A7U3. Positions 2-88.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852123. 1 interaction.
DIPDIP-47904N.
IntActP0A7U3. 30 interactions.
STRING511145.b3316.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7U3.
PRIDEP0A7U3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76341; AAC76341; b3316.
BAE77975; BAE77975; BAE77975.
GeneID12932294.
947811.
KEGGecj:Y75_p3860.
eco:b3316.
PATRIC32122064. VBIEscCol129921_3409.

Organism-specific databases

EchoBASEEB0911.
EcoGeneEG10918. rpsS.

Phylogenomic databases

eggNOGCOG0185.
HOGENOMHOG000111560.
KOK02965.
OMAVHNGRQF.
OrthoDBEOG61S365.
ProtClustDBPRK00357.

Enzyme and pathway databases

BioCycEcoCyc:EG10918-MONOMER.
ECOL316407:JW3278-MONOMER.

Gene expression databases

GenevestigatorP0A7U3.

Family and domain databases

Gene3D3.30.860.10. 1 hit.
HAMAPMF_00531. Ribosomal_S19.
InterProIPR002222. Ribosomal_S19.
IPR005732. Ribosomal_S19_bac-type.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
[Graphical view]
PANTHERPTHR11880. PTHR11880. 1 hit.
PfamPF00203. Ribosomal_S19. 1 hit.
[Graphical view]
PIRSFPIRSF002144. Ribosomal_S19. 1 hit.
PRINTSPR00975. RIBOSOMALS19.
SUPFAMSSF54570. SSF54570. 1 hit.
TIGRFAMsTIGR01050. rpsS_bact. 1 hit.
PROSITEPS00323. RIBOSOMAL_S19. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7U3.
PROP0A7U3.

Entry information

Entry nameRS19_ECOLI
AccessionPrimary (citable) accession number: P0A7U3
Secondary accession number(s): P02375, Q2M6Y1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 98 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