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P0A7K6 (RL19_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 86. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L19
Gene names
Name:rplS
Ordered Locus Names:b2606, JW2587
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length115 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome (Ref.8) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures (Ref.9) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation. HAMAP-Rule MF_00402

Subunit structure

Part of the 50S ribosomal subunit. Contacts L14 (Ref.6 and Ref.9). Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Ref.8

Induction

Part of the rpsP-rimM-trmD-rplS operon. HAMAP-Rule MF_00402

Sequence similarities

Belongs to the ribosomal protein L19P family.

Mass spectrometry

Molecular mass is 13001.7 Da from positions 2 - 115. Determined by MALDI. Ref.7

Ontologies

Keywords
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionrRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

nanEP0A7611EBI-543891,EBI-561432

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 11511450S ribosomal protein L19 HAMAP-Rule MF_00402
PRO_0000163451

Secondary structure

1 ........................ 115
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7K6 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7BD9F2EFB9DDB06B

FASTA11513,133
        10         20         30         40         50         60 
MSNIIKQLEQ EQMKQDVPSF RPGDTVEVKV WVVEGSKKRL QAFEGVVIAI RNRGLHSAFT 

        70         80         90        100        110 
VRKISNGEGV ERVFQTHSPV VDSISVKRRG AVRKAKLYYL RERTGKAARI KERLN

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21-K polypeptide."
Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.
EMBO J. 2:899-905(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE.
Strain: K12.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"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 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
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 L19 from the large subunit of Escherichia coli ribosomes."
Brosius J., Arfsten U.
Biochemistry 17:508-516(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-115.
[6]"Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli."
Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.
Biochemistry 28:4099-4105(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO L14.
[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]"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.
[9]"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.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X01818 Genomic DNA. Translation: CAA25960.1.
U00096 Genomic DNA. Translation: AAC75655.1.
AP009048 Genomic DNA. Translation: BAA16491.1.
PIRR5EC19. S07951.
RefSeqNP_417097.1. NC_000913.2.
YP_490829.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30N2-115[»]
1P86electron microscopy11.50N2-115[»]
1VS6X-ray3.46P2-114[»]
1VS8X-ray3.46P1-115[»]
1VT2X-ray3.30P1-115[»]
2AW4X-ray3.46P2-115[»]
2AWBX-ray3.46P2-115[»]
2GYAelectron microscopy15.00N2-114[»]
2GYCelectron microscopy15.00N2-115[»]
2I2TX-ray3.22P2-114[»]
2I2VX-ray3.22P2-114[»]
2J28electron microscopy8.00P2-115[»]
2QAMX-ray3.21P2-115[»]
2QAOX-ray3.21P2-115[»]
2QBAX-ray3.54P2-115[»]
2QBCX-ray3.54P2-115[»]
2QBEX-ray3.30P2-115[»]
2QBGX-ray3.30P2-115[»]
2QBIX-ray4.00P2-115[»]
2QBKX-ray4.00P2-115[»]
2QOVX-ray3.93P2-115[»]
2QOXX-ray3.93P2-115[»]
2QOZX-ray3.50P2-115[»]
2QP1X-ray3.50P2-115[»]
2RDOelectron microscopy9.10P2-115[»]
2VHMX-ray3.74P2-115[»]
2VHNX-ray3.74P2-115[»]
2WWQelectron microscopy5.80P2-115[»]
2Z4LX-ray4.45P2-115[»]
2Z4NX-ray4.45P2-115[»]
3BBXelectron microscopy10.00P2-115[»]
3DF2X-ray3.50P2-114[»]
3DF4X-ray3.50P2-114[»]
3E1Belectron microscopy-I1-115[»]
3E1Delectron microscopy-I1-115[»]
3FIKelectron microscopy6.70P2-115[»]
3I1NX-ray3.19P1-115[»]
3I1PX-ray3.19P1-115[»]
3I1RX-ray3.81P1-115[»]
3I1TX-ray3.81P1-115[»]
3I20X-ray3.71P1-115[»]
3I22X-ray3.71P1-115[»]
3IZTelectron microscopy-Q1-115[»]
3IZUelectron microscopy-Q1-115[»]
3J01electron microscopy-P2-115[»]
3J0Telectron microscopy12.10R2-114[»]
3J0Welectron microscopy14.70R2-114[»]
3J0Yelectron microscopy13.50R2-114[»]
3J11electron microscopy13.10R2-114[»]
3J12electron microscopy11.50R2-114[»]
3J14electron microscopy11.50R2-114[»]
3J19electron microscopy8.30P2-115[»]
3J37electron microscopy9.80T2-115[»]
3KCRelectron microscopy-P1-115[»]
3OASX-ray3.25P2-115[»]
3OATX-ray3.25P2-115[»]
3OFCX-ray3.19P2-115[»]
3OFDX-ray3.19P2-115[»]
3OFQX-ray3.10P2-115[»]
3OFRX-ray3.10P2-115[»]
3OFZX-ray3.29P2-115[»]
3OG0X-ray3.29P2-115[»]
3ORBX-ray3.30P1-115[»]
3R8SX-ray3.00P2-115[»]
3R8TX-ray3.00P2-115[»]
3SGFX-ray3.20T1-115[»]
3UOSX-ray3.70T1-115[»]
4GARX-ray3.30P1-115[»]
4GAUX-ray3.30P1-115[»]
ProteinModelPortalP0A7K6.
SMRP0A7K6. Positions 2-115.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35793N.
IntActP0A7K6. 100 interactions.
MINTMINT-1245288.
STRING511145.b2606.

PTM databases

PhosSiteP0810432.

Proteomic databases

PaxDbP0A7K6.
PRIDEP0A7K6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75655; AAC75655; b2606.
BAA16491; BAA16491; BAA16491.
GeneID12931612.
947096.
KEGGecj:Y75_p2554.
eco:b2606.
PATRIC32120611. VBIEscCol129921_2704.

Organism-specific databases

EchoBASEEB0873.
EcoGeneEG10880. rplS.

Phylogenomic databases

eggNOGCOG0335.
HOGENOMHOG000016264.
KOK02884.
OMATLKVHVR.
ProtClustDBPRK05338.

Enzyme and pathway databases

BioCycEcoCyc:EG10880-MONOMER.
ECOL316407:JW2587-MONOMER.

Gene expression databases

GenevestigatorP0A7K6.

Family and domain databases

HAMAPMF_00402. Ribosomal_L19.
InterProIPR001857. Ribosomal_L19.
IPR018257. Ribosomal_L19_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERPTHR15680. PTHR15680. 1 hit.
PfamPF01245. Ribosomal_L19. 1 hit.
[Graphical view]
PIRSFPIRSF002191. Ribosomal_L19. 1 hit.
PRINTSPR00061. RIBOSOMALL19.
SUPFAMSSF50104. Transl_SH3_like. 1 hit.
TIGRFAMsTIGR01024. rplS_bact. 1 hit.
PROSITEPS01015. RIBOSOMAL_L19. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7K6.

Entry information

Entry nameRL19_ECOLI
AccessionPrimary (citable) accession number: P0A7K6
Secondary accession number(s): P02420
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents