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P0A7T3 (RS16_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 91. 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 S16
Gene names
Name:rpsP
Ordered Locus Names:b2609, JW2590
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length82 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In addition to being a ribosomal protein, S16 also has a cation-dependent endonuclease activity. Ref.6

In-frame fusions with the ribosome maturation factor rimM suppress mutations in the latter (probably due to increased rimM expression) and are found in translationally active 70S ribosomes. Ref.6

Induction

Part of the rpsP-rimM-trmD-rplS operon. HAMAP-Rule MF_00385

Sequence similarities

Belongs to the ribosomal protein S16P family.

Mass spectrometry

Molecular mass is 9190.5 Da from positions 1 - 82. Determined by MALDI. Ref.10

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 828230S ribosomal protein S16 HAMAP-Rule MF_00385
PRO_0000167184

Secondary structure

......................... 82
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7T3 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F94D07049A6D489D

FASTA829,191
        10         20         30         40         50         60 
MVTIRLARHG AKKRPFYQVV VADSRNARNG RFIERVGFFN PIASEKEEGT RLDLDRIAHW 

        70         80 
VGQGATISDR VAALIKEVNK AA 

« Hide

References

« Hide 'large scale' references
[1]"The complete amino acid sequence of protein S16 from Escherichia coli."
Vandekerckhove J., Rombauts W., Wittmann-Liebold B.
Hoppe-Seyler's Z. Physiol. Chem. 358:989-1002(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: K.
[2]"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.
[3]"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.
[4]"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.
[5]"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], SEQUENCE REVISION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"The Escherichia coli ribosomal protein S16 is an endonuclease."
Oberto J., Bonnefoy E., Mouay E., Pellegrini O., Wilkstroem P.M., Rouviere-Yaniv J.
Mol. Microbiol. 19:1319-1330(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15, FUNCTION AS AN ENDONUCLEASE.
[7]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[8]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[9]"Hybrid protein between ribosomal protein S16 and RimM of Escherichia coli retains the ribosome maturation function of both proteins."
Loevgren J.M., Wikstroem P.M.
J. Bacteriol. 183:5352-5357(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUSION WITH RIBOSOME MATURATION FACTOR RIMM.
Strain: MW100.
[10]"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.
[11]"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.
[12]"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.
[13]"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: CAA25958.1.
U00096 Genomic DNA. Translation: AAC75658.1.
AP009048 Genomic DNA. Translation: BAA16494.2.
PIRR3EC16. S07948.
RefSeqNP_417100.1. NC_000913.3.
YP_490832.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-P1-82[»]
1ML5electron microscopy14.00S1-82[»]
1P6Gelectron microscopy12.30P1-82[»]
1P87electron microscopy11.50P1-82[»]
1VS5X-ray3.46P1-82[»]
1VS7X-ray3.46P1-82[»]
2AVYX-ray3.46P1-82[»]
2AW7X-ray3.46P1-82[»]
2GY9electron microscopy15.00P1-78[»]
2GYBelectron microscopy15.00P1-78[»]
2I2PX-ray3.22P1-82[»]
2I2UX-ray3.22P1-82[»]
2QALX-ray3.21P1-82[»]
2QANX-ray3.21P1-82[»]
2QB9X-ray3.54P1-82[»]
2QBBX-ray3.54P1-82[»]
2QBDX-ray3.30P1-82[»]
2QBFX-ray3.30P1-82[»]
2QBHX-ray4.00P1-82[»]
2QBJX-ray4.00P1-82[»]
2QOUX-ray3.93P1-82[»]
2QOWX-ray3.93P1-82[»]
2QOYX-ray3.50P1-82[»]
2QP0X-ray3.50P1-82[»]
2VHOX-ray3.74P1-82[»]
2VHPX-ray3.74P1-82[»]
2WWLelectron microscopy5.80P1-80[»]
2YKRelectron microscopy9.80P1-82[»]
2Z4KX-ray4.45P1-82[»]
2Z4MX-ray4.45P1-82[»]
3DF1X-ray3.50P1-82[»]
3DF3X-ray3.50P1-82[»]
3E1Aelectron microscopy-I1-82[»]
3E1Celectron microscopy-I1-82[»]
3FIHelectron microscopy6.70P1-80[»]
3I1MX-ray3.19P1-82[»]
3I1OX-ray3.19P1-82[»]
3I1QX-ray3.81P1-82[»]
3I1SX-ray3.81P1-82[»]
3I1ZX-ray3.71P1-82[»]
3I21X-ray3.71P1-82[»]
3IZVelectron microscopy-T1-82[»]
3IZWelectron microscopy-T1-82[»]
3J00electron microscopy-P1-82[»]
3J0Uelectron microscopy12.10S1-82[»]
3J0Velectron microscopy14.70S1-82[»]
3J0Xelectron microscopy13.50S1-82[»]
3J0Zelectron microscopy11.50S1-82[»]
3J10electron microscopy11.50S1-82[»]
3J13electron microscopy13.10R1-82[»]
3J18electron microscopy8.30P1-82[»]
3J36electron microscopy9.80P1-82[»]
3J4Velectron microscopy12.00P1-80[»]
3J4Welectron microscopy12.00P1-80[»]
3J4Yelectron microscopy17.00P1-80[»]
3J4Zelectron microscopy20.00P1-80[»]
3J53electron microscopy13.00P1-80[»]
3J55electron microscopy15.00P1-80[»]
3J57electron microscopy17.00P1-80[»]
3J59electron microscopy12.00P1-80[»]
3J5Belectron microscopy17.00P1-80[»]
3J5Delectron microscopy17.00P1-80[»]
3J5Felectron microscopy20.00P1-80[»]
3J5Helectron microscopy15.00P1-80[»]
3J5Jelectron microscopy9.00P1-80[»]
3J5Nelectron microscopy6.80P1-82[»]
3J5Telectron microscopy7.60P1-82[»]
3J5Xelectron microscopy7.60P1-82[»]
3KC4electron microscopy-P1-82[»]
3OAQX-ray3.25P1-82[»]
3OARX-ray3.25P1-80[»]
3OFAX-ray3.19P1-82[»]
3OFBX-ray3.19P1-80[»]
3OFOX-ray3.10P1-82[»]
3OFPX-ray3.10P1-80[»]
3OFXX-ray3.29P1-82[»]
3OFYX-ray3.29P1-80[»]
3OR9X-ray3.30P1-82[»]
3ORAX-ray3.30P1-82[»]
3SFSX-ray3.20P1-82[»]
3UOQX-ray3.70P1-82[»]
4A2Ielectron microscopy16.50P1-82[»]
4ADVelectron microscopy13.50P1-82[»]
4GAQX-ray3.30P1-82[»]
4GASX-ray3.30P1-82[»]
4GD1X-ray3.00P1-82[»]
4GD2X-ray3.00P1-82[»]
4KIYX-ray2.90P1-82[»]
4KJ0X-ray2.90P1-82[»]
4KJ2X-ray2.90P1-82[»]
4KJ4X-ray2.90P1-82[»]
4KJ6X-ray2.90P1-82[»]
4KJ8X-ray2.90P1-82[»]
4KJAX-ray2.90P1-82[»]
4KJCX-ray2.90P1-82[»]
ProteinModelPortalP0A7T3.
SMRP0A7T3. Positions 1-82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47829N.
IntActP0A7T3. 55 interactions.
MINTMINT-1280042.
STRING511145.b2609.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7T3.
PRIDEP0A7T3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75658; AAC75658; b2609.
BAA16494; BAA16494; BAA16494.
GeneID12930606.
947103.
KEGGecj:Y75_p2557.
eco:b2609.
PATRIC32120617. VBIEscCol129921_2707.

Organism-specific databases

EchoBASEEB0908.
EcoGeneEG10915. rpsP.

Phylogenomic databases

eggNOGCOG0228.
HOGENOMHOG000246720.
KOK02959.
OMARVEHWVG.
OrthoDBEOG6CVVKH.
PhylomeDBP0A7T3.

Enzyme and pathway databases

BioCycEcoCyc:EG10915-MONOMER.
ECOL316407:JW2590-MONOMER.

Gene expression databases

GenevestigatorP0A7T3.

Family and domain databases

Gene3D3.30.1320.10. 1 hit.
HAMAPMF_00385. Ribosomal_S16.
InterProIPR000307. Ribosomal_S16.
IPR020592. Ribosomal_S16_CS.
IPR023803. Ribosomal_S16_dom.
[Graphical view]
PANTHERPTHR12919. PTHR12919. 1 hit.
PfamPF00886. Ribosomal_S16. 1 hit.
[Graphical view]
SUPFAMSSF54565. SSF54565. 1 hit.
TIGRFAMsTIGR00002. S16. 1 hit.
PROSITEPS00732. RIBOSOMAL_S16. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7T3.
PROP0A7T3.

Entry information

Entry nameRS16_ECOLI
AccessionPrimary (citable) accession number: P0A7T3
Secondary accession number(s): P02372, P77006
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 91 of the entry and version 1 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