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Protein

30S ribosomal protein S16

Gene

rpsP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

In addition to being a ribosomal protein, S16 also has a cation-dependent endonuclease activity.1 Publication
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.1 Publication

GO - Molecular functioni

  1. endodeoxyribonuclease activity Source: EcoCyc
  2. structural constituent of ribosome Source: GO_Central
  3. structure-specific DNA binding Source: EcoCyc

GO - Biological processi

  1. DNA metabolic process Source: GOC
  2. ribosomal small subunit assembly Source: EcoCyc
  3. translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease, Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10915-MONOMER.
ECOL316407:JW2590-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S16UniRule annotation
Gene namesi
Name:rpsPUniRule annotation
Ordered Locus Names:b2609, JW2590
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10915. rpsP.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 828230S ribosomal protein S16PRO_0000167184Add
BLAST

Proteomic databases

PaxDbiP0A7T3.
PRIDEiP0A7T3.

Expressioni

Inductioni

Part of the rpsP-rimM-trmD-rplS operon.

Gene expression databases

GenevestigatoriP0A7T3.

Interactioni

Protein-protein interaction databases

DIPiDIP-47829N.
IntActiP0A7T3. 55 interactions.
MINTiMINT-1280042.
STRINGi511145.b2609.

Structurei

Secondary structure

1
82
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Beta strandi9 – 113Combined sources
Beta strandi12 – 143Combined sources
Beta strandi17 – 2610Combined sources
Beta strandi28 – 303Combined sources
Beta strandi33 – 397Combined sources
Beta strandi41 – 433Combined sources
Beta strandi45 – 473Combined sources
Beta strandi49 – 524Combined sources
Helixi54 – 618Combined sources
Turni62 – 643Combined sources
Helixi69 – 757Combined sources
Turni76 – 783Combined sources
Turni79 – 813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-P1-82[»]
1ML5electron microscopy14.00S1-82[»]
2YKRelectron microscopy9.80P1-82[»]
4A2Ielectron microscopy16.50P1-82[»]
4ADVelectron microscopy13.50P1-82[»]
4U1UX-ray2.95AP/CP1-82[»]
4U1VX-ray3.00AP/CP1-82[»]
4U20X-ray2.90AP/CP1-82[»]
4U24X-ray2.90AP/CP1-82[»]
4U25X-ray2.90AP/CP1-82[»]
4U26X-ray2.80AP/CP1-82[»]
4U27X-ray2.80AP/CP1-82[»]
4V47electron microscopy12.30BP1-82[»]
4V48electron microscopy11.50BP1-82[»]
4V4HX-ray3.46AP/CP1-82[»]
4V4QX-ray3.46AP/CP1-82[»]
4V4Velectron microscopy15.00AP1-78[»]
4V4Welectron microscopy15.00AP1-78[»]
4V50X-ray3.22AP/CP1-82[»]
4V52X-ray3.21AP/CP1-82[»]
4V53X-ray3.54AP/CP1-82[»]
4V54X-ray3.30AP/CP1-82[»]
4V55X-ray4.00AP/CP1-82[»]
4V56X-ray3.93AP/CP1-82[»]
4V57X-ray3.50AP/CP1-82[»]
4V5BX-ray3.74BP/DP1-82[»]
4V5Helectron microscopy5.80AP1-80[»]
4V5YX-ray4.45AP/CP1-82[»]
4V64X-ray3.50AP/CP1-82[»]
4V65electron microscopy9.00AI1-82[»]
4V66electron microscopy9.00AI1-82[»]
4V69electron microscopy6.70AP1-80[»]
4V6CX-ray3.19AP/CP1-82[»]
4V6DX-ray3.81AP/CP1-82[»]
4V6EX-ray3.71AP/CP1-82[»]
4V6Kelectron microscopy8.25BT1-82[»]
4V6Lelectron microscopy13.20AT1-82[»]
4V6Melectron microscopy7.10AP1-82[»]
4V6Nelectron microscopy12.10BS1-82[»]
4V6Oelectron microscopy14.70AS1-82[»]
4V6Pelectron microscopy13.50AS1-82[»]
4V6Qelectron microscopy11.50AS1-82[»]
4V6Relectron microscopy11.50AS1-82[»]
4V6Selectron microscopy13.10BR1-82[»]
4V6Telectron microscopy8.30AP1-82[»]
4V6Velectron microscopy9.80AP1-82[»]
4V6Yelectron microscopy12.00AP1-80[»]
4V6Zelectron microscopy12.00AP1-80[»]
4V70electron microscopy17.00AP1-80[»]
4V71electron microscopy20.00AP1-80[»]
4V72electron microscopy13.00AP1-80[»]
4V73electron microscopy15.00AP1-80[»]
4V74electron microscopy17.00AP1-80[»]
4V75electron microscopy12.00AP1-80[»]
4V76electron microscopy17.00AP1-80[»]
4V77electron microscopy17.00AP1-80[»]
4V78electron microscopy20.00AP1-80[»]
4V79electron microscopy15.00AP1-80[»]
4V7Aelectron microscopy9.00AP1-80[»]
4V7Belectron microscopy6.80AP1-82[»]
4V7Celectron microscopy7.60AP1-82[»]
4V7Delectron microscopy7.60BP1-82[»]
4V7Ielectron microscopy9.60BP1-82[»]
4V7SX-ray3.25AP1-82[»]
CP1-80[»]
4V7TX-ray3.19AP1-82[»]
CP1-80[»]
4V7UX-ray3.10AP/CP1-82[»]
4V7VX-ray3.29AP1-82[»]
CP1-80[»]
4V85X-ray3.20P1-82[»]
4V89X-ray3.70AP1-82[»]
4V9CX-ray3.30AP/CP1-82[»]
4V9DX-ray3.00AP/BP1-82[»]
4V9OX-ray2.90BP/DP/FP/HP1-82[»]
4V9PX-ray2.90BP/DP/FP/HP1-82[»]
4WF1X-ray3.09AP/CP1-82[»]
4WWWX-ray3.10QP/XP1-82[»]
5AFIelectron microscopy2.90p1-82[»]
ProteinModelPortaliP0A7T3.
SMRiP0A7T3. Positions 1-82.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7T3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S16P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0228.
HOGENOMiHOG000246720.
InParanoidiP0A7T3.
KOiK02959.
OMAiRVEHWVG.
OrthoDBiEOG6CVVKH.
PhylomeDBiP0A7T3.

Family and domain databases

Gene3Di3.30.1320.10. 1 hit.
HAMAPiMF_00385. Ribosomal_S16.
InterProiIPR000307. Ribosomal_S16.
IPR020592. Ribosomal_S16_CS.
IPR023803. Ribosomal_S16_dom.
[Graphical view]
PANTHERiPTHR12919. PTHR12919. 1 hit.
PfamiPF00886. Ribosomal_S16. 1 hit.
[Graphical view]
SUPFAMiSSF54565. SSF54565. 1 hit.
TIGRFAMsiTIGR00002. S16. 1 hit.
PROSITEiPS00732. RIBOSOMAL_S16. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7T3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTIRLARHG AKKRPFYQVV VADSRNARNG RFIERVGFFN PIASEKEEGT
60 70 80
RLDLDRIAHW VGQGATISDR VAALIKEVNK AA
Length:82
Mass (Da):9,191
Last modified:July 21, 1986 - v1
Checksum:iF94D07049A6D489D
GO

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01818 Genomic DNA. Translation: CAA25958.1.
U00096 Genomic DNA. Translation: AAC75658.1.
AP009048 Genomic DNA. Translation: BAA16494.2.
PIRiS07948. R3EC16.
RefSeqiNP_417100.1. NC_000913.3.
YP_490832.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75658; AAC75658; b2609.
BAA16494; BAA16494; BAA16494.
GeneIDi12930606.
947103.
KEGGiecj:Y75_p2557.
eco:b2609.
PATRICi32120617. VBIEscCol129921_2707.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01818 Genomic DNA. Translation: CAA25958.1.
U00096 Genomic DNA. Translation: AAC75658.1.
AP009048 Genomic DNA. Translation: BAA16494.2.
PIRiS07948. R3EC16.
RefSeqiNP_417100.1. NC_000913.3.
YP_490832.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-P1-82[»]
1ML5electron microscopy14.00S1-82[»]
2YKRelectron microscopy9.80P1-82[»]
4A2Ielectron microscopy16.50P1-82[»]
4ADVelectron microscopy13.50P1-82[»]
4U1UX-ray2.95AP/CP1-82[»]
4U1VX-ray3.00AP/CP1-82[»]
4U20X-ray2.90AP/CP1-82[»]
4U24X-ray2.90AP/CP1-82[»]
4U25X-ray2.90AP/CP1-82[»]
4U26X-ray2.80AP/CP1-82[»]
4U27X-ray2.80AP/CP1-82[»]
4V47electron microscopy12.30BP1-82[»]
4V48electron microscopy11.50BP1-82[»]
4V4HX-ray3.46AP/CP1-82[»]
4V4QX-ray3.46AP/CP1-82[»]
4V4Velectron microscopy15.00AP1-78[»]
4V4Welectron microscopy15.00AP1-78[»]
4V50X-ray3.22AP/CP1-82[»]
4V52X-ray3.21AP/CP1-82[»]
4V53X-ray3.54AP/CP1-82[»]
4V54X-ray3.30AP/CP1-82[»]
4V55X-ray4.00AP/CP1-82[»]
4V56X-ray3.93AP/CP1-82[»]
4V57X-ray3.50AP/CP1-82[»]
4V5BX-ray3.74BP/DP1-82[»]
4V5Helectron microscopy5.80AP1-80[»]
4V5YX-ray4.45AP/CP1-82[»]
4V64X-ray3.50AP/CP1-82[»]
4V65electron microscopy9.00AI1-82[»]
4V66electron microscopy9.00AI1-82[»]
4V69electron microscopy6.70AP1-80[»]
4V6CX-ray3.19AP/CP1-82[»]
4V6DX-ray3.81AP/CP1-82[»]
4V6EX-ray3.71AP/CP1-82[»]
4V6Kelectron microscopy8.25BT1-82[»]
4V6Lelectron microscopy13.20AT1-82[»]
4V6Melectron microscopy7.10AP1-82[»]
4V6Nelectron microscopy12.10BS1-82[»]
4V6Oelectron microscopy14.70AS1-82[»]
4V6Pelectron microscopy13.50AS1-82[»]
4V6Qelectron microscopy11.50AS1-82[»]
4V6Relectron microscopy11.50AS1-82[»]
4V6Selectron microscopy13.10BR1-82[»]
4V6Telectron microscopy8.30AP1-82[»]
4V6Velectron microscopy9.80AP1-82[»]
4V6Yelectron microscopy12.00AP1-80[»]
4V6Zelectron microscopy12.00AP1-80[»]
4V70electron microscopy17.00AP1-80[»]
4V71electron microscopy20.00AP1-80[»]
4V72electron microscopy13.00AP1-80[»]
4V73electron microscopy15.00AP1-80[»]
4V74electron microscopy17.00AP1-80[»]
4V75electron microscopy12.00AP1-80[»]
4V76electron microscopy17.00AP1-80[»]
4V77electron microscopy17.00AP1-80[»]
4V78electron microscopy20.00AP1-80[»]
4V79electron microscopy15.00AP1-80[»]
4V7Aelectron microscopy9.00AP1-80[»]
4V7Belectron microscopy6.80AP1-82[»]
4V7Celectron microscopy7.60AP1-82[»]
4V7Delectron microscopy7.60BP1-82[»]
4V7Ielectron microscopy9.60BP1-82[»]
4V7SX-ray3.25AP1-82[»]
CP1-80[»]
4V7TX-ray3.19AP1-82[»]
CP1-80[»]
4V7UX-ray3.10AP/CP1-82[»]
4V7VX-ray3.29AP1-82[»]
CP1-80[»]
4V85X-ray3.20P1-82[»]
4V89X-ray3.70AP1-82[»]
4V9CX-ray3.30AP/CP1-82[»]
4V9DX-ray3.00AP/BP1-82[»]
4V9OX-ray2.90BP/DP/FP/HP1-82[»]
4V9PX-ray2.90BP/DP/FP/HP1-82[»]
4WF1X-ray3.09AP/CP1-82[»]
4WWWX-ray3.10QP/XP1-82[»]
5AFIelectron microscopy2.90p1-82[»]
ProteinModelPortaliP0A7T3.
SMRiP0A7T3. Positions 1-82.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47829N.
IntActiP0A7T3. 55 interactions.
MINTiMINT-1280042.
STRINGi511145.b2609.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0A7T3.
PRIDEiP0A7T3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75658; AAC75658; b2609.
BAA16494; BAA16494; BAA16494.
GeneIDi12930606.
947103.
KEGGiecj:Y75_p2557.
eco:b2609.
PATRICi32120617. VBIEscCol129921_2707.

Organism-specific databases

EchoBASEiEB0908.
EcoGeneiEG10915. rpsP.

Phylogenomic databases

eggNOGiCOG0228.
HOGENOMiHOG000246720.
InParanoidiP0A7T3.
KOiK02959.
OMAiRVEHWVG.
OrthoDBiEOG6CVVKH.
PhylomeDBiP0A7T3.

Enzyme and pathway databases

BioCyciEcoCyc:EG10915-MONOMER.
ECOL316407:JW2590-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7T3.
PROiP0A7T3.

Gene expression databases

GenevestigatoriP0A7T3.

Family and domain databases

Gene3Di3.30.1320.10. 1 hit.
HAMAPiMF_00385. Ribosomal_S16.
InterProiIPR000307. Ribosomal_S16.
IPR020592. Ribosomal_S16_CS.
IPR023803. Ribosomal_S16_dom.
[Graphical view]
PANTHERiPTHR12919. PTHR12919. 1 hit.
PfamiPF00886. Ribosomal_S16. 1 hit.
[Graphical view]
SUPFAMiSSF54565. SSF54565. 1 hit.
TIGRFAMsiTIGR00002. S16. 1 hit.
PROSITEiPS00732. RIBOSOMAL_S16. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS16_ECOLI
AccessioniPrimary (citable) accession number: P0A7T3
Secondary accession number(s): P02372, P77006
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 29, 2015
This is version 99 of the entry and version 1 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.