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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

  • endodeoxyribonuclease activity Source: EcoCyc
  • structural constituent of ribosome Source: GO_Central
  • structure-specific DNA binding Source: EcoCyc

GO - Biological processi

  • ribosomal small subunit assembly Source: EcoCyc
  • 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
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10915. rpsP.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2363135.

PTM / Processingi

Molecule processing

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

Proteomic databases

EPDiP0A7T3.
PaxDbiP0A7T3.
PRIDEiP0A7T3.

Expressioni

Inductioni

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

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[»]
3J9Yelectron microscopy3.90p1-82[»]
3J9Zelectron microscopy3.60SP1-82[»]
3JA1electron microscopy3.60SP1-82[»]
3JBUelectron microscopy3.64P1-82[»]
3JBVelectron microscopy3.32P1-82[»]
3JCDelectron microscopy3.70p1-82[»]
3JCEelectron microscopy3.20p1-82[»]
3JCJelectron microscopy3.70y1-82[»]
3JCNelectron microscopy4.60s1-82[»]
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[»]
4WOIX-ray3.00AP/DP1-82[»]
4WWWX-ray3.10QP/XP1-82[»]
4YBBX-ray2.10AP/BP1-82[»]
5AFIelectron microscopy2.90p1-82[»]
5IQRelectron microscopy3.00u1-82[»]
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

eggNOGiENOG4105K5M. Bacteria.
COG0228. LUCA.
HOGENOMiHOG000246720.
InParanoidiP0A7T3.
KOiK02959.
OMAiRVEHWVG.
PhylomeDBiP0A7T3.

Family and domain databases

Gene3Di3.30.1320.10. 1 hit.
HAMAPiMF_00385. Ribosomal_S16. 1 hit.
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.
WP_000256450.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75658; AAC75658; b2609.
BAA16494; BAA16494; BAA16494.
GeneIDi947103.
KEGGiecj:JW2590.
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.
WP_000256450.1. NZ_LN832404.1.

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[»]
3J9Yelectron microscopy3.90p1-82[»]
3J9Zelectron microscopy3.60SP1-82[»]
3JA1electron microscopy3.60SP1-82[»]
3JBUelectron microscopy3.64P1-82[»]
3JBVelectron microscopy3.32P1-82[»]
3JCDelectron microscopy3.70p1-82[»]
3JCEelectron microscopy3.20p1-82[»]
3JCJelectron microscopy3.70y1-82[»]
3JCNelectron microscopy4.60s1-82[»]
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[»]
4WOIX-ray3.00AP/DP1-82[»]
4WWWX-ray3.10QP/XP1-82[»]
4YBBX-ray2.10AP/BP1-82[»]
5AFIelectron microscopy2.90p1-82[»]
5IQRelectron microscopy3.00u1-82[»]
ProteinModelPortaliP0A7T3.
SMRiP0A7T3. Positions 1-82.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

EPDiP0A7T3.
PaxDbiP0A7T3.
PRIDEiP0A7T3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75658; AAC75658; b2609.
BAA16494; BAA16494; BAA16494.
GeneIDi947103.
KEGGiecj:JW2590.
eco:b2609.
PATRICi32120617. VBIEscCol129921_2707.

Organism-specific databases

EchoBASEiEB0908.
EcoGeneiEG10915. rpsP.

Phylogenomic databases

eggNOGiENOG4105K5M. Bacteria.
COG0228. LUCA.
HOGENOMiHOG000246720.
InParanoidiP0A7T3.
KOiK02959.
OMAiRVEHWVG.
PhylomeDBiP0A7T3.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7T3.
PROiP0A7T3.

Family and domain databases

Gene3Di3.30.1320.10. 1 hit.
HAMAPiMF_00385. Ribosomal_S16. 1 hit.
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...

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: September 7, 2016
This is version 111 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

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 one 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.