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Protein

30S ribosomal protein S14

Gene

rpsN

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10913-MONOMER.
ECOL316407:JW3269-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S14
Gene namesi
Name:rpsN
Ordered Locus Names:b3307, JW3269
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10913. rpsN.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Chemistry

DrugBankiDB00759. Tetracycline.
DB00560. Tigecycline.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 10110030S ribosomal protein S14PRO_0000130890Add
BLAST

Proteomic databases

PaxDbiP0AG59.
PRIDEiP0AG59.

Expressioni

Gene expression databases

GenevestigatoriP0AG59.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts proteins S3 and S10 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-35805N.
IntActiP0AG59. 70 interactions.
MINTiMINT-1295909.
STRINGi511145.b3307.

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1916Combined sources
Turni20 – 234Combined sources
Helixi24 – 263Combined sources
Helixi27 – 293Combined sources
Helixi30 – 323Combined sources
Helixi44 – 474Combined sources
Turni49 – 524Combined sources
Helixi53 – 553Combined sources
Helixi57 – 593Combined sources
Turni65 – 673Combined sources
Beta strandi71 – 744Combined sources
Turni75 – 784Combined sources
Helixi81 – 888Combined sources
Turni89 – 913Combined sources
Beta strandi93 – 953Combined sources
Beta strandi96 – 983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-N42-101[»]
2YKRelectron microscopy9.80N2-101[»]
4A2Ielectron microscopy16.50N2-101[»]
4ADVelectron microscopy13.50N2-101[»]
4U1UX-ray2.95AN/CN2-101[»]
4U1VX-ray3.00AN/CN2-101[»]
4U20X-ray2.90AN/CN2-101[»]
4U24X-ray2.90AN/CN2-101[»]
4U25X-ray2.90AN/CN2-101[»]
4U26X-ray2.80AN/CN2-101[»]
4U27X-ray2.80AN/CN2-101[»]
4V47electron microscopy12.30BN2-101[»]
4V48electron microscopy11.50BN2-101[»]
4V4HX-ray3.46AN/CN1-101[»]
4V4QX-ray3.46AN/CN2-101[»]
4V4Velectron microscopy15.00AN41-101[»]
4V4Welectron microscopy15.00AN41-101[»]
4V50X-ray3.22AN/CN2-101[»]
4V52X-ray3.21AN/CN2-101[»]
4V53X-ray3.54AN/CN2-101[»]
4V54X-ray3.30AN/CN2-101[»]
4V55X-ray4.00AN/CN2-101[»]
4V56X-ray3.93AN/CN2-101[»]
4V57X-ray3.50AN/CN2-101[»]
4V5BX-ray3.74BN/DN2-101[»]
4V5Helectron microscopy5.80AN2-101[»]
4V5YX-ray4.45AN/CN2-101[»]
4V64X-ray3.50AN/CN2-101[»]
4V65electron microscopy9.00AG1-101[»]
4V66electron microscopy9.00AG1-101[»]
4V69electron microscopy6.70AN2-101[»]
4V6CX-ray3.19AN/CN1-101[»]
4V6DX-ray3.81AN/CN1-101[»]
4V6EX-ray3.71AN/CN1-101[»]
4V6Kelectron microscopy8.25BR1-101[»]
4V6Lelectron microscopy13.20AR1-101[»]
4V6Melectron microscopy7.10AN2-101[»]
4V6Nelectron microscopy12.10BQ2-101[»]
4V6Oelectron microscopy14.70AQ2-101[»]
4V6Pelectron microscopy13.50AQ2-101[»]
4V6Qelectron microscopy11.50AQ2-101[»]
4V6Relectron microscopy11.50AQ2-101[»]
4V6Selectron microscopy13.10BP2-101[»]
4V6Telectron microscopy8.30AN2-101[»]
4V6Velectron microscopy9.80AN2-101[»]
4V6Yelectron microscopy12.00AN1-101[»]
4V6Zelectron microscopy12.00AN1-101[»]
4V70electron microscopy17.00AN1-101[»]
4V71electron microscopy20.00AN1-101[»]
4V72electron microscopy13.00AN1-101[»]
4V73electron microscopy15.00AN1-101[»]
4V74electron microscopy17.00AN1-101[»]
4V75electron microscopy12.00AN1-101[»]
4V76electron microscopy17.00AN1-101[»]
4V77electron microscopy17.00AN1-101[»]
4V78electron microscopy20.00AN1-101[»]
4V79electron microscopy15.00AN1-101[»]
4V7Aelectron microscopy9.00AN1-101[»]
4V7Belectron microscopy6.80AN1-101[»]
4V7Celectron microscopy7.60AN2-101[»]
4V7Delectron microscopy7.60BN2-101[»]
4V7Ielectron microscopy9.60BN1-101[»]
4V7SX-ray3.25AN/CN2-101[»]
4V7TX-ray3.19AN/CN2-101[»]
4V7UX-ray3.10AN/CN2-101[»]
4V7VX-ray3.29AN/CN2-101[»]
4V85X-ray3.20N1-101[»]
4V89X-ray3.70AN1-101[»]
4V9CX-ray3.30AN/CN1-101[»]
4V9DX-ray3.00AN/BN2-101[»]
4V9OX-ray2.90BN/DN/FN/HN1-101[»]
4V9PX-ray2.90BN/DN/FN/HN1-101[»]
4WF1X-ray3.09AN/CN2-101[»]
4WWWX-ray3.10QN/XN1-101[»]
4YBBX-ray2.10AN/BN2-101[»]
5AFIelectron microscopy2.90n1-101[»]
ProteinModelPortaliP0AG59.
SMRiP0AG59. Positions 2-101.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG59.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S14P family.Curated

Phylogenomic databases

eggNOGiCOG0199.
HOGENOMiHOG000039864.
InParanoidiP0AG59.
KOiK02954.
OMAiGKPRGVY.
OrthoDBiEOG6BCT0K.
PhylomeDBiP0AG59.

Family and domain databases

HAMAPiMF_00537. Ribosomal_S14_1.
InterProiIPR001209. Ribosomal_S14.
IPR023036. Ribosomal_S14_bac/plaastid.
IPR018271. Ribosomal_S14_CS.
[Graphical view]
PANTHERiPTHR19836. PTHR19836. 1 hit.
PfamiPF00253. Ribosomal_S14. 1 hit.
[Graphical view]
PROSITEiPS00527. RIBOSOMAL_S14. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AG59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKQSMKARE VKRVALADKY FAKRAELKAI ISDVNASDED RWNAVLKLQT
60 70 80 90 100
LPRDSSPSRQ RNRCRQTGRP HGFLRKFGLS RIKVREAAMR GEIPGLKKAS

W
Length:101
Mass (Da):11,580
Last modified:January 23, 2007 - v2
Checksum:iE2B21D9D3752352C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921E → Q AA sequence (Ref. 1) Curated
Sequence conflicti99 – 1013ASW → G in CAA25718 (PubMed:6222285).Curated

Mass spectrometryi

Molecular mass is 11449.3 Da from positions 2 - 101. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25718.1.
U18997 Genomic DNA. Translation: AAA58104.1.
U00096 Genomic DNA. Translation: AAC76332.1.
AP009048 Genomic DNA. Translation: BAE77984.1.
PIRiF65123. R3EC14.
RefSeqiNP_417766.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76332; AAC76332; b3307.
BAE77984; BAE77984; BAE77984.
GeneIDi947801.
KEGGiecj:Y75_p3869.
eco:b3307.
PATRICi32122046. VBIEscCol129921_3400.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25718.1.
U18997 Genomic DNA. Translation: AAA58104.1.
U00096 Genomic DNA. Translation: AAC76332.1.
AP009048 Genomic DNA. Translation: BAE77984.1.
PIRiF65123. R3EC14.
RefSeqiNP_417766.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-N42-101[»]
2YKRelectron microscopy9.80N2-101[»]
4A2Ielectron microscopy16.50N2-101[»]
4ADVelectron microscopy13.50N2-101[»]
4U1UX-ray2.95AN/CN2-101[»]
4U1VX-ray3.00AN/CN2-101[»]
4U20X-ray2.90AN/CN2-101[»]
4U24X-ray2.90AN/CN2-101[»]
4U25X-ray2.90AN/CN2-101[»]
4U26X-ray2.80AN/CN2-101[»]
4U27X-ray2.80AN/CN2-101[»]
4V47electron microscopy12.30BN2-101[»]
4V48electron microscopy11.50BN2-101[»]
4V4HX-ray3.46AN/CN1-101[»]
4V4QX-ray3.46AN/CN2-101[»]
4V4Velectron microscopy15.00AN41-101[»]
4V4Welectron microscopy15.00AN41-101[»]
4V50X-ray3.22AN/CN2-101[»]
4V52X-ray3.21AN/CN2-101[»]
4V53X-ray3.54AN/CN2-101[»]
4V54X-ray3.30AN/CN2-101[»]
4V55X-ray4.00AN/CN2-101[»]
4V56X-ray3.93AN/CN2-101[»]
4V57X-ray3.50AN/CN2-101[»]
4V5BX-ray3.74BN/DN2-101[»]
4V5Helectron microscopy5.80AN2-101[»]
4V5YX-ray4.45AN/CN2-101[»]
4V64X-ray3.50AN/CN2-101[»]
4V65electron microscopy9.00AG1-101[»]
4V66electron microscopy9.00AG1-101[»]
4V69electron microscopy6.70AN2-101[»]
4V6CX-ray3.19AN/CN1-101[»]
4V6DX-ray3.81AN/CN1-101[»]
4V6EX-ray3.71AN/CN1-101[»]
4V6Kelectron microscopy8.25BR1-101[»]
4V6Lelectron microscopy13.20AR1-101[»]
4V6Melectron microscopy7.10AN2-101[»]
4V6Nelectron microscopy12.10BQ2-101[»]
4V6Oelectron microscopy14.70AQ2-101[»]
4V6Pelectron microscopy13.50AQ2-101[»]
4V6Qelectron microscopy11.50AQ2-101[»]
4V6Relectron microscopy11.50AQ2-101[»]
4V6Selectron microscopy13.10BP2-101[»]
4V6Telectron microscopy8.30AN2-101[»]
4V6Velectron microscopy9.80AN2-101[»]
4V6Yelectron microscopy12.00AN1-101[»]
4V6Zelectron microscopy12.00AN1-101[»]
4V70electron microscopy17.00AN1-101[»]
4V71electron microscopy20.00AN1-101[»]
4V72electron microscopy13.00AN1-101[»]
4V73electron microscopy15.00AN1-101[»]
4V74electron microscopy17.00AN1-101[»]
4V75electron microscopy12.00AN1-101[»]
4V76electron microscopy17.00AN1-101[»]
4V77electron microscopy17.00AN1-101[»]
4V78electron microscopy20.00AN1-101[»]
4V79electron microscopy15.00AN1-101[»]
4V7Aelectron microscopy9.00AN1-101[»]
4V7Belectron microscopy6.80AN1-101[»]
4V7Celectron microscopy7.60AN2-101[»]
4V7Delectron microscopy7.60BN2-101[»]
4V7Ielectron microscopy9.60BN1-101[»]
4V7SX-ray3.25AN/CN2-101[»]
4V7TX-ray3.19AN/CN2-101[»]
4V7UX-ray3.10AN/CN2-101[»]
4V7VX-ray3.29AN/CN2-101[»]
4V85X-ray3.20N1-101[»]
4V89X-ray3.70AN1-101[»]
4V9CX-ray3.30AN/CN1-101[»]
4V9DX-ray3.00AN/BN2-101[»]
4V9OX-ray2.90BN/DN/FN/HN1-101[»]
4V9PX-ray2.90BN/DN/FN/HN1-101[»]
4WF1X-ray3.09AN/CN2-101[»]
4WWWX-ray3.10QN/XN1-101[»]
4YBBX-ray2.10AN/BN2-101[»]
5AFIelectron microscopy2.90n1-101[»]
ProteinModelPortaliP0AG59.
SMRiP0AG59. Positions 2-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35805N.
IntActiP0AG59. 70 interactions.
MINTiMINT-1295909.
STRINGi511145.b3307.

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB00759. Tetracycline.
DB00560. Tigecycline.

Proteomic databases

PaxDbiP0AG59.
PRIDEiP0AG59.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76332; AAC76332; b3307.
BAE77984; BAE77984; BAE77984.
GeneIDi947801.
KEGGiecj:Y75_p3869.
eco:b3307.
PATRICi32122046. VBIEscCol129921_3400.

Organism-specific databases

EchoBASEiEB0906.
EcoGeneiEG10913. rpsN.

Phylogenomic databases

eggNOGiCOG0199.
HOGENOMiHOG000039864.
InParanoidiP0AG59.
KOiK02954.
OMAiGKPRGVY.
OrthoDBiEOG6BCT0K.
PhylomeDBiP0AG59.

Enzyme and pathway databases

BioCyciEcoCyc:EG10913-MONOMER.
ECOL316407:JW3269-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AG59.
PROiP0AG59.

Gene expression databases

GenevestigatoriP0AG59.

Family and domain databases

HAMAPiMF_00537. Ribosomal_S14_1.
InterProiIPR001209. Ribosomal_S14.
IPR023036. Ribosomal_S14_bac/plaastid.
IPR018271. Ribosomal_S14_CS.
[Graphical view]
PANTHERiPTHR19836. PTHR19836. 1 hit.
PfamiPF00253. Ribosomal_S14. 1 hit.
[Graphical view]
PROSITEiPS00527. RIBOSOMAL_S14. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Yaguchi M., Roy C., Reithmeier R.A.F., Wittmann-Liebold B.
    Submitted (OCT-1982) to the PIR data bank
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-101.
    Strain: K12.
  2. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
    Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
    Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. 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. "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.
  6. "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.
  7. "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.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS14_ECOLI
AccessioniPrimary (citable) accession number: P0AG59
Secondary accession number(s): P02370, Q2M6X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 99 of the entry and version 2 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.