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P0AG59 (RS14_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. 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 S14
Gene names
Name:rpsN
Ordered Locus Names:b3307, JW3269
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length101 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00537

Subunit structure

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

Sequence similarities

Belongs to the ribosomal protein S14P family.

Mass spectrometry

Molecular mass is 11449.3 Da from positions 2 - 101. Determined by MALDI. Ref.5

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 10110030S ribosomal protein S14 HAMAP-Rule MF_00537
PRO_0000130890

Experimental info

Sequence conflict921E → Q AA sequence Ref.1
Sequence conflict99 – 1013ASW → G in CAA25718. Ref.2

Secondary structure

.......................... 101
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AG59 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E2B21D9D3752352C

FASTA10111,580
        10         20         30         40         50         60 
MAKQSMKARE VKRVALADKY FAKRAELKAI ISDVNASDED RWNAVLKLQT LPRDSSPSRQ 

        70         80         90        100 
RNRCRQTGRP HGFLRKFGLS RIKVREAAMR GEIPGLKKAS W 

« Hide

References

« Hide 'large scale' references
[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]"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.
[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]"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
X01563 Genomic DNA. Translation: CAA25718.1.
U18997 Genomic DNA. Translation: AAA58104.1.
U00096 Genomic DNA. Translation: AAC76332.1.
AP009048 Genomic DNA. Translation: BAE77984.1.
PIRR3EC14. F65123.
RefSeqNP_417766.1. NC_000913.3.
YP_492125.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-N42-101[»]
1P6Gelectron microscopy12.30N2-101[»]
1P87electron microscopy11.50N2-101[»]
1VS5X-ray3.46N1-101[»]
1VS7X-ray3.46N1-101[»]
2AVYX-ray3.46N2-101[»]
2AW7X-ray3.46N2-101[»]
2GY9electron microscopy15.00N41-101[»]
2GYBelectron microscopy15.00N41-101[»]
2I2PX-ray3.22N2-101[»]
2I2UX-ray3.22N2-101[»]
2QALX-ray3.21N2-101[»]
2QANX-ray3.21N2-101[»]
2QB9X-ray3.54N2-101[»]
2QBBX-ray3.54N2-101[»]
2QBDX-ray3.30N2-101[»]
2QBFX-ray3.30N2-101[»]
2QBHX-ray4.00N2-101[»]
2QBJX-ray4.00N2-101[»]
2QOUX-ray3.93N2-101[»]
2QOWX-ray3.93N2-101[»]
2QOYX-ray3.50N2-101[»]
2QP0X-ray3.50N2-101[»]
2VHOX-ray3.74N2-101[»]
2VHPX-ray3.74N2-101[»]
2WWLelectron microscopy5.80N2-101[»]
2YKRelectron microscopy9.80N2-101[»]
2Z4KX-ray4.45N2-101[»]
2Z4MX-ray4.45N2-101[»]
3DF1X-ray3.50N2-101[»]
3DF3X-ray3.50N2-101[»]
3E1Aelectron microscopy-G1-101[»]
3E1Celectron microscopy-G1-101[»]
3FIHelectron microscopy6.70N2-101[»]
3I1MX-ray3.19N1-101[»]
3I1OX-ray3.19N1-101[»]
3I1QX-ray3.81N1-101[»]
3I1SX-ray3.81N1-101[»]
3I1ZX-ray3.71N1-101[»]
3I21X-ray3.71N1-101[»]
3IZVelectron microscopy-R1-101[»]
3IZWelectron microscopy-R1-101[»]
3J00electron microscopy-N2-101[»]
3J0Uelectron microscopy12.10Q2-101[»]
3J0Velectron microscopy14.70Q2-101[»]
3J0Xelectron microscopy13.50Q2-101[»]
3J0Zelectron microscopy11.50Q2-101[»]
3J10electron microscopy11.50Q2-101[»]
3J13electron microscopy13.10P2-101[»]
3J18electron microscopy8.30N2-101[»]
3J36electron microscopy9.80N2-101[»]
3J4Velectron microscopy12.00N1-101[»]
3J4Welectron microscopy12.00N1-101[»]
3J4Yelectron microscopy17.00N1-101[»]
3J4Zelectron microscopy20.00N1-101[»]
3J53electron microscopy13.00N1-101[»]
3J55electron microscopy15.00N1-101[»]
3J57electron microscopy17.00N1-101[»]
3J59electron microscopy12.00N1-101[»]
3J5Belectron microscopy17.00N1-101[»]
3J5Delectron microscopy17.00N1-101[»]
3J5Felectron microscopy20.00N1-101[»]
3J5Helectron microscopy15.00N1-101[»]
3J5Jelectron microscopy9.00N1-101[»]
3J5Nelectron microscopy6.80N1-101[»]
3J5Telectron microscopy7.60N2-101[»]
3J5Xelectron microscopy7.60N2-101[»]
3KC4electron microscopy-N1-101[»]
3OAQX-ray3.25N2-101[»]
3OARX-ray3.25N2-101[»]
3OFAX-ray3.19N2-101[»]
3OFBX-ray3.19N2-101[»]
3OFOX-ray3.10N2-101[»]
3OFPX-ray3.10N2-101[»]
3OFXX-ray3.29N2-101[»]
3OFYX-ray3.29N2-101[»]
3OR9X-ray3.30N1-101[»]
3ORAX-ray3.30N1-101[»]
3SFSX-ray3.20N1-101[»]
3UOQX-ray3.70N1-101[»]
4A2Ielectron microscopy16.50N2-101[»]
4ADVelectron microscopy13.50N2-101[»]
4GAQX-ray3.30N1-101[»]
4GASX-ray3.30N1-101[»]
4GD1X-ray3.00N2-101[»]
4GD2X-ray3.00N2-101[»]
4KIYX-ray2.90N1-101[»]
4KJ0X-ray2.90N1-101[»]
4KJ2X-ray2.90N1-101[»]
4KJ4X-ray2.90N1-101[»]
4KJ6X-ray2.90N1-101[»]
4KJ8X-ray2.90N1-101[»]
4KJAX-ray2.90N1-101[»]
4KJCX-ray2.90N1-101[»]
ProteinModelPortalP0AG59.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35805N.
IntActP0AG59. 70 interactions.
MINTMINT-1295909.
STRING511145.b3307.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0AG59.
PRIDEP0AG59.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76332; AAC76332; b3307.
BAE77984; BAE77984; BAE77984.
GeneID12934450.
947801.
KEGGecj:Y75_p3869.
eco:b3307.
PATRIC32122046. VBIEscCol129921_3400.

Organism-specific databases

EchoBASEEB0906.
EcoGeneEG10913. rpsN.

Phylogenomic databases

eggNOGCOG0199.
HOGENOMHOG000039864.
KOK02954.
OMARIRNRCW.
OrthoDBEOG6BCT0K.
PhylomeDBP0AG59.

Enzyme and pathway databases

BioCycEcoCyc:EG10913-MONOMER.
ECOL316407:JW3269-MONOMER.

Gene expression databases

GenevestigatorP0AG59.

Family and domain databases

HAMAPMF_00537. Ribosomal_S14_1.
InterProIPR001209. Ribosomal_S14.
IPR023036. Ribosomal_S14_bac/plaastid.
IPR018271. Ribosomal_S14_CS.
[Graphical view]
PANTHERPTHR19836. PTHR19836. 1 hit.
PfamPF00253. Ribosomal_S14. 1 hit.
[Graphical view]
PROSITEPS00527. RIBOSOMAL_S14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AG59.
PROP0AG59.

Entry information

Entry nameRS14_ECOLI
AccessionPrimary (citable) accession number: P0AG59
Secondary accession number(s): P02370, Q2M6X2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 90 of the entry and version 2 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