Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P0AG59 (RS14_ECOLI)

Last modified June 16, 2009. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    30S ribosomal protein S14
Gene names
Name: rpsN
Ordered Locus Names: b3307, JW3269
OrganismEscherichia coli (strain K12) [Complete 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 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

Ontologies

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionrRNA binding

Inferred from electronic annotation. Source: HAMAP

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 10110030S ribosomal protein S14 HAMAP 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
P0AG59-1 [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: 6222285] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 10094780] [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: 12244297] [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: 12809609] [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: 16272117] [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

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.
RefSeqAP_004483.1.
NP_417766.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-N42-101[»]
1P6Gelectron microscopy12.30N1-101[»]
1P87electron microscopy11.50N1-101[»]
1VS5X-ray3.46N1-101[»]
1VS7X-ray3.46N1-101[»]
2AVYX-ray3.46N1-101[»]
2AW7X-ray3.46N1-101[»]
2GY9electron microscopy-N41-100[»]
2GYBelectron microscopy-N41-100[»]
2I2PX-ray3.22N2-100[»]
2I2UX-ray3.22N2-100[»]
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[»]
2Z4KX-ray4.45N2-101[»]
2Z4MX-ray4.45N2-101[»]
3DF1X-ray3.50N2-101[»]
3DF3X-ray3.50N2-101[»]
3FIHelectron microscopy-N2-101[»]
ModBaseSearch...

Genome annotation databases

GeneID947801.
GenomeReviewsGene locus JW3269 in contig AP009048_GR.
Gene locus b3307 in contig U00096_GR.
KEGGecj:JW3269.
eco:b3307.

Organism-specific databases

EchoBASEEB0906.
EcoGeneEG10913. rpsN.
CMRSearch...

Phylogenomic databases

HOGENOMP0AG59.
OMAP0AG59. RLEIHRK.

Enzyme and pathway databases

BioCycEcoCyc:EG10913-MON.

Family and domain databases

HAMAPMF_00537.
[Tree]
InterProIPR001209. Ribosomal_S14.
IPR018271. Ribosomal_S14_CS.
[Graphical view]
PANTHERPTHR19836. Ribosomal_S14. 1 hit.
PfamPF00253. Ribosomal_S14. 1 hit.
[Graphical view]
PROSITEPS00527. RIBOSOMAL_S14. 1 hit.
[Graphical view]
ProtoNetSearch...

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 16, 2009
This is version 41 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents