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P02358 (RS6_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. 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 S6
Gene names
Name:rpsF
Ordered Locus Names:b4200, JW4158
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds together with S18 to 16S ribosomal RNA. HAMAP-Rule MF_00360

Subunit structure

Part of the 30S ribosomal subunit. Interacts weakly with L2 in one of the 3.5 A resolved structures (Ref.15).

Post-translational modification

5 different forms of the protein, varying only in the number of C-terminal glutamate residues, were isolated. The sequence shown is form S6-6, which is the longest. The first two Glu are encoded by the rpsF gene, the other Glu are added post-translationally by the RimK enzyme. HAMAP-Rule MF_00360

Sequence similarities

Belongs to the ribosomal protein S6P family.

Mass spectrometry

Molecular mass is 15187.2 Da from positions 1 - 131. Determined by MALDI. Ref.11

Sequence caution

The sequence AAA97096.1 differs from that shown. Reason: Up to 4 Glu residues can be added post-translationally.

The sequence AAC77157.5 differs from that shown. Reason: Up to 4 Glu residues can be added post-translationally.

The sequence BAE78201.1 differs from that shown. Reason: Up to 4 Glu residues can be added post-translationally.

The sequence CAA27652.1 differs from that shown. Reason: Up to 4 Glu residues can be added post-translationally.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13513530S ribosomal protein S6, fully modified isoform HAMAP-Rule MF_00360
PRO_0000030640
Chain1 – 13113130S ribosomal protein S6, non-modified isoform HAMAP-Rule MF_00360
PRO_0000030641

Amino acid modifications

Modified residue931N6-acetyllysine Ref.12

Experimental info

Sequence conflict141Q → T AA sequence Ref.6
Sequence conflict201G → A AA sequence Ref.6

Secondary structure

........................ 135
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02358 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F4CC629711C1FD0E

FASTA13515,703
        10         20         30         40         50         60 
MRHYEIVFMV HPDQSEQVPG MIERYTAAIT GAEGKIHRLE DWGRRQLAYP INKLHKAHYV 

        70         80         90        100        110        120 
LMNVEAPQEV IDELETTFRF NDAVIRSMVM RTKHAVTEAS PMVKAKDERR ERRDDFANET 

       130 
ADDAEAGDSE EEEEE 

« Hide

References

« Hide 'large scale' references
[1]"Determination of the complete amino-acid sequence of protein S6 from the wild-type and a mutant of Escherichia coli."
Hitz H., Schaefer D., Wittmann-Liebold B.
Eur. J. Biochem. 75:497-512(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: K.
[2]"The nucleotide sequence of an Escherichia coli chromosomal region containing the genes for ribosomal proteins S6, S18, L9 and an open reading frame."
Schnier J., Kitakawa M., Isono K.
Mol. Gen. Genet. 204:126-132(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131.
[3]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-131.
Strain: K12 / MG1655 / ATCC 47076.
[4]"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] OF 1-131.
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] OF 1-131.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Small genes/gene-products in Escherichia coli K-12."
Wasinger V.C., Humphery-Smith I.
FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20.
Strain: K12.
[7]Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.
Submitted (SEP-1994) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-11.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"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.
[9]"Protein identification with N and C-terminal sequence tags in proteome projects."
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-4.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]"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.
[11]"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.
[12]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[13]"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.
[14]"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.
[15]"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
X04022 Genomic DNA. Translation: CAA27652.1. Sequence problems.
U14003 Genomic DNA. Translation: AAA97096.1. Sequence problems.
U00096 Genomic DNA. Translation: AAC77157.5. Sequence problems.
AP009048 Genomic DNA. Translation: BAE78201.1. Sequence problems.
PIRR3EC6. C65231.
RefSeqNP_418621.5. NC_000913.3.
YP_492342.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50C1-97[»]
1M5Gmodel-F1-100[»]
1P6Gelectron microscopy12.30F1-135[»]
1P87electron microscopy11.50F1-135[»]
1VS5X-ray3.46F1-135[»]
1VS7X-ray3.46F1-135[»]
2AVYX-ray3.46F1-135[»]
2AW7X-ray3.46F1-135[»]
2GY9electron microscopy15.00F1-95[»]
2GYBelectron microscopy15.00F1-95[»]
2I2PX-ray3.22F1-135[»]
2I2UX-ray3.22F1-135[»]
2QALX-ray3.21F1-135[»]
2QANX-ray3.21F1-135[»]
2QB9X-ray3.54F1-135[»]
2QBBX-ray3.54F1-135[»]
2QBDX-ray3.30F1-135[»]
2QBFX-ray3.30F1-135[»]
2QBHX-ray4.00F1-135[»]
2QBJX-ray4.00F1-135[»]
2QOUX-ray3.93F1-135[»]
2QOWX-ray3.93F1-135[»]
2QOYX-ray3.50F1-135[»]
2QP0X-ray3.50F1-135[»]
2VHOX-ray3.74F1-135[»]
2VHPX-ray3.74F1-135[»]
2WWLelectron microscopy5.80F1-100[»]
2YKRelectron microscopy9.80F1-100[»]
2Z4KX-ray4.45F1-135[»]
2Z4MX-ray4.45F1-135[»]
3DF1X-ray3.50F1-135[»]
3DF3X-ray3.50F1-135[»]
3E1Aelectron microscopy-T1-135[»]
3E1Celectron microscopy-T1-135[»]
3FIHelectron microscopy6.70F1-100[»]
3I1MX-ray3.19F1-135[»]
3I1OX-ray3.19F1-135[»]
3I1QX-ray3.81F1-135[»]
3I1SX-ray3.81F1-135[»]
3I1ZX-ray3.71F1-135[»]
3I21X-ray3.71F1-135[»]
3IY8electron microscopy14.10F2-100[»]
3IZVelectron microscopy-J1-135[»]
3IZWelectron microscopy-J1-135[»]
3J00electron microscopy-F1-135[»]
3J0Uelectron microscopy12.10I1-135[»]
3J0Velectron microscopy14.70I1-135[»]
3J0Xelectron microscopy13.50I1-135[»]
3J0Zelectron microscopy11.50I1-135[»]
3J10electron microscopy11.50I1-135[»]
3J13electron microscopy13.10H1-135[»]
3J18electron microscopy8.30F1-100[»]
3J36electron microscopy9.80F1-135[»]
3J4Velectron microscopy12.00F1-100[»]
3J4Welectron microscopy12.00F1-100[»]
3J4Yelectron microscopy17.00F1-100[»]
3J4Zelectron microscopy20.00F1-100[»]
3J53electron microscopy13.00F1-100[»]
3J55electron microscopy15.00F1-100[»]
3J57electron microscopy17.00F1-100[»]
3J59electron microscopy12.00F1-100[»]
3J5Belectron microscopy17.00F1-100[»]
3J5Delectron microscopy17.00F1-100[»]
3J5Felectron microscopy20.00F1-100[»]
3J5Helectron microscopy15.00F1-100[»]
3J5Jelectron microscopy9.00F1-100[»]
3J5Nelectron microscopy6.80F1-135[»]
3J5Telectron microscopy7.60F1-131[»]
3J5Xelectron microscopy7.60F1-131[»]
3KC4electron microscopy-F1-135[»]
3OAQX-ray3.25F1-100[»]
3OARX-ray3.25F1-100[»]
3OFAX-ray3.19F1-100[»]
3OFBX-ray3.19F1-100[»]
3OFOX-ray3.10F1-100[»]
3OFPX-ray3.10F1-100[»]
3OFXX-ray3.29F1-100[»]
3OFYX-ray3.29F1-100[»]
3OR9X-ray3.30F1-135[»]
3ORAX-ray3.30F1-135[»]
3SFSX-ray3.20F1-131[»]
3UOQX-ray3.70F1-135[»]
4A2Ielectron microscopy16.50F1-100[»]
4ADVelectron microscopy13.50F1-135[»]
4GAQX-ray3.30F1-135[»]
4GASX-ray3.30F1-135[»]
4GD1X-ray3.00F1-100[»]
4GD2X-ray3.00F1-100[»]
4KIYX-ray2.90F1-135[»]
4KJ0X-ray2.90F1-135[»]
4KJ2X-ray2.90F1-135[»]
4KJ4X-ray2.90F1-135[»]
4KJ6X-ray2.90F1-135[»]
4KJ8X-ray2.90F1-135[»]
4KJAX-ray2.90F1-135[»]
4KJCX-ray2.90F1-135[»]
ProteinModelPortalP02358.
SMRP02358. Positions 1-129.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10782N.
IntActP02358. 57 interactions.
MINTMINT-1279331.
STRING511145.b4200.

Chemistry

ChEMBLCHEMBL2363135.

2D gel databases

SWISS-2DPAGEP02358.

Proteomic databases

PaxDbP02358.
PRIDEP02358.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77157; AAC77157; b4200.
BAE78201; BAE78201; BAE78201.
GeneID12930647.
948723.
KEGGecj:Y75_p4086.
eco:b4200.
PATRIC48667972. VBIEscCol107702_4239.

Organism-specific databases

EchoBASEEB0898.
EcoGeneEG10905. rpsF.

Phylogenomic databases

eggNOGCOG0360.
HOGENOMHOG000040438.
KOK02990.
OMAITEASPM.
PhylomeDBP02358.
ProtClustDBPRK00453.

Enzyme and pathway databases

BioCycEcoCyc:EG10905-MONOMER.
ECOL316407:JW4158-MONOMER.

Gene expression databases

GenevestigatorP02358.

Family and domain databases

Gene3D3.30.70.60. 1 hit.
HAMAPMF_00360. Ribosomal_S6.
InterProIPR000529. Ribosomal_S6.
IPR020815. Ribosomal_S6_CS.
IPR020814. Ribosomal_S6_plastid/chlpt.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
[Graphical view]
PfamPF01250. Ribosomal_S6. 1 hit.
[Graphical view]
SUPFAMSSF54995. SSF54995. 1 hit.
TIGRFAMsTIGR00166. S6. 1 hit.
PROSITEPS01048. RIBOSOMAL_S6. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02358.
PROP02358.

Entry information

Entry nameRS6_ECOLI
AccessionPrimary (citable) accession number: P02358
Secondary accession number(s): Q2M6A5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 156 of the entry and version 1 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