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P02358

- RS6_ECOLI

UniProt

P02358 - RS6_ECOLI

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Protein

30S ribosomal protein S6

Gene

rpsF

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

Functioni

Binds together with S18 to 16S ribosomal RNA.

GO - Molecular functioni

  1. mRNA 5'-UTR binding Source: EcoCyc
  2. small ribosomal subunit rRNA binding Source: EcoCyc
  3. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10905-MONOMER.
ECOL316407:JW4158-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S6
Cleaved into the following 2 chains:
Gene namesi
Name:rpsF
Ordered Locus Names:b4200, JW4158
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10905. rpsF.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13513530S ribosomal protein S6, fully modified isoformPRO_0000030640Add
BLAST
Chaini1 – 13113130S ribosomal protein S6, non-modified isoformPRO_0000030641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931N6-acetyllysine1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP02358.
PRIDEiP02358.

2D gel databases

SWISS-2DPAGEP02358.

Expressioni

Gene expression databases

GenevestigatoriP02358.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Interacts weakly with L2 in one of the 3.5 A resolved structures (PubMed:16272117).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
rpsRP0A7T74EBI-543068,EBI-548844

Protein-protein interaction databases

DIPiDIP-10782N.
IntActiP02358. 57 interactions.
MINTiMINT-1279331.
STRINGi511145.b4200.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43
Beta strandi7 – 104
Helixi12 – 176
Helixi18 – 3114
Beta strandi35 – 373
Beta strandi40 – 456
Beta strandi53 – 553
Beta strandi57 – 615
Beta strandi64 – 663
Helixi68 – 8013
Beta strandi82 – 865
Beta strandi88 – 903

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4PE9X-ray2.95F1-100[»]
4PEAX-ray2.95F1-100[»]
4TOLX-ray3.00F1-100[»]
4TONX-ray3.00F1-100[»]
4TOUX-ray2.90F1-100[»]
4TOWX-ray2.90F1-100[»]
4TP0X-ray2.90F1-100[»]
4TP2X-ray2.90F1-100[»]
4TP4X-ray2.90F1-100[»]
4TP6X-ray2.90F1-100[»]
4TP8X-ray2.80F1-100[»]
4TPAX-ray2.80F1-100[»]
4TPCX-ray2.80F1-100[»]
4TPEX-ray2.80F1-100[»]
ProteinModelPortaliP02358.
SMRiP02358. Positions 1-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02358.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S6P family.Curated

Phylogenomic databases

eggNOGiCOG0360.
HOGENOMiHOG000040438.
InParanoidiP02358.
KOiK02990.
OMAiIRNMIMR.
PhylomeDBiP02358.

Family and domain databases

Gene3Di3.30.70.60. 1 hit.
HAMAPiMF_00360. Ribosomal_S6.
InterProiIPR000529. Ribosomal_S6.
IPR020815. Ribosomal_S6_CS.
IPR020814. Ribosomal_S6_plastid/chlpt.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
[Graphical view]
PfamiPF01250. Ribosomal_S6. 1 hit.
[Graphical view]
SUPFAMiSSF54995. SSF54995. 1 hit.
TIGRFAMsiTIGR00166. S6. 1 hit.
PROSITEiPS01048. RIBOSOMAL_S6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02358-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRHYEIVFMV HPDQSEQVPG MIERYTAAIT GAEGKIHRLE DWGRRQLAYP
60 70 80 90 100
INKLHKAHYV LMNVEAPQEV IDELETTFRF NDAVIRSMVM RTKHAVTEAS
110 120 130
PMVKAKDERR ERRDDFANET ADDAEAGDSE EEEEE
Length:135
Mass (Da):15,703
Last modified:July 21, 1986 - v1
Checksum:iF4CC629711C1FD0E
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141Q → T AA sequence (PubMed:9868784)Curated
Sequence conflicti20 – 201G → A AA sequence (PubMed:9868784)Curated

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiC65231. R3EC6.
RefSeqiNP_418621.5. NC_000913.3.
YP_492342.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77157; AAC77157; b4200.
BAE78201; BAE78201; BAE78201.
GeneIDi12930647.
948723.
KEGGiecj:Y75_p4086.
eco:b4200.
PATRICi48667972. VBIEscCol107702_4239.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRi C65231. R3EC6.
RefSeqi NP_418621.5. NC_000913.3.
YP_492342.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EG0 electron microscopy 11.50 C 1-97 [» ]
1M5G model - F 1-100 [» ]
1P6G electron microscopy 12.30 F 1-135 [» ]
1P87 electron microscopy 11.50 F 1-135 [» ]
1VS5 X-ray 3.46 F 1-135 [» ]
1VS7 X-ray 3.46 F 1-135 [» ]
2AVY X-ray 3.46 F 1-135 [» ]
2AW7 X-ray 3.46 F 1-135 [» ]
2GY9 electron microscopy 15.00 F 1-95 [» ]
2GYB electron microscopy 15.00 F 1-95 [» ]
2I2P X-ray 3.22 F 1-135 [» ]
2I2U X-ray 3.22 F 1-135 [» ]
2QAL X-ray 3.21 F 1-135 [» ]
2QAN X-ray 3.21 F 1-135 [» ]
2QB9 X-ray 3.54 F 1-135 [» ]
2QBB X-ray 3.54 F 1-135 [» ]
2QBD X-ray 3.30 F 1-135 [» ]
2QBF X-ray 3.30 F 1-135 [» ]
2QBH X-ray 4.00 F 1-135 [» ]
2QBJ X-ray 4.00 F 1-135 [» ]
2QOU X-ray 3.93 F 1-135 [» ]
2QOW X-ray 3.93 F 1-135 [» ]
2QOY X-ray 3.50 F 1-135 [» ]
2QP0 X-ray 3.50 F 1-135 [» ]
2VHO X-ray 3.74 F 1-135 [» ]
2VHP X-ray 3.74 F 1-135 [» ]
2WWL electron microscopy 5.80 F 1-100 [» ]
2YKR electron microscopy 9.80 F 1-100 [» ]
2Z4K X-ray 4.45 F 1-135 [» ]
2Z4M X-ray 4.45 F 1-135 [» ]
3DF1 X-ray 3.50 F 1-135 [» ]
3DF3 X-ray 3.50 F 1-135 [» ]
3E1A electron microscopy - T 1-135 [» ]
3E1C electron microscopy - T 1-135 [» ]
3FIH electron microscopy 6.70 F 1-100 [» ]
3I1M X-ray 3.19 F 1-135 [» ]
3I1O X-ray 3.19 F 1-135 [» ]
3I1Q X-ray 3.81 F 1-135 [» ]
3I1S X-ray 3.81 F 1-135 [» ]
3I1Z X-ray 3.71 F 1-135 [» ]
3I21 X-ray 3.71 F 1-135 [» ]
3IY8 electron microscopy 14.10 F 2-100 [» ]
3IZV electron microscopy - J 1-135 [» ]
3IZW electron microscopy - J 1-135 [» ]
3J00 electron microscopy - F 1-135 [» ]
3J0U electron microscopy 12.10 I 1-135 [» ]
3J0V electron microscopy 14.70 I 1-135 [» ]
3J0X electron microscopy 13.50 I 1-135 [» ]
3J0Z electron microscopy 11.50 I 1-135 [» ]
3J10 electron microscopy 11.50 I 1-135 [» ]
3J13 electron microscopy 13.10 H 1-135 [» ]
3J18 electron microscopy 8.30 F 1-100 [» ]
3J36 electron microscopy 9.80 F 1-135 [» ]
3J4V electron microscopy 12.00 F 1-100 [» ]
3J4W electron microscopy 12.00 F 1-100 [» ]
3J4Y electron microscopy 17.00 F 1-100 [» ]
3J4Z electron microscopy 20.00 F 1-100 [» ]
3J53 electron microscopy 13.00 F 1-100 [» ]
3J55 electron microscopy 15.00 F 1-100 [» ]
3J57 electron microscopy 17.00 F 1-100 [» ]
3J59 electron microscopy 12.00 F 1-100 [» ]
3J5B electron microscopy 17.00 F 1-100 [» ]
3J5D electron microscopy 17.00 F 1-100 [» ]
3J5F electron microscopy 20.00 F 1-100 [» ]
3J5H electron microscopy 15.00 F 1-100 [» ]
3J5J electron microscopy 9.00 F 1-100 [» ]
3J5N electron microscopy 6.80 F 1-135 [» ]
3J5T electron microscopy 7.60 F 1-131 [» ]
3J5X electron microscopy 7.60 F 1-131 [» ]
3KC4 electron microscopy - F 1-135 [» ]
3OAQ X-ray 3.25 F 1-100 [» ]
3OAR X-ray 3.25 F 1-100 [» ]
3OFA X-ray 3.19 F 1-100 [» ]
3OFB X-ray 3.19 F 1-100 [» ]
3OFO X-ray 3.10 F 1-100 [» ]
3OFP X-ray 3.10 F 1-100 [» ]
3OFX X-ray 3.29 F 1-100 [» ]
3OFY X-ray 3.29 F 1-100 [» ]
3OR9 X-ray 3.30 F 1-135 [» ]
3ORA X-ray 3.30 F 1-135 [» ]
3SFS X-ray 3.20 F 1-131 [» ]
3UOQ X-ray 3.70 F 1-135 [» ]
4A2I electron microscopy 16.50 F 1-100 [» ]
4ADV electron microscopy 13.50 F 1-135 [» ]
4GAQ X-ray 3.30 F 1-135 [» ]
4GAS X-ray 3.30 F 1-135 [» ]
4GD1 X-ray 3.00 F 1-100 [» ]
4GD2 X-ray 3.00 F 1-100 [» ]
4KIY X-ray 2.90 F 1-135 [» ]
4KJ0 X-ray 2.90 F 1-135 [» ]
4KJ2 X-ray 2.90 F 1-135 [» ]
4KJ4 X-ray 2.90 F 1-135 [» ]
4KJ6 X-ray 2.90 F 1-135 [» ]
4KJ8 X-ray 2.90 F 1-135 [» ]
4KJA X-ray 2.90 F 1-135 [» ]
4KJC X-ray 2.90 F 1-135 [» ]
4PE9 X-ray 2.95 F 1-100 [» ]
4PEA X-ray 2.95 F 1-100 [» ]
4TOL X-ray 3.00 F 1-100 [» ]
4TON X-ray 3.00 F 1-100 [» ]
4TOU X-ray 2.90 F 1-100 [» ]
4TOW X-ray 2.90 F 1-100 [» ]
4TP0 X-ray 2.90 F 1-100 [» ]
4TP2 X-ray 2.90 F 1-100 [» ]
4TP4 X-ray 2.90 F 1-100 [» ]
4TP6 X-ray 2.90 F 1-100 [» ]
4TP8 X-ray 2.80 F 1-100 [» ]
4TPA X-ray 2.80 F 1-100 [» ]
4TPC X-ray 2.80 F 1-100 [» ]
4TPE X-ray 2.80 F 1-100 [» ]
ProteinModelPortali P02358.
SMRi P02358. Positions 1-129.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10782N.
IntActi P02358. 57 interactions.
MINTi MINT-1279331.
STRINGi 511145.b4200.

Chemistry

ChEMBLi CHEMBL2363135.

2D gel databases

SWISS-2DPAGE P02358.

Proteomic databases

PaxDbi P02358.
PRIDEi P02358.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77157 ; AAC77157 ; b4200 .
BAE78201 ; BAE78201 ; BAE78201 .
GeneIDi 12930647.
948723.
KEGGi ecj:Y75_p4086.
eco:b4200.
PATRICi 48667972. VBIEscCol107702_4239.

Organism-specific databases

EchoBASEi EB0898.
EcoGenei EG10905. rpsF.

Phylogenomic databases

eggNOGi COG0360.
HOGENOMi HOG000040438.
InParanoidi P02358.
KOi K02990.
OMAi IRNMIMR.
PhylomeDBi P02358.

Enzyme and pathway databases

BioCyci EcoCyc:EG10905-MONOMER.
ECOL316407:JW4158-MONOMER.

Miscellaneous databases

EvolutionaryTracei P02358.
PROi P02358.

Gene expression databases

Genevestigatori P02358.

Family and domain databases

Gene3Di 3.30.70.60. 1 hit.
HAMAPi MF_00360. Ribosomal_S6.
InterProi IPR000529. Ribosomal_S6.
IPR020815. Ribosomal_S6_CS.
IPR020814. Ribosomal_S6_plastid/chlpt.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
[Graphical view ]
Pfami PF01250. Ribosomal_S6. 1 hit.
[Graphical view ]
SUPFAMi SSF54995. SSF54995. 1 hit.
TIGRFAMsi TIGR00166. S6. 1 hit.
PROSITEi PS01048. RIBOSOMAL_S6. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS6_ECOLI
AccessioniPrimary (citable) accession number: P02358
Secondary accession number(s): Q2M6A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 160 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

External Data

Dasty 3