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Sample Preparation and Post-separation Analysis



Searching in 'SWISS-2DPAGE' for entry matching: EFTU2_ECOLI




SWISS-2DPAGE:  EFTU2_ECOLI


EFTU2_ECOLI


General information about the entry
View entry in simple text format
Entry nameEFTU2_ECOLI
Primary accession numberP0CE48
Secondary accession number(s) P02990 P0A6N1
integrated into SWISS-2DPAGE on August 1, 1995 (release 2)
2D Annotations were last modified onMay 15, 2003 (version 5)
General Annotations were last modified on May 19, 2011 (version 12)
Name and origin of the protein
DescriptionRecName: Full=Elongation factor Tu 2; Short=EF-Tu 2; AltName: Full=P-43;.
Gene nameName=tufB
OrderedLocusNames=b3980, JW3943
Annotated speciesEscherichia coli [TaxID: 562]
TaxonomyBacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
References
[1]   MAPPING ON GEL
MEDLINE=96314059; PubMed=8740179; [NCBI, ExPASy, EBI, Israel, Japan]
Pasquali C., Frutiger S., Wilkins M.R., Hughes G.J., Appel R.D., Bairoch A., Schaller D., Sanchez J.-C., Hochstrasser D.F.
''''''Two-dimensional gel electrophoresis of Escherichia coli homogenates: the Escherichia coli SWISS-2DPAGE database'';'';''
Electrophoresis 17(1):547-555(1996)
[2]   MAPPING ON GEL
Vanbogelen R.A., Abshire K.Z., Pertsemlidis A., Clark R.L., Neidhardt F.C.
''''''Gene-protein database of Escherichia coli K-12, edition 6'';'';''
(IN) Neidhardt et al. (eds.)Escherichia coli and Salmonella: Cellular and Molecular Biology (2nd ed.), pp.2067-2117, ASM Press, Washington DC (1996)
[3]   MAPPING ON GEL
MEDLINE=80159887; PubMed=6988414; [NCBI, ExPASy, EBI, Israel, Japan]
Bloch P.L., Phillips T.A., Neidhardt F.C.
''''''Protein identifications of O'Farrell two-dimensional gels: locations of 81 Escherichia coli proteins'';'';''
J. Bacteriol. 141(1):1409-1420(1980)
[4]   PROTEIN EXPRESSION
MEDLINE=79216190; PubMed=156716; [NCBI, ExPASy, EBI, Israel, Japan]
Herendeen S.L., Vanbogelen R.A., Neidhardt F.C.
''''''Levels of major proteins of Escherichia coli during growth at different temperatures'';'';''
J. Bacteriol. 139(1):185-194(1979)
[5]   PROTEIN EXPRESSION
MEDLINE=78212912; PubMed=352533; [NCBI, ExPASy, EBI, Israel, Japan]
Pedersen S., Bloch P.L., Reeh S., Neidhardt F.C.
''''''Patterns of protein synthesis in E. coli: a catalog of the amount of 140 individual proteins at different growth rates'';'';''
Cell 14(1):179-190(1978)
[6]   MAPPING ON GEL
PubMed=11680886; [NCBI, ExPASy, EBI, Israel, Japan]
Tonella L., Hoogland C., Binz P.-A., Appel R.D., Hochstrasser D.F., Sanchez J.-C.
''''''New perspectives in the Escherichia coli proteome investigation'';'';''
Proteomics 1(1):409-423(2001)
[7]   MAPPING ON GEL
PubMed=12469338; [NCBI, ExPASy, EBI, Israel, Japan]
Yan J.X., Devenish A.T., Wait R., Stone T., Lewis S., Fowler S.
''''''Fluorescence 2-D difference gel electrophoresis and mass spectrometry based proteomic analysis of E. coli'';'';''
Proteomics 2(1):1682-1698(2002)
Comments
  • SUBUNIT: MONOMER
2D PAGE maps for identified proteins
How to interpret a protein

ECOLI {Escherichia coli}
Escherichia coli
ECOLI
  map experimental info
  protein estimated location
 
ECOLI

MAP LOCATIONS:
pI=5.32; Mw=44704

EXPRESSION:
CHANGED VERY LITTLE THROUGHOUT THE NORMAL ARRHENIUS TEMPERATURE RANGE (23 TO 37°C) [4]; INCREASED IN LEVEL WITH INCREASING GROWTH RATE [5].

MAPPING (identification):
GEL MATCHING [1] AND IDENTIFIED ON 2-D GELS BY VANBOGELEN [2] AND BLOCH [3].



ECOLI4.5-5.5 {Escherichia coli(4.5-5.5)}
Escherichia coli
ECOLI4.5-5.5
  map experimental info
  protein estimated location
 
ECOLI4.5-5.5

MAP LOCATIONS:
pI=5.58; Mw=45311  [identification data]
pI=5.14; Mw=30129  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [6].



ECOLI5-6 {Escherichia coli(5-6)}
Escherichia coli
ECOLI5-6
  map experimental info
  protein estimated location
 
ECOLI5-6

MAP LOCATIONS:
pI=5.39; Mw=51249  [identification data]
pI=5.20; Mw=51059  [identification data]
pI=5.32; Mw=50990  [identification data]
pI=5.35; Mw=50921  [identification data]
pI=5.34; Mw=50034  [identification data]
pI=5.31; Mw=48144  [identification data]
pI=5.33; Mw=47448  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [6].



ECOLI-DIGE4.5-6.5 {Escherichia coli DIGE (4.5-6.5)}
Escherichia coli
ECOLI-DIGE4.5-6.5
  map experimental info
  protein estimated location
 
ECOLI-DIGE4.5-6.5

MAP LOCATIONS:
pI=5.38; Mw=41860  [identification data]
pI=5.40; Mw=42307  [identification data]
pI=5.07; Mw=32442  [identification data]
pI=5.69; Mw=25098  [identification data]

EXPRESSION:
increase after benzoic acid treatment [7].

MAPPING (identification):
SPOTS 1WL*: Peptide mass fingerprinting [7]; SPOTS 1WQY, 1WTU, 1WLU: Tandem mass spectrometry [7].

Copyright
This SWISS-2DPAGE entry is copyright the Swiss Institute of Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://world-2dpage.expasy.org/swiss-2dpage/docs/license.html or send email from license@isb-sib.ch).
Cross-references
2DBase-EcoliP0A6N1; EFTU_ECOLI.
ECO2DBASEE042.0; 6TH EDITION.
UniProtKB/Swiss-ProtP0CE48; EFTU2_ECOLI.
2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 2011_10
Entry nameEFTU2_ECOLI
Primary accession numberP0CE48
Secondary accession number(s) O68929 P02990 P0A6N1 Q2M704 Q2M8R6 Q8X4S9 Q8XED3
Sequence was last modified on March 23, 2010 (version 1)
Annotations were last modified on October 19, 2011 (version 13)
Name and origin of the protein
DescriptionRecName: Full=Elongation factor Tu 2; Short=EF-Tu 2; AltName: Full=P-43;
Gene nameName=tufB
OrderedLocusNames=b3980, JW3943
Encoded onName=tufB; OrderedLocusNames=b3980, JW3943
Keywords3D-structure; Acetylation; Antibiotic resistance; Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding; Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLX57091; CAA40370.1; -; Genomic_DNA
EMBLJ01717; AAA24669.1; -; Genomic_DNA
EMBLU00006; AAC43078.1; -; Genomic_DNA
EMBLU00096; AAC76954.1; -; Genomic_DNA
EMBLAP009048; BAE77340.1; -; Genomic_DNA
PIRA91478; EFECT; .
RefSeqNP_418407.1; NC_000913.2; .
PDB1DG1; X-ray; 2.50 A; G/H=1-394
PDB1EFM; X-ray; 2.70 A; A=2-394
PDB1EFU; X-ray; 2.50 A; A/C=10-394
PDB1LS2; EM; 16.80 A; A=2-394
PDB1OB2; X-ray; 3.35 A; A=3-394
PDB1QZD; EM; -; A=2-394
PDB2BVN; X-ray; 2.30 A; A/B=2-394
PDB3EP2; EM; -; X=2-394
PDB3EQ3; EM; -; X=2-394
PDB3EQ4; EM; -; X=2-394
PDB3FIH; EM; 6.70 A; Z=2-394
PDB3IZV; EM; -; C=2-394
PDB3IZW; EM; -; C=2-394
PDB3MMP; X-ray; 2.50 A; A/C=1-394
PDBsum1DG1; -; .
PDBsum1EFM; -; .
PDBsum1EFU; -; .
PDBsum1LS2; -; .
PDBsum1OB2; -; .
PDBsum1QZD; -; .
PDBsum2BVN; -; .
PDBsum3EP2; -; .
PDBsum3EQ3; -; .
PDBsum3EQ4; -; .
PDBsum3FIH; -; .
PDBsum3IZV; -; .
PDBsum3IZW; -; .
PDBsum3MMP; -; .
ProteinModelPortalP0CE48; -; .
SMRP0CE48; 9-394; .
2DBase-EcoliP0A6N1; -; .
ECO2DBASEE042.0; 6TH EDITION; .
PRIDEP0CE48; -; .
EnsemblBacteriaEBESCT00000001015; EBESCP00000001015; EBESCG00000000836; .
EnsemblBacteriaEBESCT00000015379; EBESCP00000014670; EBESCG00000014439; .
GeneID948482; -; .
GenomeReviewsAP009048_GR; JW3943; .
GenomeReviewsU00096_GR; b3980; .
KEGGecj:JW3943; -; .
KEGGeco:b3980; -; .
EchoBASEEB1029; -; .
EchoBASEEB1030; -; .
EcoGeneEG11037; tufB; .
GeneTreeEBGT00050000008366; -; .
OMAMEKGLRF; -; .
BioCycEcoCyc:EG11037-MONOMER; -; .
GenevestigatorP0A6N1; -; .
GOGO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell; .
GOGO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell; .
GOGO:0005525; F:GTP binding; IEA:UniProtKB-KW; .
GOGO:0003924; F:GTPase activity; IEA:InterPro; .
GOGO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW; .
GOGO:0046677; P:response to antibiotic; IEA:UniProtKB-KW; .
HAMAPMF_00118_B; EF_Tu_B; 1; -
InterProIPR000795; ProtSyn_GTP-bd; .
InterProIPR005225; Small_GTP-bd_dom; .
InterProIPR009001; Transl_elong_EF1A/Init_IF2_C; .
InterProIPR004161; Transl_elong_EFTu/EF1A_2; .
InterProIPR004541; Transl_elong_EFTu/EF1A_bac/org; .
InterProIPR004160; Transl_elong_EFTu/EF1A_C; .
InterProIPR009000; Transl_elong_init/rib_B-barrel; .
PANTHERPTHR23115:SF31; Transl_elong_EFTu/EF1A_bac/org; 1; .
PfamPF00009; GTP_EFTU; 1; .
PfamPF03144; GTP_EFTU_D2; 1; .
PfamPF03143; GTP_EFTU_D3; 1; .
PRINTSPR00315; ELONGATNFCT; .
SUPFAMSSF50465; Elong_init_C; 1; .
SUPFAMSSF50447; Translat_factor; 1; .
TIGRFAMsTIGR00485; EF-Tu; 1; .
TIGRFAMsTIGR00231; Small_GTP; 1; .
PROSITEPS00301; EFACTOR_GTP; 1; .



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