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SWISS-2DPAGE 
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Sample Preparation and Post-separation Analysis



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




SWISS-2DPAGE:  ATPE_ECOLI


ATPE_ECOLI


General information about the entry
View entry in simple text format
Entry nameATPE_ECOLI
Primary accession numberP0A6E6
Secondary accession number(s) P00832
integrated into SWISS-2DPAGE on August 1, 1995 (release 2)
2D Annotations were last modified onMarch 31, 2004 (version 3)
General Annotations were last modified on May 19, 2011 (version 16)
Name and origin of the protein
DescriptionRecName: Full=ATP synthase epsilon chain; AltName: Full=ATP synthase F1 sector epsilon subunit; AltName: Full=F-ATPase epsilon subunit;.
Gene nameName=atpC
Synonyms=papG, uncC
OrderedLocusNames=b3731, JW3709
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
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)
Comments
  • SUBUNIT: F-TYPE ATPASES HAVE 2 COMPONENTS, CF(1) - THE CATALYTIC CORE - AND CF(0) - THE MEMBRANE PROTON CHANNEL; CF(1) HAS FIVE SUBUNITS: ALPHA(3), BETA(3), GAMMA(1), DELTA(1), EPSILON(1); CF(0) HAS THREE MAIN SUBUNITS: A, B AND C
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=5.48; Mw=14937

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



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=5.34; Mw=10459  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [3].



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

MAP LOCATIONS:
pI=5.45; Mw=13773  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [3].

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 legal@sib.swiss).
Cross-references
UniProtKB/Swiss-ProtP0A6E6; ATPE_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 nameATPE_ECOLI
Primary accession numberP0A6E6
Secondary accession number(s) P00832 Q2M849
Sequence was last modified on January 23, 2007 (version 2)
Annotations were last modified on October 19, 2011 (version 69)
Name and origin of the protein
DescriptionRecName: Full=ATP synthase epsilon chain; AltName: Full=ATP synthase F1 sector epsilon subunit; AltName: Full=F-ATPase epsilon subunit;
Gene nameName=atpC
Synonyms=papG, uncC
OrderedLocusNames=b3731, JW3709
Encoded onName=atpC; Synonyms=papG, uncC; OrderedLocusNames=b3731, JW3709
Keywords3D-structure; ATP synthesis; Cell inner membrane; Cell membrane; CF(1); Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Reference proteome; Transport.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLJ01594; AAA24738.1; -; Genomic_DNA
EMBLX01631; CAA25783.1; -; Genomic_DNA
EMBLV00311; CAA23595.1; -; Genomic_DNA
EMBLM25464; AAA83876.1; -; Genomic_DNA
EMBLV00267; CAA23528.1; ALT_FRAME; Genomic_DNA
EMBLL10328; AAA62083.1; -; Genomic_DNA
EMBLU00096; AAC76754.1; -; Genomic_DNA
EMBLAP009048; BAE77557.1; -; Genomic_DNA
PIRB90106; PWECE; .
RefSeqNP_418187.1; NC_000913.2; .
PDB1AQT; X-ray; 2.30 A; A=4-139
PDB1BSH; NMR; -; A=2-139
PDB1BSN; NMR; -; A=2-139
PDB1FS0; X-ray; 2.10 A; E=2-138
PDB1QO1; X-ray; 3.90 A; J=4-139
PDBsum1AQT; -; .
PDBsum1BSH; -; .
PDBsum1BSN; -; .
PDBsum1FS0; -; .
PDBsum1QO1; -; .
ProteinModelPortalP0A6E6; -; .
SMRP0A6E6; 2-139; .
DIPDIP-47828N; -; .
IntActP0A6E6; 4; .
TCDB3.A.2.1.1; H+- or Na+-translocating F-type; V-type and A-type ATPase (F-ATPase) superfamily; .
SWISS-2DPAGEP0A6E6; -; .
EnsemblBacteriaEBESCT00000000699; EBESCP00000000699; EBESCG00000000585; .
EnsemblBacteriaEBESCT00000000700; EBESCP00000000700; EBESCG00000000585; .
EnsemblBacteriaEBESCT00000000701; EBESCP00000000701; EBESCG00000000585; .
EnsemblBacteriaEBESCT00000017864; EBESCP00000017155; EBESCG00000016920; .
GeneID948245; -; .
GenomeReviewsAP009048_GR; JW3709; .
GenomeReviewsU00096_GR; b3731; .
KEGGecj:JW3709; -; .
KEGGeco:b3731; -; .
EchoBASEEB0098; -; .
EcoGeneEG10100; atpC; .
eggNOGCOG0355; -; .
GeneTreeEBGT00050000011811; -; .
HOGENOMHBG663981; -; .
OMASAEASIF; -; .
ProtClustDBPRK00571; -; .
BioCycEcoCyc:ATPC-MONOMER; -; .
BioCycMetaCyc:ATPC-MONOMER; -; .
GenevestigatorP0A6E6; -; .
GOGO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell; .
GOGO:0045261; C:proton-transporting ATP synthase complex; catalytic core F(1); IDA:EcoliWiki
GOGO:0046933; F:hydrogen ion transporting ATP synthase activity; rotational mechanism; IEA:InterPro
GOGO:0046961; F:proton-transporting ATPase activity; rotational mechanism; IEA:InterPro
GOGO:0015986; P:ATP synthesis coupled proton transport; IMP:EcoliWiki; .
HAMAPMF_00530; ATP_synth_epsil_bac; 1; -
InterProIPR001469; ATPase_F1-cplx_dsu/esu; .
InterProIPR020547; ATPase_F1-cplx_dsu/esu_C; .
InterProIPR020546; ATPase_F1-cplx_dsu/esu_N; .
Gene3DG3DSA:1.20.5.440; ATPase_F1_d/e; 1; .
Gene3DG3DSA:2.60.15.10; ATPase_F1_d/e; 1; .
PANTHERPTHR13822; ATPase_F1_d/e; 1; .
PfamPF00401; ATP-synt_DE; 1; .
PfamPF02823; ATP-synt_DE_N; 1; .
ProDomPD000944; ATPase_F1-cplx_dsu/esu; 1; .
SUPFAMSSF46604; ATPsynt_DE; 1; .
SUPFAMSSF51344; ATPsynt_DE; 1; .
TIGRFAMsTIGR01216; ATP_synt_epsi; 1; .



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Database constructed and maintained by SIB, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server