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SWISS-2DPAGE 
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Sample Preparation and Post-separation Analysis



Searching in 'SWISS-2DPAGE' for entry matching: P00811




SWISS-2DPAGE:  P00811


P00811


General information about the entry
View entry in simple text format
Entry nameAMPC_ECOLI
Primary accession numberP00811
integrated into SWISS-2DPAGE on December 1, 2000 (release 13)
2D Annotations were last modified onOctober 1, 2001 (version 1)
General Annotations were last modified on May 19, 2011 (version 7)
Name and origin of the protein
DescriptionRecName: Full=Beta-lactamase; EC=3.5.2.6; AltName: Full=Cephalosporinase; Flags: Precursor;.
Gene nameName=ampC
Synonyms=ampA
OrderedLocusNames=b4150, JW4111
Annotated speciesEscherichia coli [TaxID: 562]
TaxonomyBacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
References
[1]   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)
2D PAGE maps for identified proteins
How to interpret a protein

ECOLI6-11 {Escherichia coli(6-11)}
Escherichia coli
ECOLI6-11
  map experimental info
  protein estimated location
 
ECOLI6-11

MAP LOCATIONS:
pI=9.06; Mw=43647  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [1].

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
ECO2DBASEI035.7; 6TH EDITION.
UniProtKB/Swiss-ProtP00811; AMPC_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 nameAMPC_ECOLI
Primary accession numberP00811
Secondary accession number(s) Q2M6F2
Sequence was last modified on July 21, 1986 (version 1)
Annotations were last modified on October 19, 2011 (version 119)
Name and origin of the protein
DescriptionRecName: Full=Beta-lactamase; EC=3.5.2.6; AltName: Full=Cephalosporinase; Flags: Precursor;
Gene nameName=ampC
Synonyms=ampA
OrderedLocusNames=b4150, JW4111
Encoded onName=ampC; Synonyms=ampA; OrderedLocusNames=b4150, JW4111
Keywords3D-structure; Antibiotic resistance; Complete proteome; Direct protein sequencing; Hydrolase; Periplasm; Reference proteome; Signal.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLJ01611; AAA23441.1; -; Genomic_DNA
EMBLU14003; AAA97049.1; -; Genomic_DNA
EMBLU00096; AAC77110.1; -; Genomic_DNA
EMBLAP009048; BAE78154.1; -; Genomic_DNA
EMBLV00277; CAA23537.1; -; Genomic_DNA
PIRA01007; QKEC; .
RefSeqNP_418574.1; NC_000913.2; .
PDB1C3B; X-ray; 2.25 A; A/B=20-377
PDB1FCM; X-ray; 2.46 A; A/B=20-377
PDB1FCN; X-ray; 2.35 A; A/B=20-377
PDB1FCO; X-ray; 2.20 A; A/B=20-377
PDB1FSW; X-ray; 1.90 A; A/B=20-376
PDB1FSY; X-ray; 1.75 A; A/B=20-376
PDB1GA9; X-ray; 2.10 A; A/B=20-377
PDB1I5Q; X-ray; 1.83 A; A/B=20-377
PDB1IEL; X-ray; 2.00 A; A/B=20-377
PDB1IEM; X-ray; 2.30 A; A/B=20-377
PDB1KDS; X-ray; 2.15 A; A/B=20-377
PDB1KDW; X-ray; 2.28 A; A/B=20-377
PDB1KE0; X-ray; 2.30 A; A/B=20-377
PDB1KE3; X-ray; 2.15 A; A/B=20-377
PDB1KE4; X-ray; 1.72 A; A/B=20-377
PDB1KVL; X-ray; 1.53 A; A/B=20-377
PDB1KVM; X-ray; 2.06 A; A/B=20-377
PDB1L0D; X-ray; 1.53 A; A/B=20-377
PDB1L0E; X-ray; 1.90 A; A/B=20-377
PDB1L0F; X-ray; 1.66 A; A/B=20-377
PDB1L0G; X-ray; 1.50 A; A/B=20-377
PDB1L2S; X-ray; 1.94 A; A/B=20-377
PDB1LL5; X-ray; 1.80 A; A/B=20-377
PDB1LL9; X-ray; 1.87 A; A/B=20-377
PDB1LLB; X-ray; 1.72 A; A/B=20-377
PDB1MXO; X-ray; 1.83 A; A/B=20-377
PDB1MY8; X-ray; 1.72 A; A/B=20-377
PDB1O07; X-ray; 1.71 A; A/B=20-377
PDB1PI4; X-ray; 1.39 A; A/B=20-377
PDB1PI5; X-ray; 1.49 A; A/B=20-377
PDB1XGI; X-ray; 1.96 A; A/B=20-377
PDB1XGJ; X-ray; 1.97 A; A/B=20-377
PDB2BLS; X-ray; 2.00 A; A/B=20-377
PDB2FFY; X-ray; 1.07 A; A/B=20-377
PDB2HDQ; X-ray; 2.10 A; A/B=20-377
PDB2HDR; X-ray; 2.20 A; A/B=20-377
PDB2HDS; X-ray; 1.16 A; A/B=20-377
PDB2HDU; X-ray; 1.49 A; A/B=20-377
PDB2I72; X-ray; 2.20 A; A/B=20-377
PDB2P9V; X-ray; 1.80 A; A/B=20-377
PDB2PU2; X-ray; 1.86 A; A/B=20-377
PDB2PU4; X-ray; 2.00 A; A/B=20-377
PDB2R9W; X-ray; 1.80 A; A/B=20-377
PDB2R9X; X-ray; 1.90 A; A/B=20-377
PDB2RCX; X-ray; 2.00 A; A/B=20-377
PDB3BLS; X-ray; 2.30 A; A/B=20-377
PDB3BM6; X-ray; 2.10 A; A/B=20-377
PDB3FKV; X-ray; 1.85 A; A/B=20-377
PDB3FKW; X-ray; 1.50 A; A/B=20-377
PDB3GQZ; X-ray; 1.80 A; A/B=20-377
PDB3GR2; X-ray; 1.80 A; A/B=20-377
PDB3GRJ; X-ray; 2.49 A; A/B=20-377
PDB3GSG; X-ray; 2.10 A; A/B=20-377
PDB3GTC; X-ray; 1.90 A; A/B=20-377
PDB3GV9; X-ray; 1.80 A; A/B=20-377
PDB3GVB; X-ray; 1.80 A; A/B=20-377
PDB3IWI; X-ray; 1.64 A; A/B=20-377
PDB3IWO; X-ray; 1.90 A; A/B=20-377
PDB3IWQ; X-ray; 1.84 A; A/B=20-377
PDB3IXB; X-ray; 1.63 A; A/B=20-377
PDB3IXD; X-ray; 2.64 A; A/B=20-377
PDB3IXG; X-ray; 2.14 A; A/B=20-377
PDB3IXH; X-ray; 2.30 A; A/B=20-377
PDB3O86; X-ray; 1.60 A; A/B=20-377
PDB3O87; X-ray; 1.78 A; A/B=20-377
PDB3O88; X-ray; 1.64 A; A/B=20-377
PDBsum1C3B; -; .
PDBsum1FCM; -; .
PDBsum1FCN; -; .
PDBsum1FCO; -; .
PDBsum1FSW; -; .
PDBsum1FSY; -; .
PDBsum1GA9; -; .
PDBsum1I5Q; -; .
PDBsum1IEL; -; .
PDBsum1IEM; -; .
PDBsum1KDS; -; .
PDBsum1KDW; -; .
PDBsum1KE0; -; .
PDBsum1KE3; -; .
PDBsum1KE4; -; .
PDBsum1KVL; -; .
PDBsum1KVM; -; .
PDBsum1L0D; -; .
PDBsum1L0E; -; .
PDBsum1L0F; -; .
PDBsum1L0G; -; .
PDBsum1L2S; -; .
PDBsum1LL5; -; .
PDBsum1LL9; -; .
PDBsum1LLB; -; .
PDBsum1MXO; -; .
PDBsum1MY8; -; .
PDBsum1O07; -; .
PDBsum1PI4; -; .
PDBsum1PI5; -; .
PDBsum1XGI; -; .
PDBsum1XGJ; -; .
PDBsum2BLS; -; .
PDBsum2FFY; -; .
PDBsum2HDQ; -; .
PDBsum2HDR; -; .
PDBsum2HDS; -; .
PDBsum2HDU; -; .
PDBsum2I72; -; .
PDBsum2P9V; -; .
PDBsum2PU2; -; .
PDBsum2PU4; -; .
PDBsum2R9W; -; .
PDBsum2R9X; -; .
PDBsum2RCX; -; .
PDBsum3BLS; -; .
PDBsum3BM6; -; .
PDBsum3FKV; -; .
PDBsum3FKW; -; .
PDBsum3GQZ; -; .
PDBsum3GR2; -; .
PDBsum3GRJ; -; .
PDBsum3GSG; -; .
PDBsum3GTC; -; .
PDBsum3GV9; -; .
PDBsum3GVB; -; .
PDBsum3IWI; -; .
PDBsum3IWO; -; .
PDBsum3IWQ; -; .
PDBsum3IXB; -; .
PDBsum3IXD; -; .
PDBsum3IXG; -; .
PDBsum3IXH; -; .
PDBsum3O86; -; .
PDBsum3O87; -; .
PDBsum3O88; -; .
ProteinModelPortalP00811; -; .
SMRP00811; 20-377; .
IntActP00811; 1; .
PhosSiteP00811; -; .
SWISS-2DPAGEP00811; -; .
ECO2DBASEI035.7; 6TH EDITION; .
EnsemblBacteriaEBESCT00000000012; EBESCP00000000012; EBESCG00000000012; .
EnsemblBacteriaEBESCT00000015545; EBESCP00000014836; EBESCG00000014605; .
GeneID948669; -; .
GenomeReviewsAP009048_GR; JW4111; .
GenomeReviewsU00096_GR; b4150; .
KEGGecj:JW4111; -; .
KEGGeco:b4150; -; .
EchoBASEEB0038; -; .
EcoGeneEG10040; ampC; .
eggNOGCOG1680; -; .
GeneTreeEBGT00050000010224; -; .
HOGENOMHBG289125; -; .
OMAAACQILN; -; .
ProtClustDBPRK11289; -; .
BioCycEcoCyc:EG10040-MONOMER; -; .
BioCycMetaCyc:EG10040-MONOMER; -; .
DrugBankDB00456; Cefalotin; .
DrugBankDB01147; Cloxacillin; .
GenevestigatorP00811; -; .
GOGO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro; .
GOGO:0008800; F:beta-lactamase activity; IDA:EcoliWiki; .
GOGO:0017001; P:antibiotic catabolic process; IEA:InterPro; .
GOGO:0046677; P:response to antibiotic; IEA:UniProtKB-KW; .
GOGO:0042493; P:response to drug; IDA:EcoliWiki; .
InterProIPR001466; Beta-lactam-related; .
InterProIPR012338; Beta-lactam/transpept-like; .
InterProIPR001586; Beta-lactam_class-C_AS; .
Gene3DG3DSA:3.40.710.10; G3DSA:3.40.710.10; 1; .
PfamPF00144; Beta-lactamase; 1; .
SUPFAMSSF56601; PBP_transp_fold; 1; .
PROSITEPS00336; BETA_LACTAMASE_C; 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