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Sample Preparation and Post-separation Analysis



Searching in 'SWISS-2DPAGE' for entry matching: P37744




SWISS-2DPAGE:  P37744


P37744


General information about the entry
View entry in simple text format
Entry nameRMLA1_ECOLI
Primary accession numberP37744
integrated into SWISS-2DPAGE on May 15, 2003 (release 16)
2D Annotations were last modified onDecember 30, 2004 (version 1)
General Annotations were last modified on May 19, 2011 (version 7)
Name and origin of the protein
DescriptionRecName: Full=Glucose-1-phosphate thymidylyltransferase 1; Short=G1P-TT 1; EC=2.7.7.24; AltName: Full=dTDP-glucose pyrophosphorylase 1; AltName: Full=dTDP-glucose synthase 1;.
Gene nameName=rmlA1
Synonyms=rfbA, rmlA
OrderedLocusNames=b2039, JW2024
Annotated speciesEscherichia coli [TaxID: 562]
TaxonomyBacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
References
[1]   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)
2D PAGE maps for identified proteins
How to interpret a protein

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=5.41; Mw=32544  [identification data]

EXPRESSION:
decrease after benzoic acid treatment [1].

MAPPING (identification):
Tandem mass spectrometry [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 license@isb-sib.ch).
Cross-references
UniProtKB/Swiss-ProtP37744; RMLA1_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 nameRMLA1_ECOLI
Primary accession numberP37744
Secondary accession number(s) P78081
Sequence was last modified on November 1, 1997 (version 2)
Annotations were last modified on October 19, 2011 (version 98)
Name and origin of the protein
DescriptionRecName: Full=Glucose-1-phosphate thymidylyltransferase 1; Short=G1P-TT 1; EC=2.7.7.24; AltName: Full=dTDP-glucose pyrophosphorylase 1; AltName: Full=dTDP-glucose synthase 1;
Gene nameName=rmlA1
Synonyms=rfbA, rmlA
OrderedLocusNames=b2039, JW2024
Encoded onName=rmlA1; Synonyms=rfbA, rmlA; OrderedLocusNames=b2039, JW2024
Keywords3D-structure; Complete proteome; Lipopolysaccharide biosynthesis; Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome; Transferase.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLU09876; AAB88400.1; -; Genomic_DNA
EMBLU00096; AAC75100.1; -; Genomic_DNA
EMBLAP009048; BAA15881.1; -; Genomic_DNA
EMBLU03041; AAC31629.1; -; Genomic_DNA
PIRF64969; F64969; .
RefSeqNP_416543.1; NC_000913.2; .
PDB1H5R; X-ray; 1.90 A; A/B/C/D=1-293
PDB1H5S; X-ray; 2.30 A; A/B/C/D=1-293
PDB1H5T; X-ray; 1.90 A; A/B/C/D=1-293
PDBsum1H5R; -; .
PDBsum1H5S; -; .
PDBsum1H5T; -; .
ProteinModelPortalP37744; -; .
SMRP37744; 2-291; .
IntActP37744; 9; .
SWISS-2DPAGEP37744; -; .
EnsemblBacteriaEBESCT00000001700; EBESCP00000001700; EBESCG00000001402; .
EnsemblBacteriaEBESCT00000018315; EBESCP00000017606; EBESCG00000017369; .
GeneID945154; -; .
GenomeReviewsAP009048_GR; JW2024; .
GenomeReviewsU00096_GR; b2039; .
KEGGecj:JW2024; -; .
KEGGeco:b2039; -; .
EchoBASEEB1921; -; .
EcoGeneEG11978; rmlA1; .
eggNOGCOG1209; -; .
GeneTreeEBGT00050000009640; -; .
HOGENOMHBG688195; -; .
OMAYRAGWID; -; .
ProtClustDBPRK15480; -; .
BioCycEcoCyc:DTDPGLUCOSEPP-MONOMER; -; .
BioCycMetaCyc:DTDPGLUCOSEPP-MONOMER; -; .
GenevestigatorP37744; -; .
GOGO:0005829; C:cytosol; IDA:UniProtKB; .
GOGO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:EC; .
GOGO:0046872; F:metal ion binding; IEA:UniProtKB-KW; .
GOGO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro; .
GOGO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW; .
InterProIPR005907; G1P_thy_trans_s; .
InterProIPR005835; NTP_transferase; .
PANTHERPTHR22572:SF13; PTHR22572:SF13; 1; .
PfamPF00483; NTP_transferase; 1; .
TIGRFAMsTIGR01207; RmlA; 1; .



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