Escherichia coli K-12 substr. MG1655 Enzyme: undecaprenyl-phosphate glucose phosphotransferase

Gene: wcaJ Accession Numbers: G7098 (EcoCyc), b2047, ECK2041

Regulation Summary Diagram: ?

Regulation summary diagram for wcaJ

WcaJ belongs to the polyisoprenyl-phosphate hexose-1-phosphate transferase (PHPT) family and catalyzes the transfer of glucose-1-phosphate from UDP-glucose to undecaprenyl-phosphate [Patel12], which is the initial step of colanic acid biosynthesis in E. coli [Johnson77]. WcaJ was predicted to catalyze this reaction based on sequence similarity and its presence in a colanic acid biosynthesis operon [Stevenson96].

Inactivation of wcaJ was used to increase the cellular pool of the colanic acid (CA) synthesis building block GDP-fucose [Dumon01]. A wcaJ mutant produces nonmucoid colonies in an RcsA-overexpressing strain background [Patel12].

Locations: inner membrane

Map Position: [2,118,184 <- 2,119,578] (45.65 centisomes, 164°)
Length: 1395 bp / 464 aa

Molecular Weight of Polypeptide: 52.408 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0006785 , DIP:DIP-11125N , EchoBASE:EB3345 , EcoGene:EG13575 , EcoliWiki:b2047 , OU-Microarray:b2047 , PortEco:wcaJ , Pride:P71241 , Protein Model Portal:P71241 , RefSeq:NP_416551 , RegulonDB:G7098 , String:511145.b2047 , UniProt:P71241

Relationship Links: InterPro:IN-FAMILY:IPR003362 , InterPro:IN-FAMILY:IPR017473 , InterPro:IN-FAMILY:IPR017475 , Pfam:IN-FAMILY:PF02397

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0009242 - colanic acid biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, Patel12]
GO:0000271 - polysaccharide biosynthetic process Inferred by computational analysis [UniProtGOA11a]
GO:0009103 - lipopolysaccharide biosynthetic process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0089702 - undecaprenyl-phosphate glucose phosphotransferase activity Inferred from experiment [Patel12]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016757 - transferase activity, transferring glycosyl groups Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: metabolism biosynthesis of macromolecules (cellular constituents) colanic acid (M antigen)

Essentiality data for wcaJ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Curated 05-Jan-2006 by Shearer A , SRI International
Last-Curated ? 22-Oct-2014 by Keseler I , SRI International

Enzymatic reaction of: undecaprenyl-phosphate glucose phosphotransferase

EC Number:

UDP-α-D-glucose + di-trans,octa-cis-undecaprenyl phosphate <=> UMP + α-D-glucopyranosyl-diphosphoundecaprenol

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.

WcaJ can complement a S. enterica ΔwbaP mutant in vivo; thus, the enzyme may have a low level of galactose-1-P transferase activity that was not detectable by the in vitro assay [Patel12].

Sequence Features

Protein sequence of undecaprenyl-phosphate glucose phosphotransferase with features indicated

Feature Class Location Citations Comment
Transmembrane-Region 16 -> 36
UniProt: Helical; Non-Experimental Qualifier: potential.
Transmembrane-Region 39 -> 59
UniProt: Helical; Non-Experimental Qualifier: potential.
Transmembrane-Region 81 -> 101
UniProt: Helical; Non-Experimental Qualifier: potential.
Transmembrane-Region 105 -> 125
UniProt: Helical; Non-Experimental Qualifier: potential.
Sequence-Conflict 202 -> 203
[Stevenson96, UniProt10]
UniProt: (in Ref. 1; AAC77848);
Transmembrane-Region 279 -> 299
UniProt: Helical; Non-Experimental Qualifier: potential.
Sequence-Conflict 297
[Stevenson96, UniProt10]
UniProt: (in Ref. 1; AAC77848);
Sequence-Conflict 312
[Stevenson96, UniProt10]
UniProt: (in Ref. 1; AAC77848);
Sequence-Conflict 399 -> 400
[Stevenson96, UniProt10]
UniProt: (in Ref. 1; AAC77848);

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Dumon01: Dumon C, Priem B, Martin SL, Heyraud A, Bosso C, Samain E (2001). "In vivo fucosylation of lacto-N-neotetraose and lacto-N-neohexaose by heterologous expression of Helicobacter pylori alpha-1,3 fucosyltransferase in engineered Escherichia coli." Glycoconj J 18(6);465-74. PMID: 12084982

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Johnson77: Johnson JG, Wilson DB (1977). "Role of a sugar-lipid intermediate in colanic acid synthesis by Escherichia coli." J Bacteriol 129(1);225-36. PMID: 318640

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Patel12: Patel KB, Toh E, Fernandez XB, Hanuszkiewicz A, Hardy GG, Brun YV, Bernards MA, Valvano MA (2012). "Functional characterization of UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferases of Escherichia coli and Caulobacter crescentus." J Bacteriol 194(10);2646-57. PMID: 22408159

Stevenson96: Stevenson G, Andrianopoulos K, Hobbs M, Reeves PR (1996). "Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid." J Bacteriol 1996;178(16);4885-93. PMID: 8759852

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Tue Oct 13, 2015, biocyc13.