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Escherichia coli K-12 substr. MG1655 Enzyme: phosphoglycerol transferase I



Gene: opgB Accession Numbers: EG12591 (EcoCyc), b4359, ECK4349

Synonyms: yjjO, mdoB

Regulation Summary Diagram: ?

Alternative forms of phosphoglycerol transferase I: phosphoglycerol transferase II (summary available)

Summary:
E. coli opgB encodes two phosphoglycerol transferases. Phosphoglycerol transferase I is a membrane bound enzyme which catalyzes the transfer of phosphoglycerol residues from phosphatidylglycerol to membrane derived oligosaccharides (MDOs), now known as osmoregulated periplasmic glucans (OPGs). Phosphoglycerol transferase II is a soluble periplasmic enzyme which catalyzes the transfer of phosphoglycerol residues between species of MDO leading to the formation of multiply substituted oligosaccharides. In addition, at low concentrations of acceptor, phosphoglycerol transferase II can act as a cyclase liberating free cyclic phosphoglycerol [Jackson83, Goldberg81, Bohin84].

Locations: inner membrane

Map Position: [4,595,173 <- 4,597,464] (99.04 centisomes)
Length: 2292 bp / 763 aa

Molecular Weight of Polypeptide: 85.494 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0014297 , CGSC:18169 , DIP:DIP-10175N , EchoBASE:EB2476 , EcoGene:EG12591 , EcoliWiki:b4359 , Mint:MINT-1305397 , ModBase:P39401 , OU-Microarray:b4359 , PortEco:mdoB , PR:PRO_000023177 , Pride:P39401 , Protein Model Portal:P39401 , RefSeq:NP_418779 , RegulonDB:EG12591 , SMR:P39401 , String:511145.b4359 , UniProt:P39401

Relationship Links: InterPro:IN-FAMILY:IPR000917 , InterPro:IN-FAMILY:IPR017849 , InterPro:IN-FAMILY:IPR017850 , InterPro:IN-FAMILY:IPR020881 , Pfam:IN-FAMILY:PF00884

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0009250 - glucan biosynthetic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0008960 - phosphatidylglycerol-membrane-oligosaccharide glycerophosphotransferase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Jackson83]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0008484 - sulfuric ester hydrolase activity Inferred by computational analysis [GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA01a, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, Jackson83]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell processes adaptations osmotic pressure
cell structure membrane
metabolism biosynthesis of macromolecules (cellular constituents) osmoregulated periplasmic glucan
metabolism biosynthesis of macromolecules (cellular constituents) phospholipid

Essentiality data for opgB knockouts: ?

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

Enzymatic reaction of: phosphoglycerol transferase

Synonyms: phosphatidylglycerol-membrane-oligosaccharide glycerophosphotransferase, phosphatidylglycerol:membrane-derived-oligosaccharide-D-glucose glycerophosphotransferase

EC Number: 2.7.8.20

an osmoregulated periplasmic glucan[periplasmic space] + an L-1-phosphatidyl-glycerol[periplasmic space] <=> a 1,2-diacyl-sn-glycerol[periplasmic space] + an OPG-6-(glycerophospho)-D-glucose[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Alternative Substrates [Comment 3]:

Cofactors or Prosthetic Groups: Mn2+ [Comment 4]

pH(opt): 8.9 [BRENDA14, Jackson83]


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 1 -> 21
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 26 -> 46
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 77 -> 97
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 108 -> 128
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Amanda Mackie on Thu Dec 19, 2013:
20/12/2013 - membrane derived oligosaccharides (MDOs) are now called osmoregulateed periplasmic glucans (OPGs) and gene names have been changed accordingly
Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
10/20/97 Gene b4359 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12591; confirmed by SwissProt match.


References

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

Bohin84: Bohin JP, Kennedy EP (1984). "Regulation of the synthesis of membrane-derived oligosaccharides in Escherichia coli. Assay of phosphoglycerol transferase I in vivo." J Biol Chem 1984;259(13);8388-93. PMID: 6330111

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

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

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Goldberg81: Goldberg DE, Rumley MK, Kennedy EP (1981). "Biosynthesis of membrane-derived oligosaccharides: a periplasmic phosphoglyceroltransferase." Proc Natl Acad Sci U S A 1981;78(9);5513-7. PMID: 6272307

Jackson83: Jackson BJ, Kennedy EP (1983). "The biosynthesis of membrane-derived oligosaccharides. A membrane-bound phosphoglycerol transferase." J Biol Chem 1983;258(4);2394-8. PMID: 6296144

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

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

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

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


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 18.5 on Wed Nov 26, 2014, biocyc14.