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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Enzyme: phosphatidylglycerol-prolipoprotein diacylglyceryl transferase

Gene: lgt Accession Numbers: EG12128 (MetaCyc), b2828, ECK2824

Synonyms: umpA

Species: Escherichia coli K-12 substr. MG1655

Summary:
Lgt catalyses the transfer of an sn-1,2-diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a proliporotein [Sankaran94]. It is the first of 3 sequential reactions that result in the formation of mature triacylated lipoprotein.

Lgt is an essential inner membrane protein [Williams89, Pailler12]. Lgt contains 7 transmembrane segments; the N-terminus faces the periplasm and the C-terminus faces the cytoplasm [Pailler12]. Lgt is a peripheral membrane protein on the cytoplasmic side of the inner membrane [Sankaran94].

Sequence analysis, chemical inactivation, mutation, and complementation studies indicate that His-103 is essential for the activity of the enzyme; Tyr-235 and His-196 also have significant roles in its function [Qi95a, Sankaran97].

Locations: inner membrane

Map Position: [2,963,184 <- 2,964,059]

Molecular Weight of Polypeptide: 33.108 kD (from nucleotide sequence), 25 kD (experimental) [Williams89 ]

Unification Links: ASAP:ABE-0009270 , CGSC:33350 , EchoBASE:EB2049 , EcoGene:EG12128 , EcoliWiki:b2828 , OU-Microarray:b2828 , PortEco:lgt , PR:PRO_000023088 , Protein Model Portal:P60955 , RefSeq:NP_417305 , RegulonDB:EG12128 , String:511145.b2828 , UniProt:P60955

Relationship Links: InterPro:IN-FAMILY:IPR001640 , Pfam:IN-FAMILY:PF01790 , Prosite:IN-FAMILY:PS01311

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0042158 - lipoprotein biosynthetic process Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, Sankaran94]
GO:0009249 - protein lipoylation Inferred by computational analysis [GOA01a]
Molecular Function: GO:0008961 - phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity Inferred from experiment Inferred by computational analysis [GOA06, Sankaran94]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016757 - transferase activity, transferring glycosyl groups Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, DiazMejia09, Daley05]
GO:0005887 - integral component of plasma membrane Inferred from experiment [Pailler12]
GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Williams89]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: cell structure membrane
information transfer protein related posttranslational modification
metabolism biosynthesis of macromolecules (cellular constituents) phospholipid

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: phosphatidylglycerol-prolipoprotein diacylglyceryl transferase

Synonyms: prolipoprotein diacylglyceryl transferase

a prolipoprotein + an L-1-phosphatidyl-glycerol <=> a diacylglycerol prolipoprotein + sn-glycerol 1-phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Reversibility of this reaction is unspecified.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Sequence Features

Feature Class Location Citations Comment
Mutagenesis-Variant 7
[Sankaran97, UniProt11a]
Alternate sequence: Q; UniProt: No effect.
Transmembrane-Region 21 -> 41
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 24
[Sankaran97, UniProt11a]
Alternate sequence: Q; UniProt: No effect.
Extrinsic-Sequence-Variant 25
[UniProt10a]
Alternate sequence: R; UniProt: (in SK636, temperature-sensitive);
Mutagenesis-Variant 26
[Sankaran97, UniProt11a]
Alternate sequence: F; UniProt: No effect.
Transmembrane-Region 60 -> 80
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 62
[Sankaran97, UniProt11a]
Alternate sequence: F; UniProt: No effect.
Mutagenesis-Variant 76
[Sankaran97, UniProt11a]
Alternate sequence: F; UniProt: No effect.
Transmembrane-Region 96 -> 116
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 103
[Sankaran97, UniProt11a]
Alternate sequence: N; UniProt: Loss of activity.
Alternate sequence: Q; UniProt: Loss of activity.
Extrinsic-Sequence-Variant 104
[UniProt10a]
Alternate sequence: S; UniProt: (in SK634, temperature-sensitive);
Extrinsic-Sequence-Variant 139
[UniProt10a]
Alternate sequence: F; UniProt: (in SK635, temperature-sensitive);
Mutagenesis-Variant 190
[Sankaran97, UniProt11a]
Alternate sequence: F; UniProt: No effect.
Mutagenesis-Variant 196
[Sankaran97, UniProt11a]
Alternate sequence: R; UniProt: 50% decrease in activity.
Alternate sequence: Q; UniProt: 50% decrease in activity.
Alternate sequence: L; UniProt: No effect.
Alternate sequence: N; UniProt: No effect.
Mutagenesis-Variant 201
[Sankaran97, UniProt11a]
Alternate sequence: F; UniProt: No effect.
Transmembrane-Region 225 -> 245
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 235
[Sankaran97, UniProt11a]
Alternate sequence: S; UniProt: 37% decrease in activity.
Alternate sequence: T; UniProt: Loss of activity.
Alternate sequence: F; UniProt: Loss of activity.
Transmembrane-Region 260 -> 280
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 282
[Sankaran97, UniProt11a]
Alternate sequence: F; UniProt: No effect.
Mutagenesis-Variant 289
[Sankaran97, UniProt11a]
Alternate sequence: Q; UniProt: No effect.

History:
10/20/97 Gene b2828 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12128; confirmed by SwissProt match.


References

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

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

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Pailler12: Pailler J, Aucher W, Pires M, Buddelmeijer N (2012). "Phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments, and its essential residues are embedded in the membrane." J Bacteriol 194(9);2142-51. PMID: 22287519

Qi95a: Qi HY, Sankaran K, Gan K, Wu HC (1995). "Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase: functionally significant conserved regions." J Bacteriol 177(23);6820-4. PMID: 7592473

Sankaran94: Sankaran K, Wu HC (1994). "Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol." J Biol Chem 269(31);19701-6. PMID: 8051048

Sankaran97: Sankaran K, Gan K, Rash B, Qi HY, Wu HC, Rick PD (1997). "Roles of histidine-103 and tyrosine-235 in the function of the prolipoprotein diacylglyceryl transferase of Escherichia coli." J Bacteriol 179(9);2944-8. PMID: 9139912

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

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 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."

Williams89: Williams MG, Fortson M, Dykstra CC, Jensen P, Kushner SR (1989). "Identification and genetic mapping of the structural gene for an essential Escherichia coli membrane protein." J Bacteriol 171(1);565-8. PMID: 2644208


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, BIOCYC14B.