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ECOLI:LGT

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) lgt (synonyms: umpA)
Protein Name(s) Prolipoprotein diacylglyceryl transferase
External Links
UniProt P60955
EMBL U12289
U29581
U00096
AP009048
J01710
PIR A56149
RefSeq NP_417305.1
YP_491033.1
ProteinModelPortal P60955
STRING 511145.b2828
EnsemblBacteria AAC75867
BAE76897
GeneID 12934282
947303
KEGG ecj:Y75_p2762
eco:b2828
PATRIC 32121074
EchoBASE EB2049
EcoGene EG12128
eggNOG COG0682
HOGENOM HOG000098666
InParanoid P60955
KO K13292
OMA HWYGLAY
OrthoDB EOG6MH5CQ
PhylomeDB P60955
BioCyc EcoCyc:EG12128-MONOMER
ECOL316407:JW2796-MONOMER
MetaCyc:EG12128-MONOMER
UniPathway UPA00664
PRO PR:P60955
Proteomes UP000000318
UP000000625
Genevestigator P60955
GO GO:0016021
GO:0005887
GO:0008961
GO:0042158
GO:0009249
HAMAP MF_01147
InterPro IPR001640
Pfam PF01790
TIGRFAMs TIGR00544
PROSITE PS01311

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0008961

phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity

PMID:7896715[1]

ECO:0000315

F

These results (Fig. 1 and Table 1) show that E. coli umpA mutants (strains SK634, SK635, and SK636) were defective in diacylglyceryl modification of prolipoprotein because of defective diacylglyceryl transferase. Defective modification of prolipoprotein in umpA mutants was confirmed by in vitro analysis of prolipoprotein modification activity.

complete
CACAO 11172

involved_in

GO:0042158

lipoprotein biosynthetic process

PMID:7896715[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042158

lipoprotein biosynthetic process

PMID:8051048[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0009898

cytoplasmic side of plasma membrane

PMID:18602442[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008961

phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity

PMID:8051048[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008961

phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity

PMID:7896715[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:22287519[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:2644208[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:15919996[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001640

C

Seeded From UniProt

complete

enables

GO:0016757

transferase activity, transferring glycosyl groups

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001640

F

Seeded From UniProt

complete

involved_in

GO:0042158

lipoprotein biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001640

P

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000071004

C

Seeded From UniProt

complete

involved_in

GO:0042158

lipoprotein biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000071004

P

Seeded From UniProt

complete

enables

GO:0008961

phosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000071004

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-KW:KW-0997
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 Gan, K et al. (1995) The umpA gene of Escherichia coli encodes phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling. J. Bacteriol. 177 1879-82 PubMed GONUTS page
  2. 2.0 2.1 Sankaran, K & Wu, HC (1994) Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J. Biol. Chem. 269 19701-6 PubMed GONUTS page
  3. Selvan, AT & Sankaran, K () Localization and characterization of prolipoprotein diacylglyceryl transferase (Lgt) critical in bacterial lipoprotein biosynthesis. Biochimie 90 1647-55 PubMed GONUTS page
  4. Pailler, J et al. (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 2142-51 PubMed GONUTS page
  5. Williams, MG et al. (1989) Identification and genetic mapping of the structural gene for an essential Escherichia coli membrane protein. J. Bacteriol. 171 565-8 PubMed GONUTS page
  6. Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed GONUTS page