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AGRT5:A9CIM3

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Species (Taxon ID) Agrobacterium tumefaciens (strain C58 / ATCC 33970). (176299)
Gene Name(s) pcs
Protein Name(s) Phosphatidylcholine synthase
External Links
UniProt A9CIM3
EMBL AE007869
RefSeq NP_354778.2
ProteinModelPortal A9CIM3
STRING 176299.Atu1793
EnsemblBacteria AAK87563
GeneID 1133831
KEGG atu:Atu1793
PATRIC 20813363
eggNOG COG1183
HOGENOM HOG000066428
KO K01004
OMA FLHPFRV
OrthoDB EOG6P5ZJN
ProtClustDB CLSK863002
GO GO:0016020
GO:0016780
GO:0008654
InterPro IPR000462
IPR026027
Pfam PF01066
PIRSF PIRSF000851

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0008654

phospholipid biosynthetic process

PMID:2612428[1]

ECO:0000314

P

Figure 2B shows that Phosphatidylcholine synthase uses choline to directly synthesize PC. Figure 2 (A&B) shows that Pcs is active when expressed and is likely responsible for PC synthesis without the requirement of additional proteins.

complete

GO:0072657

protein localization to membrane

PMID:2612428[1]

ECO:0000314

P

Figure 6 shows that A. tumefaciens has significant levels of PC in both the inner and outer membranes, indicating Pcs activity in these locations.

complete

GO:0048870

cell motility

PMID:2612428[1]

ECO:0000315

P

Figure 7 shows that A. tumefaciens is highly motile, and that the motility of the pmtA/pcs double mutant was greatly decreased. This figure also showed that when the pcs mutant was complimented with pcs expressed from a low copy number vector, motility was partially restored.

complete

GO:0042710

biofilm formation

PMID:2612428[1]

ECO:0000315

P

Figure 8 shows that a PC-deficient double mutant (pcs/pmtA) formed thicker and more dense communities in comparison to wild type. It shows that there were numerous large, towering structures present.

complete

enables

GO:0050520

phosphatidylcholine synthase activity

PMID:14663079[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0050520

phosphatidylcholine synthase activity

PMID:18978052[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0008654

phospholipid biosynthetic process

PMID:14663079[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008654

phospholipid biosynthetic process

PMID:18978052[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24931117[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:A9CIM3

F

Seeded From UniProt

complete

enables

GO:0050520

phosphatidylcholine synthase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.8.24

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

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

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

C

Seeded From UniProt

complete

involved_in

GO:0006629

lipid metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0443

P

Seeded From UniProt

complete

involved_in

GO:0008654

phospholipid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0594

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 1.2 1.3 Van Gossum, A et al. (1989) Methods of disinfecting endoscopic material: results of an international survey. Endoscopy 21 247-50 PubMed GONUTS page
  2. 2.0 2.1 Martínez-Morales, F et al. (2003) Pathways for phosphatidylcholine biosynthesis in bacteria. Microbiology (Reading, Engl.) 149 3461-71 PubMed GONUTS page
  3. 3.0 3.1 Klüsener, S et al. (2009) Expression and physiological relevance of Agrobacterium tumefaciens phosphatidylcholine biosynthesis genes. J. Bacteriol. 191 365-74 PubMed GONUTS page
  4. Aktas, M et al. (2014) Enzymatic properties and substrate specificity of a bacterial phosphatidylcholine synthase. FEBS J. 281 3523-41 PubMed GONUTS page