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ECOLI:CLS

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) cls (synonyms: nov, yciJ)
Protein Name(s) Cardiolipin synthase

CL synthase

External Links
UniProt P0A6H8
EMBL L12044
U01911
D38779
U15986
U24206
U24195
U24196
U24197
U24198
U24199
U24200
U24201
U24202
U24203
U24204
U24205
U00096
AP009048
PIR A56145
RefSeq NP_415765.1
YP_489517.1
ProteinModelPortal P0A6H8
SMR P0A6H8
STRING 511145.b1249
PaxDb P0A6H8
PRIDE P0A6H8
EnsemblBacteria AAC74331
BAA14781
GeneID 12931118
945821
KEGG ecj:Y75_p1223
eco:b1249
PATRIC 32117758
EchoBASE EB1565
EcoGene EG11608
eggNOG COG1502
HOGENOM HOG000077403
KO K06131
OMA EDMIHQA
OrthoDB EOG6Q2ST0
PhylomeDB P0A6H8
BioCyc EcoCyc:CARDIOLIPSYN-MONOMER
ECOL316407:JW1241-MONOMER
MetaCyc:CARDIOLIPSYN-MONOMER
PRO PR:P0A6H8
Genevestigator P0A6H8
GO GO:0016021
GO:0016020
GO:0005886
GO:0008808
GO:0032049
HAMAP MF_00190
InterPro IPR022924
IPR027379
IPR001736
Pfam PF00614
PF13396
SMART SM00155
TIGRFAMs TIGR04265
PROSITE PS50035

Annotations

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

involved_in

GO:0032049

cardiolipin biosynthetic process

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11608
EcoGene:EG13671
EcoGene:EG13875
PANTHER:PTN000478645

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11608
EcoGene:EG13671
PANTHER:PTN000478645

C

Seeded From UniProt

complete

enables

GO:0008808

cardiolipin synthase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11608
EcoGene:EG13671
PANTHER:PTN000478645

F

Seeded From UniProt

complete

enables

GO:0008808

cardiolipin synthase activity

PMID:353047[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0032049

cardiolipin biosynthetic process

PMID:353047[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0032049

cardiolipin biosynthetic process

PMID:2982784[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:353047[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008808

cardiolipin synthase activity

PMID:7918616[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008808

cardiolipin synthase activity

PMID:1663113[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001736

F

Seeded From UniProt

complete

enables

GO:0008808

cardiolipin synthase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR022924
InterPro:IPR030840

F

Seeded From UniProt

complete

enables

GO:0016780

phosphotransferase activity, for other substituted phosphate groups

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR022924
InterPro:IPR030840

F

Seeded From UniProt

complete

involved_in

GO:0032049

cardiolipin biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR022924
InterPro:IPR030840

P

Seeded From UniProt

complete

involved_in

GO:0008654

phospholipid biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079267

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079267

C

Seeded From UniProt

complete

enables

GO:0016780

phosphotransferase activity, for other substituted phosphate groups

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000079267

F

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

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: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

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

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 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. 2.0 2.1 2.2 Pluschke, G et al. (1978) Function of phospholipids in Escherichia coli. Characterization of a mutant deficient in cardiolipin synthesis. J. Biol. Chem. 253 5048-55 PubMed GONUTS page
  3. Shibuya, I et al. (1985) Alteration of phospholipid composition by combined defects in phosphatidylserine and cardiolipin synthases and physiological consequences in Escherichia coli. J. Bacteriol. 161 1086-92 PubMed GONUTS page
  4. Ragolia, L & Tropp, BE (1994) The effects of phosphoglycerides on Escherichia coli cardiolipin synthase. Biochim. Biophys. Acta 1214 323-32 PubMed GONUTS page
  5. Hiraoka, S et al. (1991) Amplification and substantial purification of cardiolipin synthase of Escherichia coli. J. Biochem. 110 443-9 PubMed GONUTS page