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ECOLI:ACP

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) acpP (ECO:0000255 with HAMAP-Rule:MF_01217)
Protein Name(s) Acyl carrier protein (ECO:0000255 with HAMAP-Rule:MF_01217)

ACP (ECO:0000255 with HAMAP-Rule:MF_01217) Cytosolic-activating factor CAF Fatty acid synthase acyl carrier protein

External Links
UniProt P0A6A8
EMBL M84991
S65033
U00096
AP009048
Z34979
PIR C42147
RefSeq NP_415612.1
YP_489362.1
PDB 1ACP
1L0H
1L0I
1T8K
2FAC
2FAD
2FAE
2FHS
2K92
2K93
2K94
3EJB
3EJD
3EJE
PDBsum 1ACP
1L0H
1L0I
1T8K
2FAC
2FAD
2FAE
2FHS
2K92
2K93
2K94
3EJB
3EJD
3EJE
DisProt DP00416
ProteinModelPortal P0A6A8
SMR P0A6A8
DIP DIP-29374N
IntAct P0A6A8
MINT MINT-1231626
STRING 511145.b1094
PaxDb P0A6A8
PRIDE P0A6A8
EnsemblBacteria AAC74178
BAA35902
GeneID 12934366
944805
KEGG ecj:Y75_p1064
eco:b1094
PATRIC 32117429
EchoBASE EB4297
EcoGene EG50003
eggNOG COG0236
HOGENOM HOG000178184
InParanoid P0A6A8
KO K02078
OMA IKPESSF
OrthoDB EOG6MWNJM
PhylomeDB P0A6A8
BioCyc EcoCyc:EG50003-MONOMER
ECOL316407:JW1080-MONOMER
MetaCyc:EG50003-MONOMER
UniPathway UPA00094
EvolutionaryTrace P0A6A8
PRO PR:P0A6A8
Proteomes UP000000318
UP000000625
Genevestigator P0A6A8
GO GO:0005737
GO:0000036
GO:0000035
GO:0031177
GO:0006633
GO:0009245
GO:0008610
GO:0042493
Gene3D 1.10.1200.10
HAMAP MF_01217
InterPro IPR003231
IPR009081
IPR006162
Pfam PF00550
ProDom PD000887
SUPFAM SSF47336
TIGRFAMs TIGR00517
PROSITE PS50075
PS00012

Annotations

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

enables

GO:0008289

lipid binding

PMID:12057197[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000035

acyl binding

PMID:12057197[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0009245

lipid A biosynthetic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG50003
PANTHER:PTN000466714

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG50003
PANTHER:PTN000466714
UniProtKB:P9WQF3

C

Seeded From UniProt

complete

enables

GO:0000036

acyl carrier activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG50003
PANTHER:PTN000466551
UniProtKB:P11943
UniProtKB:P9WQF3

F

Seeded From UniProt

complete

enables

GO:0000035

acyl binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG50003
PANTHER:PTN000466551
UniProtKB:P9WQF3

F

Seeded From UniProt

complete

involved_in

GO:0042493

response to drug

PMID:15459190[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0031177

phosphopantetheine binding

PMID:16352845[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009245

lipid A biosynthetic process

PMID:16352845[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008610

lipid biosynthetic process

PMID:16352845[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006633

fatty acid biosynthetic process

PMID:16352845[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:15459190[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0000036

acyl carrier activity

PMID:15459190[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000035

acyl binding

PMID:15459190[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006633

fatty acid biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003231

P

Seeded From UniProt

complete

involved_in

GO:0006633

fatty acid biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101233

P

Seeded From UniProt

complete

enables

GO:0000036

acyl carrier activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101233

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101233

C

Seeded From UniProt

complete

involved_in

GO:0006633

fatty acid biosynthetic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0275
UniPathway:UPA00094

P

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:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0006631

fatty acid metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0276

P

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ 1.0 1.1 Roujeinikova, A et al. (2002) X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site. Structure 10 825-35 PubMed GONUTS page
  2. ↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 4.3 Zhang, YM et al. (2004) Acyl carrier protein is a cellular target for the antibacterial action of the pantothenamide class of pantothenate antimetabolites. J. Biol. Chem. 279 50969-75 PubMed GONUTS page
  5. ↑ 5.0 5.1 5.2 5.3 De Lay, NR & Cronan, JE (2006) Gene-specific random mutagenesis of Escherichia coli in vivo: isolation of temperature-sensitive mutations in the acyl carrier protein of fatty acid synthesis. J. Bacteriol. 188 287-96 PubMed GONUTS page
  6. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
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