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Protein

Acyl carrier protein

Gene

acpP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Carrier of the growing fatty acid chain in fatty acid biosynthesis.

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

  • ACP phosphopantetheine attachment site binding involved in fatty acid biosynthetic process Source: EcoliWiki
  • acyl binding Source: EcoliWiki
  • phosphopantetheine binding Source: EcoliWiki

GO - Biological processi

  • fatty acid biosynthetic process Source: EcoliWiki
  • lipid A biosynthetic process Source: EcoliWiki
  • lipid biosynthetic process Source: EcoliWiki
  • response to drug Source: EcoliWiki
Complete GO annotation...

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:EG50003-MONOMER.
ECOL316407:JW1080-MONOMER.
MetaCyc:EG50003-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl carrier proteinUniRule annotation
Short name:
ACPUniRule annotation
Alternative name(s):
Cytosolic-activating factor
Short name:
CAF
Fatty acid synthase acyl carrier protein
Gene namesi
Name:acpPUniRule annotation
Ordered Locus Names:b1094, JW1080
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG50003. acpP.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi37 – 371S → A or T: Loss of phosphopantetheinylation, and inhibition of cell growth. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 7877Acyl carrier proteinPRO_0000180134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371O-(pantetheine 4'-phosphoryl)serineUniRule annotation1 Publication

Post-translational modificationi

4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

EPDiP0A6A8.
PaxDbiP0A6A8.
PRIDEiP0A6A8.

Interactioni

Subunit structurei

Interacts with MukB.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
espPO325912EBI-542566,EBI-852989From a different organism.
plsBP0A7A73EBI-542566,EBI-542961
spoTP0AG245EBI-542566,EBI-543228
ybgCP0A8Z36EBI-542566,EBI-543276

Protein-protein interaction databases

BioGridi4263360. 478 interactions.
DIPiDIP-29374N.
IntActiP0A6A8. 41 interactions.
MINTiMINT-1231626.
STRINGi511145.b1094.

Structurei

Secondary structure

1
78
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1613Combined sources
Helixi20 – 223Combined sources
Turni29 – 335Combined sources
Helixi37 – 5115Combined sources
Helixi57 – 604Combined sources
Helixi66 – 7510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACPNMR-A2-78[»]
1L0HX-ray2.00A1-77[»]
1L0IX-ray1.20A1-78[»]
1T8KX-ray1.10A2-78[»]
2FACX-ray1.76A/B2-78[»]
2FADX-ray1.60A/B2-78[»]
2FAEX-ray1.55A/B2-78[»]
2FHSX-ray2.70C1-78[»]
2K92NMR-A2-78[»]
2K93NMR-A2-78[»]
2K94NMR-A2-78[»]
3EJBX-ray2.00A/C/E/G1-78[»]
3EJDX-ray2.10A/C/E/G1-78[»]
3EJEX-ray2.10A/C/E/G1-78[»]
3NY7X-ray1.92B1-78[»]
DisProtiDP00416.
ProteinModelPortaliP0A6A8.
SMRiP0A6A8. Positions 2-78.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6A8.

Family & Domainsi

Sequence similaritiesi

Contains 1 acyl carrier domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0236. LUCA.
HOGENOMiHOG000178184.
InParanoidiP0A6A8.
KOiK02078.
OMAiIKPESSF.
OrthoDBiEOG6MWNJM.
PhylomeDBiP0A6A8.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
HAMAPiMF_01217. Acyl_carrier.
InterProiIPR003231. Acyl_carrier.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00550. PP-binding. 1 hit.
[Graphical view]
ProDomiPD000887. PD000887. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47336. SSF47336. 1 hit.
TIGRFAMsiTIGR00517. acyl_carrier. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6A8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTIEERVKK IIGEQLGVKQ EEVTNNASFV EDLGADSLDT VELVMALEEE
60 70
FDTEIPDEEA EKITTVQAAI DYINGHQA
Length:78
Mass (Da):8,640
Last modified:January 23, 2007 - v2
Checksum:i41FCFC39D45BFEA1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251N → D AA sequence (PubMed:4882207).Curated
Sequence conflicti44 – 441V → I AA sequence (PubMed:3549687).Curated
Sequence conflicti71 – 711D → V in AAB27925 (PubMed:8359454).Curated
Sequence conflicti76 – 761H → N in AAB27925 (PubMed:8359454).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84991 Genomic DNA. Translation: AAA23740.1.
S65033 Genomic DNA. Translation: AAB27925.2.
U00096 Genomic DNA. Translation: AAC74178.1.
AP009048 Genomic DNA. Translation: BAA35902.1.
Z34979 Genomic DNA. No translation available.
PIRiC42147. AYEC.
RefSeqiNP_415612.1. NC_000913.3.
WP_000103754.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74178; AAC74178; b1094.
BAA35902; BAA35902; BAA35902.
GeneIDi5551779.
944805.
KEGGiecj:JW1080.
eco:b1094.
PATRICi32117429. VBIEscCol129921_1137.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84991 Genomic DNA. Translation: AAA23740.1.
S65033 Genomic DNA. Translation: AAB27925.2.
U00096 Genomic DNA. Translation: AAC74178.1.
AP009048 Genomic DNA. Translation: BAA35902.1.
Z34979 Genomic DNA. No translation available.
PIRiC42147. AYEC.
RefSeqiNP_415612.1. NC_000913.3.
WP_000103754.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACPNMR-A2-78[»]
1L0HX-ray2.00A1-77[»]
1L0IX-ray1.20A1-78[»]
1T8KX-ray1.10A2-78[»]
2FACX-ray1.76A/B2-78[»]
2FADX-ray1.60A/B2-78[»]
2FAEX-ray1.55A/B2-78[»]
2FHSX-ray2.70C1-78[»]
2K92NMR-A2-78[»]
2K93NMR-A2-78[»]
2K94NMR-A2-78[»]
3EJBX-ray2.00A/C/E/G1-78[»]
3EJDX-ray2.10A/C/E/G1-78[»]
3EJEX-ray2.10A/C/E/G1-78[»]
3NY7X-ray1.92B1-78[»]
DisProtiDP00416.
ProteinModelPortaliP0A6A8.
SMRiP0A6A8. Positions 2-78.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263360. 478 interactions.
DIPiDIP-29374N.
IntActiP0A6A8. 41 interactions.
MINTiMINT-1231626.
STRINGi511145.b1094.

Proteomic databases

EPDiP0A6A8.
PaxDbiP0A6A8.
PRIDEiP0A6A8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74178; AAC74178; b1094.
BAA35902; BAA35902; BAA35902.
GeneIDi5551779.
944805.
KEGGiecj:JW1080.
eco:b1094.
PATRICi32117429. VBIEscCol129921_1137.

Organism-specific databases

EchoBASEiEB4297.
EcoGeneiEG50003. acpP.

Phylogenomic databases

eggNOGiCOG0236. LUCA.
HOGENOMiHOG000178184.
InParanoidiP0A6A8.
KOiK02078.
OMAiIKPESSF.
OrthoDBiEOG6MWNJM.
PhylomeDBiP0A6A8.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciEcoCyc:EG50003-MONOMER.
ECOL316407:JW1080-MONOMER.
MetaCyc:EG50003-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A6A8.
PROiP0A6A8.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
HAMAPiMF_01217. Acyl_carrier.
InterProiIPR003231. Acyl_carrier.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00550. PP-binding. 1 hit.
[Graphical view]
ProDomiPD000887. PD000887. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47336. SSF47336. 1 hit.
TIGRFAMsiTIGR00517. acyl_carrier. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes."
    Rawlings M., Cronan J.E. Jr.
    J. Biol. Chem. 267:5751-5754(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "The cloning and overexpression of E. coli acyl carrier protein (ACP)."
    Jones A.L., Kille P., Dancer J.E., Harwood J.L.
    Biochem. Soc. Trans. 21:202S-202S(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "The complete amino acid sequence of the acyl carrier protein of Escherichia coli."
    Vanaman T.C., Wakil S.J., Hill R.L.
    J. Biol. Chem. 243:6420-6431(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-78, PHOSPHOPANTETHEINYLATION AT SER-37.
    Strain: K12 / E15.
  7. "Altered molecular form of acyl carrier protein associated with beta-ketoacyl-acyl carrier protein synthase II (fabF) mutants."
    Jackowski S., Rock C.O.
    J. Bacteriol. 169:1469-1473(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-78.
    Strain: K12.
  8. "Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation."
    Issartel J.P., Koronakis V., Hughes C.
    Nature 351:759-761(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21.
  9. "Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction."
    Li Y., Stewart N.K., Berger A.J., Vos S., Schoeffler A.J., Berger J.M., Chait B.T., Oakley M.G.
    Proc. Natl. Acad. Sci. U.S.A. 107:18832-18837(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 10-19 AND 63-78, INTERACTION WITH MUKB.
  10. "The fabJ-encoded beta-ketoacyl-[acyl carrier protein] synthase IV from Escherichia coli is sensitive to cerulenin and specific for short-chain substrates."
    Siggaard-Andersen M., Wissenbach M., Chuck J.-A., Svendsen I., Olsen J.G., von Wettstein-Knowles P.V.
    Proc. Natl. Acad. Sci. U.S.A. 91:11027-11031(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-78.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  11. "The preparation of tryptic, peptic, thermolysin, and cyanogen bromide peptides from the acyl carrier protein of Escherichia coli."
    Vanaman T.C., Wakil S.J., Hill R.L.
    J. Biol. Chem. 243:6409-6419(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Strain: K12 / E15.
  12. "The unmodified (apo) form of Escherichia coli acyl carrier protein is a potent inhibitor of cell growth."
    Keating D.H., Rawlings Carey M., Cronan J.E. Jr.
    J. Biol. Chem. 270:22229-22235(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-37.
  13. "Three-dimensional structure of acyl carrier protein in solution determined by nuclear magnetic resonance and the combined use of dynamical simulated annealing and distance geometry."
    Holak T.A., Nilges M., Prestegard J.H., Gronenborn A.M., Clore G.M.
    Eur. J. Biochem. 175:9-16(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  14. "Three-dimensional structure of acyl carrier protein determined by NMR pseudoenergy and distance geometry calculations."
    Holak T.A., Kearsley S.K., Kim Y., Prestegard J.H.
    Biochemistry 27:6135-6142(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  15. "Refinement of the NMR structures for acyl carrier protein with scalar coupling data."
    Kim Y., Prestegard J.H.
    Proteins 8:377-385(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiACP_ECOLI
AccessioniPrimary (citable) accession number: P0A6A8
Secondary accession number(s): P02901, Q53352
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.