Acyl carrier protein
Details
- Name
- Acyl carrier protein
- Kind
- protein
- Synonyms
- ACP
- CAF
- Cytosolic-activating factor
- Fatty acid synthase acyl carrier protein
- Gene Name
- acpP
- UniProtKB Entry
- P0A6A8Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0012878|Acyl carrier protein MSTIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEA EKITTVQAAIDYINGHQA
- Number of residues
- 78
- Molecular Weight
- 8639.455
- Theoretical pI
- 3.71
- GO Classification
- FunctionsACP phosphopantetheine attachment site binding involved in fatty acid biosynthetic process / acyl binding / lipid binding / phosphopantetheine bindingProcessesfatty acid biosynthetic process / lipid A biosynthetic process / lipid biosynthetic process / response to drugComponentscytoplasm / cytosol
- General Function
- Carrier of the growing fatty acid chain in fatty acid biosynthesis.
- Specific Function
- acyl binding
- Pfam Domain Function
- PP-binding (PF00550)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0012879|Acyl carrier protein (acpP) ATGAGCACTATCGAAGAACGCGTTAAGAAAATTATCGGCGAACAGCTGGGCGTTAAGCAG GAAGAAGTTACCAACAATGCTTCTTTCGTTGAAGACCTGGGCGCGGATTCTCTTGACACC GTTGAGCTGGTAATGGCTCTGGAAGAAGAGTTTGATACTGAGATTCCGGACGAAGAAGCT GAGAAAATCACCACCGTTCAGGCTGCCATTGATTACATCAACGGCCACCAGGCGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A6A8 UniProtKB Entry Name ACP_ECOLI GenBank Protein ID 145880 GenBank Gene ID M84991 PDB ID(s) 1ACP, 1L0H, 1L0I, 1T8K, 2FAC, 2FAD, 2FAE, 2FHS, 2K92, 2K93, 2K94, 3EJB, 3EJD, 3EJE, 3NY7 KEGG ID ecj:JW1080 NCBI Gene ID 32369337 - General References
- Rawlings M, Cronan JE Jr: The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes. J Biol Chem. 1992 Mar 25;267(9):5751-4. [Article]
- Jones AL, Kille P, Dancer JE, Harwood JL: The cloning and overexpression of E. coli acyl carrier protein (ACP). Biochem Soc Trans. 1993 May;21(2):202S. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Vanaman TC, Wakil SJ, Hill RL: The complete amino acid sequence of the acyl carrier protein of Escherichia coli. J Biol Chem. 1968 Dec 25;243(24):6420-31. [Article]
- Jackowski S, Rock CO: Altered molecular form of acyl carrier protein associated with beta-ketoacyl-acyl carrier protein synthase II (fabF) mutants. J Bacteriol. 1987 Apr;169(4):1469-73. [Article]
- Issartel JP, Koronakis V, Hughes C: Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation. Nature. 1991 Jun 27;351(6329):759-61. [Article]
- Li Y, Stewart NK, Berger AJ, Vos S, Schoeffler AJ, Berger JM, Chait BT, Oakley MG: Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction. Proc Natl Acad Sci U S A. 2010 Nov 2;107(44):18832-7. doi: 10.1073/pnas.1008678107. Epub 2010 Oct 4. [Article]
- Siggaard-Andersen M, Wissenbach M, Chuck JA, Svendsen I, Olsen JG, von Wettstein-Knowles P: The fabJ-encoded beta-ketoacyl-[acyl carrier protein] synthase IV from Escherichia coli is sensitive to cerulenin and specific for short-chain substrates. Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):11027-31. [Article]
- Vanaman TC, Wakil SJ, Hill RL: The preparation of tryptic, peptic, thermolysin, and cyanogen bromide peptides from the acyl carrier protein of Escherichia coli. J Biol Chem. 1968 Dec 25;243(24):6409-19. [Article]
- Keating DH, Carey MR, Cronan JE Jr: The unmodified (apo) form of Escherichia coli acyl carrier protein is a potent inhibitor of cell growth. J Biol Chem. 1995 Sep 22;270(38):22229-35. [Article]
- Holak TA, Nilges M, Prestegard JH, Gronenborn AM, Clore GM: 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. Eur J Biochem. 1988 Jul 15;175(1):9-15. [Article]
- Holak TA, Kearsley SK, Kim Y, Prestegard JH: Three-dimensional structure of acyl carrier protein determined by NMR pseudoenergy and distance geometry calculations. Biochemistry. 1988 Aug 9;27(16):6135-42. [Article]
- Kim Y, Prestegard JH: Refinement of the NMR structures for acyl carrier protein with scalar coupling data. Proteins. 1990;8(4):377-85. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Heptyl 1-Thiohexopyranoside experimental unknown target Details S-(2-{[N-(2-HYDROXY-4-{[HYDROXY(OXIDO)PHOSPHINO]OXY}-3,3-DIMETHYLBUTANOYL)-BETA-ALANYL]AMINO}ETHYL) HEXANETHIOATE experimental unknown target Details S-(2-{[N-(2-HYDROXY-4-{[HYDROXY(OXIDO)PHOSPHINO]OXY}-3,3-DIMETHYLBUTANOYL)-BETA-ALANYL]AMINO}ETHYL) HEPTANETHIOATE experimental unknown target Details