Reviewed, UniProtKB/Swiss-Prot P0A6A8 (ACP_ECOLI)

Names and origin

Protein names

Recommended name:
    Acyl carrier protein
      Short name=ACP
Alternative name(s):
    Cytosolic-activating factor
      Short name=CAF
    Fatty acid synthase acyl carrier protein

Gene names

Name:	acpP
Ordered Locus Names:	b1094, JW1080

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	78 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Carrier of the growing fatty acid chain in fatty acid biosynthesis. HAMAP MF_01217
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01217
Subcellular location	Cytoplasm. HAMAP MF_01217
Post-translational modification	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. HAMAP MF_01217
Sequence similarities	Contains 1 acyl carrier domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Ligand	Phosphopantetheine
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	acyl carrier activity Inferred from electronic annotation. Source: HAMAP cofactor binding Inferred from electronic annotation. Source: InterPro phosphopantetheine binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6 Ref.7 Ref.8

Chain

2 – 78

77

Acyl carrier protein HAMAP MF_01217

PRO_0000180134

Amino acid modifications

Modified residue

37

1

O-(pantetheine 4'-phosphoryl)serine HAMAP MF_01217

Experimental info

Mutagenesis

37

1

S → A or T: Loss of phosphopantetheinylation, and inhibition of cell growth. Ref.11

Sequence conflict

25

1

N → D AA sequence Ref.6

Sequence conflict

44

1

V → I AA sequence Ref.7

Sequence conflict

71

1

D → V in AAB27925. Ref.2

Sequence conflict

76

1

H → N in AAB27925. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

78

Helix Strand Turn

Details...

Helix

4 – 16

13

Helix

20 – 22

3

Turn

29 – 32

4

Helix

37 – 51

15

Helix

57 – 60

4

Helix

66 – 75

10

Sequences

	Sequence		Length	Mass (Da)
	P0A6A8-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 41FCFC39D45BFEA1	FASTA	78	8,640
	10 20 30 40 50 60 MSTIEERVKK IIGEQLGVKQ EEVTNNASFV EDLGADSLDT VELVMALEEE FDTEIPDEEA 70 EKITTVQAAI DYINGHQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1556094] [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: 8359454] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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." 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., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 4882207] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-78. 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: 3549687] [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: 2062368] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21.
[9]	"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: 7972002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-78. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]	"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: 4882206] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Strain: K12 / E15.
[11]	"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: 7673201] [Abstract] Cited for: MUTAGENESIS OF SER-37.
[12]	"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: 3402450] [Abstract] Cited for: STRUCTURE BY NMR.
[13]	"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: 3056520] [Abstract] Cited for: STRUCTURE BY NMR.
[14]	"Refinement of the NMR structures for acyl carrier protein with scalar coupling data." Kim Y., Prestegard J.H. Proteins 8:377-385(1990) [PubMed: 2091027] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

PIR

AYEC. C42147.

RefSeq

AP_001720.1.
NP_415612.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ACP	NMR	-	A	2-78	[»]
1L0H	X-ray	2.00	A	2-76	[»]
1L0I	X-ray	1.20	A	1-78	[»]
1T8K	X-ray	1.10	A	2-77	[»]
2FAC	X-ray	1.76	A/B	2-77	[»]
2FAD	X-ray	1.60	A/B	2-77	[»]
2FAE	X-ray	1.55	A/B	2-77	[»]
2FHS	X-ray	2.70	C	1-78	[»]
2K92	NMR	-	A	2-78	[»]
2K93	NMR	-	A	2-78	[»]
2K94	NMR	-	A	2-78	[»]
3EJB	X-ray	2.00	A/C/E/G	1-78	[»]
3EJD	X-ray	2.10	A/C/E/G	1-78	[»]
3EJE	X-ray	2.10	A/C/E/G	1-78	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6A8. 40 interactions.

STRING

P0A6A8.

Proteomic databases

PRIDE

P0A6A8.

Genome annotation databases

GeneID

944805.

GenomeReviews

Gene locus JW1080 in contig AP009048_GR.
Gene locus b1094 in contig U00096_GR.

KEGG

ecj:JW1080.
eco:b1094.

Organism-specific databases

EchoBASE

EB4297.

EcoGene

EG50003. acpP.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A6A8.

OMA

IDYITEH.

Gene expression databases

Genevestigator

P0A6A8.

Family and domain databases

HAMAP

MF_01217.
[Tree]

InterPro

IPR003231. Acyl_carrier.
IPR009081. Acyl_carrier_prot-like.
IPR006163. Phsphopanteth_bd.
IPR006162. PPantetheine_attach_site.
[Graphical view]

Pfam

PF00550. PP-binding. 1 hit.
[Graphical view]

ProDom

PD000887. Acyl_carrier. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00517. acyl_carrier. 1 hit.

PROSITE

PS50075. ACP_DOMAIN. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ACP_ECOLI

Accession

Primary (citable) accession number: P0A6A8
Secondary accession number(s): P02901, Q53352

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)