ID ACP_ECOLI Reviewed; 78 AA.
AC P0A6A8; P02901; Q53352;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 158.
DE RecName: Full=Acyl carrier protein {ECO:0000255|HAMAP-Rule:MF_01217};
DE Short=ACP {ECO:0000255|HAMAP-Rule:MF_01217};
DE AltName: Full=Cytosolic-activating factor;
DE Short=CAF;
DE AltName: Full=Fatty acid synthase acyl carrier protein;
GN Name=acpP {ECO:0000255|HAMAP-Rule:MF_01217};
GN OrderedLocusNames=b1094, JW1080;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1556094; DOI=10.1016/s0021-9258(18)42616-6;
RA Rawlings M., Cronan J.E. Jr.;
RT "The gene encoding Escherichia coli acyl carrier protein lies within a
RT cluster of fatty acid biosynthetic genes.";
RL J. Biol. Chem. 267:5751-5754(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8359454; DOI=10.1042/bst021202s;
RA Jones A.L., Kille P., Dancer J.E., Harwood J.L.;
RT "The cloning and overexpression of E. coli acyl carrier protein (ACP).";
RL Biochem. Soc. Trans. 21:202S-202S(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 2-78, AND PHOSPHOPANTETHEINYLATION AT SER-37.
RC STRAIN=K12 / E15;
RX PubMed=4882207; DOI=10.1016/s0021-9258(18)93155-8;
RA Vanaman T.C., Wakil S.J., Hill R.L.;
RT "The complete amino acid sequence of the acyl carrier protein of
RT Escherichia coli.";
RL J. Biol. Chem. 243:6420-6431(1968).
RN [7]
RP PROTEIN SEQUENCE OF 2-78.
RC STRAIN=K12;
RX PubMed=3549687; DOI=10.1128/jb.169.4.1469-1473.1987;
RA Jackowski S., Rock C.O.;
RT "Altered molecular form of acyl carrier protein associated with beta-
RT ketoacyl-acyl carrier protein synthase II (fabF) mutants.";
RL J. Bacteriol. 169:1469-1473(1987).
RN [8]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=2062368; DOI=10.1038/351759a0;
RA Issartel J.P., Koronakis V., Hughes C.;
RT "Activation of Escherichia coli prohaemolysin to the mature toxin by acyl
RT carrier protein-dependent fatty acylation.";
RL Nature 351:759-761(1991).
RN [9]
RP PROTEIN SEQUENCE OF 10-19 AND 63-78, AND INTERACTION WITH MUKB.
RX PubMed=20921377; DOI=10.1073/pnas.1008678107;
RA Li Y., Stewart N.K., Berger A.J., Vos S., Schoeffler A.J., Berger J.M.,
RA Chait B.T., Oakley M.G.;
RT "Escherichia coli condensin MukB stimulates topoisomerase IV activity by a
RT direct physical interaction.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18832-18837(2010).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-78.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7972002; DOI=10.1073/pnas.91.23.11027;
RA Siggaard-Andersen M., Wissenbach M., Chuck J.-A., Svendsen I., Olsen J.G.,
RA von Wettstein-Knowles P.V.;
RT "The fabJ-encoded beta-ketoacyl-[acyl carrier protein] synthase IV from
RT Escherichia coli is sensitive to cerulenin and specific for short-chain
RT substrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11027-11031(1994).
RN [11]
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12 / E15;
RX PubMed=4882206; DOI=10.1016/s0021-9258(18)93154-6;
RA Vanaman T.C., Wakil S.J., Hill R.L.;
RT "The preparation of tryptic, peptic, thermolysin, and cyanogen bromide
RT peptides from the acyl carrier protein of Escherichia coli.";
RL J. Biol. Chem. 243:6409-6419(1968).
RN [12]
RP MUTAGENESIS OF SER-37.
RX PubMed=7673201; DOI=10.1074/jbc.270.38.22229;
RA Keating D.H., Rawlings Carey M., Cronan J.E. Jr.;
RT "The unmodified (apo) form of Escherichia coli acyl carrier protein is a
RT potent inhibitor of cell growth.";
RL J. Biol. Chem. 270:22229-22235(1995).
RN [13]
RP STRUCTURE BY NMR.
RX PubMed=3402450; DOI=10.1111/j.1432-1033.1988.tb14159.x;
RA Holak T.A., Nilges M., Prestegard J.H., Gronenborn A.M., Clore G.M.;
RT "Three-dimensional structure of acyl carrier protein in solution determined
RT by nuclear magnetic resonance and the combined use of dynamical simulated
RT annealing and distance geometry.";
RL Eur. J. Biochem. 175:9-16(1988).
RN [14]
RP STRUCTURE BY NMR.
RX PubMed=3056520; DOI=10.1021/bi00416a046;
RA Holak T.A., Kearsley S.K., Kim Y., Prestegard J.H.;
RT "Three-dimensional structure of acyl carrier protein determined by NMR
RT pseudoenergy and distance geometry calculations.";
RL Biochemistry 27:6135-6142(1988).
RN [15]
RP STRUCTURE BY NMR.
RX PubMed=2091027; DOI=10.1002/prot.340080411;
RA Kim Y., Prestegard J.H.;
RT "Refinement of the NMR structures for acyl carrier protein with scalar
RT coupling data.";
RL Proteins 8:377-385(1990).
CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_01217}.
CC -!- SUBUNIT: Interacts with MukB. {ECO:0000269|PubMed:20921377}.
CC -!- INTERACTION:
CC P0A6A8; P13001: bioH; NbExp=3; IntAct=EBI-542566, EBI-1132260;
CC P0A6A8; P0A7A7: plsB; NbExp=3; IntAct=EBI-542566, EBI-542961;
CC P0A6A8; P0AG24: spoT; NbExp=6; IntAct=EBI-542566, EBI-543228;
CC P0A6A8; P0A8Z3: ybgC; NbExp=7; IntAct=EBI-542566, EBI-543276;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of apo-ACP by AcpS. This modification is essential for activity because
CC fatty acids are bound in thioester linkage to the sulfhydryl of the
CC prosthetic group.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000255|HAMAP-Rule:MF_01217}.
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DR EMBL; M84991; AAA23740.1; -; Genomic_DNA.
DR EMBL; S65033; AAB27925.2; -; Genomic_DNA.
DR EMBL; U00096; AAC74178.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35902.1; -; Genomic_DNA.
DR EMBL; Z34979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C42147; AYEC.
DR RefSeq; NP_415612.1; NC_000913.3.
DR RefSeq; WP_000103754.1; NZ_STEB01000016.1.
DR PDB; 1ACP; NMR; -; A=2-78.
DR PDB; 1L0H; X-ray; 2.00 A; A=1-77.
DR PDB; 1L0I; X-ray; 1.20 A; A=1-78.
DR PDB; 1T8K; X-ray; 1.10 A; A=2-78.
DR PDB; 2FAC; X-ray; 1.76 A; A/B=2-78.
DR PDB; 2FAD; X-ray; 1.60 A; A/B=2-78.
DR PDB; 2FAE; X-ray; 1.55 A; A/B=2-78.
DR PDB; 2FHS; X-ray; 2.70 A; C=1-78.
DR PDB; 2K92; NMR; -; A=2-78.
DR PDB; 2K93; NMR; -; A=2-78.
DR PDB; 2K94; NMR; -; A=2-78.
DR PDB; 3EJB; X-ray; 2.00 A; A/C/E/G=1-78.
DR PDB; 3EJD; X-ray; 2.10 A; A/C/E/G=1-78.
DR PDB; 3EJE; X-ray; 2.10 A; A/C/E/G=1-78.
DR PDB; 3NY7; X-ray; 1.92 A; B=1-78.
DR PDB; 5KOF; X-ray; 2.40 A; C/D=1-78.
DR PDB; 5USR; X-ray; 3.09 A; I/J/K/L=1-78.
DR PDB; 5VCB; X-ray; 4.10 A; D/E/F/J/K/L/P/Q/R/V/W/X/d/e/f=2-78.
DR PDB; 5WGB; X-ray; 2.75 A; C=2-78.
DR PDB; 5WKP; X-ray; 3.15 A; C/G=2-78.
DR PDB; 5WLW; X-ray; 3.32 A; C/G=2-78.
DR PDB; 6DFL; X-ray; 2.40 A; B=3-74.
DR PDB; 6N3P; X-ray; 2.50 A; G/H/I/J/K/L=2-78.
DR PDB; 6OKC; X-ray; 1.55 A; C/D=1-78.
DR PDB; 6OKF; X-ray; 2.50 A; C/D=1-78.
DR PDB; 6OKG; X-ray; 2.30 A; B=1-78.
DR PDB; 6OLT; X-ray; 2.35 A; B=1-78.
DR PDB; 6U0J; X-ray; 1.90 A; B=1-78.
DR PDB; 6UXE; X-ray; 1.57 A; C=2-78.
DR PDB; 6W1D; X-ray; 1.79 A; C=2-78.
DR PDB; 6W98; EM; 2.90 A; B=1-78.
DR PDB; 6WI2; X-ray; 1.95 A; C=2-78.
DR PDB; 6WIH; X-ray; 1.90 A; C=2-78.
DR PDB; 7L4E; X-ray; 2.00 A; B=1-78.
DR PDB; 7L4L; X-ray; 2.65 A; C/D=1-78.
DR PDB; 7NYW; EM; 3.10 A; G/H=1-78.
DR PDB; 7NYX; EM; 4.60 A; G/H=1-78.
DR PDB; 7NYY; EM; 6.80 A; G/H=1-78.
DR PDB; 7NYZ; EM; 6.50 A; G/H=1-78.
DR PDB; 7NZ0; EM; 6.30 A; G/H=1-78.
DR PDB; 7RTK; X-ray; 2.50 A; C=2-78.
DR PDB; 7SQI; X-ray; 1.70 A; C/D=1-78.
DR PDB; 7SZ9; X-ray; 2.20 A; C/D=2-78.
DR PDB; 8DLE; X-ray; 2.30 A; B=1-78.
DR PDBsum; 1ACP; -.
DR PDBsum; 1L0H; -.
DR PDBsum; 1L0I; -.
DR PDBsum; 1T8K; -.
DR PDBsum; 2FAC; -.
DR PDBsum; 2FAD; -.
DR PDBsum; 2FAE; -.
DR PDBsum; 2FHS; -.
DR PDBsum; 2K92; -.
DR PDBsum; 2K93; -.
DR PDBsum; 2K94; -.
DR PDBsum; 3EJB; -.
DR PDBsum; 3EJD; -.
DR PDBsum; 3EJE; -.
DR PDBsum; 3NY7; -.
DR PDBsum; 5KOF; -.
DR PDBsum; 5USR; -.
DR PDBsum; 5VCB; -.
DR PDBsum; 5WGB; -.
DR PDBsum; 5WKP; -.
DR PDBsum; 5WLW; -.
DR PDBsum; 6DFL; -.
DR PDBsum; 6N3P; -.
DR PDBsum; 6OKC; -.
DR PDBsum; 6OKF; -.
DR PDBsum; 6OKG; -.
DR PDBsum; 6OLT; -.
DR PDBsum; 6U0J; -.
DR PDBsum; 6UXE; -.
DR PDBsum; 6W1D; -.
DR PDBsum; 6W98; -.
DR PDBsum; 6WI2; -.
DR PDBsum; 6WIH; -.
DR PDBsum; 7L4E; -.
DR PDBsum; 7L4L; -.
DR PDBsum; 7NYW; -.
DR PDBsum; 7NYX; -.
DR PDBsum; 7NYY; -.
DR PDBsum; 7NYZ; -.
DR PDBsum; 7NZ0; -.
DR PDBsum; 7RTK; -.
DR PDBsum; 7SQI; -.
DR PDBsum; 7SZ9; -.
DR PDBsum; 8DLE; -.
DR AlphaFoldDB; P0A6A8; -.
DR EMDB; EMD-12656; -.
DR EMDB; EMD-12657; -.
DR EMDB; EMD-12658; -.
DR EMDB; EMD-12659; -.
DR EMDB; EMD-12660; -.
DR EMDB; EMD-21580; -.
DR SASBDB; P0A6A8; -.
DR SMR; P0A6A8; -.
DR BioGRID; 4263360; 495.
DR BioGRID; 849206; 1.
DR DIP; DIP-29374N; -.
DR IntAct; P0A6A8; 45.
DR STRING; 511145.b1094; -.
DR ChEMBL; CHEMBL3309006; -.
DR DrugBank; DB04450; Heptyl 1-Thiohexopyranoside.
DR DrugBank; DB08405; S-(2-{[N-(2-HYDROXY-4-{[HYDROXY(OXIDO)PHOSPHINO]OXY}-3,3-DIMETHYLBUTANOYL)-BETA-ALANYL]AMINO}ETHYL) HEPTANETHIOATE.
DR DrugBank; DB08404; S-(2-{[N-(2-HYDROXY-4-{[HYDROXY(OXIDO)PHOSPHINO]OXY}-3,3-DIMETHYLBUTANOYL)-BETA-ALANYL]AMINO}ETHYL) HEXANETHIOATE.
DR jPOST; P0A6A8; -.
DR PaxDb; 511145-b1094; -.
DR EnsemblBacteria; AAC74178; AAC74178; b1094.
DR GeneID; 85162693; -.
DR GeneID; 944805; -.
DR KEGG; ecj:JW1080; -.
DR KEGG; eco:b1094; -.
DR PATRIC; fig|1411691.4.peg.1174; -.
DR EchoBASE; EB4297; -.
DR eggNOG; COG0236; Bacteria.
DR HOGENOM; CLU_108696_5_1_6; -.
DR InParanoid; P0A6A8; -.
DR OMA; TMEASFI; -.
DR OrthoDB; 9804551at2; -.
DR PhylomeDB; P0A6A8; -.
DR BioCyc; EcoCyc:EG50003-MONOMER; -.
DR BioCyc; MetaCyc:EG50003-MONOMER; -.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; P0A6A8; -.
DR PRO; PR:P0A6A8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0000035; F:acyl binding; IDA:EcoliWiki.
DR GO; GO:0000036; F:acyl carrier activity; IDA:EcoliWiki.
DR GO; GO:0008289; F:lipid binding; IMP:CAFA.
DR GO; GO:0031177; F:phosphopantetheine binding; IMP:EcoliWiki.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0009245; P:lipid A biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:EcoliWiki.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR HAMAP; MF_01217; Acyl_carrier; 1.
DR InterPro; IPR003231; ACP.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR00517; acyl_carrier; 1.
DR PANTHER; PTHR20863; ACYL CARRIER PROTEIN; 1.
DR PANTHER; PTHR20863:SF77; ACYL CARRIER PROTEIN; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Phosphopantetheine; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2062368,
FT ECO:0000269|PubMed:3549687, ECO:0000269|PubMed:4882207"
FT CHAIN 2..78
FT /note="Acyl carrier protein"
FT /id="PRO_0000180134"
FT DOMAIN 2..77
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 37
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:4882207"
FT MUTAGEN 37
FT /note="S->A,T: Loss of phosphopantetheinylation, and
FT inhibition of cell growth."
FT /evidence="ECO:0000269|PubMed:7673201"
FT CONFLICT 25
FT /note="N -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="V -> I (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="D -> V (in Ref. 2; AAB27925)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="H -> N (in Ref. 2; AAB27925)"
FT /evidence="ECO:0000305"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:1T8K"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1T8K"
FT TURN 29..33
FT /evidence="ECO:0007829|PDB:1T8K"
FT HELIX 37..51
FT /evidence="ECO:0007829|PDB:1T8K"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1T8K"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:1T8K"
SQ SEQUENCE 78 AA; 8640 MW; 41FCFC39D45BFEA1 CRC64;
MSTIEERVKK IIGEQLGVKQ EEVTNNASFV EDLGADSLDT VELVMALEEE FDTEIPDEEA
EKITTVQAAI DYINGHQA
//
