ID ACPT_ECOLI Reviewed; 195 AA. AC P37623; Q2M7D8; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 04-NOV-2026, entry version 166. DE RecName: Full=4'-phosphopantetheinyl transferase AcpT; DE EC=2.7.8.7 {ECO:0000305|PubMed:10625633}; GN Name=acpT {ECO:0000303|PubMed:10625633}; Synonyms=yhhU; GN OrderedLocusNames=b3475, JW3440; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8041620; DOI=10.1093/nar/22.13.2576; RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.; RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region RT from 76.0 to 81.5 minutes."; RL Nucleic Acids Res. 22:2576-2586(1994). RN [2] 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 [3] 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 [4] RP FUNCTION. RX PubMed=8939709; DOI=10.1016/s1074-5521(96)90181-7; RA Lambalot R.H., Gehring A.M., Flugel R.S., Zuber P., LaCelle M., RA Marahiel M.A., Reid R., Khosla C., Walsh C.T.; RT "A new enzyme superfamily -- the phosphopantetheinyl transferases."; RL Chem. Biol. 3:923-936(1996). RN [5] RP FUNCTION. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=10625633; DOI=10.1074/jbc.275.2.959; RA Flugel R.S., Hwangbo Y., Lambalot R.H., Cronan J.E. Jr., Walsh C.T.; RT "Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in RT Escherichia coli."; RL J. Biol. Chem. 275:959-968(2000). CC -!- FUNCTION: May be involved in an alternative pathway for CC phosphopantetheinyl transfer and holo-ACP synthesis in E.coli. The CC native apo-protein substrate is unknown. Is able to functionally CC replace AcpS in vivo but only when expressed at high levels. CC {ECO:0000269|PubMed:10625633, ECO:0000269|PubMed:8939709}. CC -!- CATALYTIC ACTIVITY: CC Reaction=apo-[ACP] + CoA = holo-[ACP] + adenosine 3',5'-bisphosphate + CC H(+); Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9690, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7; CC Evidence={ECO:0000305|PubMed:10625633}; CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. CC Gsp/Sfp/HetI/AcpT family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U00039; AAB18450.1; -; Genomic_DNA. DR EMBL; U00096; AAC76500.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77818.1; -; Genomic_DNA. DR PIR; S47694; S47694. DR RefSeq; NP_417932.1; NC_000913.3. DR RefSeq; WP_000285774.1; NZ_CP009789.1. DR AlphaFoldDB; P37623; -. DR SMR; P37623; -. DR BioGRID; 4259300; 100. DR DIP; DIP-12355N; -. DR FunCoup; P37623; 54. DR IntAct; P37623; 1. DR STRING; 511145.b3475; -. DR jPOST; P37623; -. DR PaxDb; 511145-b3475; -. DR EnsemblBacteria; AAC76500; AAC76500; b3475. DR GeneID; 947979; -. DR KEGG; ecj:JW3440; -. DR KEGG; eco:b3475; -. DR KEGG; ecoc:C3026_18820; -. DR PATRIC; fig|1411691.4.peg.3250; -. DR EchoBASE; EB2135; -. DR eggNOG; COG2091; Bacteria. DR HOGENOM; CLU_119926_0_0_6; -. DR InParanoid; P37623; -. DR OMA; ADDYPLW; -. DR OrthoDB; 9808281at2; -. DR PhylomeDB; P37623; -. DR BioCyc; EcoCyc:EG12221-MONOMER; -. DR BioCyc; MetaCyc:EG12221-MONOMER; -. DR PRO; PR:P37623; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IDA:EcoliWiki. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IGI:EcoliWiki. DR GO; GO:0051604; P:protein maturation; IBA:GO_Central. DR FunFam; 3.90.470.20:FF:000002; Holo-(Acyl carrier protein) synthase 2; 1. DR FunFam; 3.90.470.20:FF:000004; Holo-(Acyl carrier protein) synthase 2; 1. DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1. DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom. DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf. DR InterPro; IPR050559; P-Pant_transferase_sf. DR NCBIfam; NF007676; acpT; 1. DR PANTHER; PTHR12215:SF10; L-AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE; 1. DR PANTHER; PTHR12215; PHOSPHOPANTETHEINE TRANSFERASE; 1. DR Pfam; PF01648; ACPS; 1. DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 2. PE 3: Inferred from homology; KW Reference proteome; Transferase. FT CHAIN 1..195 FT /note="4'-phosphopantetheinyl transferase AcpT" FT /id="PRO_0000206081" SQ SEQUENCE 195 AA; 21768 MW; 29385FDA343B2AB7 CRC64; MYRIVLGKVS TLSAAPLPPG LREQAPQGPR RERWLAGRAL LSHTLSPLPE IIYGEQGKPA FAPEMPLWFN LSHSGDDIAL LLSDEGEVGC DIEVIRPRAN WRWLANAVFS LGEHAEMDAV HPDQQLEMFW RIWTRKEAIV KQRGGSAWQI VSVDSTYHSS LSVSHCQLEN LSLAICTPTP FTLTADSVQW IDSVN //