ID   ACPT_ECO57              Reviewed;         195 AA.
AC   Q8X5U4;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=4'-phosphopantetheinyl transferase AcpT;
DE            EC=2.7.8.7 {ECO:0000250|UniProtKB:P37623};
GN   Name=acpT; OrderedLocusNames=Z4867, ECs4342;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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:0000250|UniProtKB:P37623}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC         [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC         Evidence={ECO:0000250|UniProtKB:P37623};
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily.
CC       Gsp/Sfp/HetI/AcpT family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58602.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37765.1; -; Genomic_DNA.
DR   PIR; F86017; F86017.
DR   PIR; F91171; F91171.
DR   RefSeq; NP_312369.1; NC_002695.1.
DR   RefSeq; WP_000285784.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X5U4; -.
DR   SMR; Q8X5U4; -.
DR   STRING; 155864.EDL933_4706; -.
DR   PRIDE; Q8X5U4; -.
DR   EnsemblBacteria; AAG58602; AAG58602; Z4867.
DR   EnsemblBacteria; BAB37765; BAB37765; ECs_4342.
DR   GeneID; 66672641; -.
DR   GeneID; 915791; -.
DR   KEGG; ece:Z4867; -.
DR   KEGG; ecs:ECs_4342; -.
DR   PATRIC; fig|386585.9.peg.4535; -.
DR   eggNOG; COG2091; Bacteria.
DR   HOGENOM; CLU_119926_0_0_6; -.
DR   OMA; WQIVSID; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   Gene3D; 3.90.470.20; -; 1.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   Pfam; PF01648; ACPS; 1.
DR   SUPFAM; SSF56214; SSF56214; 2.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..195
FT                   /note="4'-phosphopantetheinyl transferase AcpT"
FT                   /id="PRO_0000206082"
SQ   SEQUENCE   195 AA;  21738 MW;  360557D7230B2AB7 CRC64;
     MYRIVLGKVS TLSAAPLPPG LREQAPQGPR RERWLAGRAL LSHTLSPLPE IIYGEQGKPA
     FAPETPLWFN LSHSGDDIAL LLSDEGEVGC DIEVIRPRAN WRWLANAVFS LGEHAEMDAV
     HPDQQLEMFW RIWTRKEAIV KQRGGSAWQI VSVDSTYHSS LSVSHCQLEN LSLAICTPTP
     FTLTADSVQW IDSVN