ID   ACPT_SALTY              Reviewed;         192 AA.
AC   Q8ZLE2;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=4'-phosphopantetheinyl transferase AcpT;
DE            EC=2.7.8.7 {ECO:0000250|UniProtKB:P37623};
GN   Name=acpT; OrderedLocusNames=STM3583;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: May be involved in an alternative pathway for
CC       phosphopantetheinyl transfer and holo-ACP synthesis. The native apo-
CC       protein substrate is unknown. {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}.
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; AE006468; AAL22443.1; -; Genomic_DNA.
DR   RefSeq; NP_462484.1; NC_003197.2.
DR   RefSeq; WP_000285376.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZLE2; -.
DR   SMR; Q8ZLE2; -.
DR   STRING; 99287.STM3583; -.
DR   PaxDb; Q8ZLE2; -.
DR   EnsemblBacteria; AAL22443; AAL22443; STM3583.
DR   GeneID; 1255106; -.
DR   KEGG; stm:STM3583; -.
DR   PATRIC; fig|99287.12.peg.3786; -.
DR   HOGENOM; CLU_119926_0_0_6; -.
DR   OMA; WQIVSID; -.
DR   PhylomeDB; Q8ZLE2; -.
DR   BioCyc; SENT99287:STM3583-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
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..192
FT                   /note="4'-phosphopantetheinyl transferase AcpT"
FT                   /id="PRO_0000206084"
SQ   SEQUENCE   192 AA;  20799 MW;  E530B7A3EF30EC7A CRC64;
     MYQVVLGKVS TLSAGQLPDA LIAQAPQGVR RASWLAGRVL LSRALSPLPE MVYGEQGKPA
     FSAGAPLWFN LSHSGDTIAL LLSDEGEVGC DIEVIRPRDN WRSLANAVFS LGEHAEMEAE
     RPEQQLAAFW RIWTRKEAIV KQRGGSAWQI VSVDSTLPSA LSVSQCQLDT LSLAVCTPTP
     FTLTPQTITK AL