ID   ACPT_SALTI              Reviewed;         192 AA.
AC   Q8Z259;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=4'-phosphopantetheinyl transferase AcpT;
DE            EC=2.7.8.7 {ECO:0000250|UniProtKB:P37623};
GN   Name=acpT; OrderedLocusNames=STY4228, t3939;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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}.
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DR   EMBL; AL513382; CAD08047.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO71410.1; -; Genomic_DNA.
DR   RefSeq; NP_458338.1; NC_003198.1.
DR   RefSeq; WP_000284366.1; NZ_WSUR01000001.1.
DR   AlphaFoldDB; Q8Z259; -.
DR   SMR; Q8Z259; -.
DR   STRING; 220341.16505027; -.
DR   EnsemblBacteria; AAO71410; AAO71410; t3939.
DR   KEGG; stt:t3939; -.
DR   KEGG; sty:STY4228; -.
DR   PATRIC; fig|220341.7.peg.4318; -.
DR   eggNOG; COG2091; Bacteria.
DR   HOGENOM; CLU_119926_0_0_6; -.
DR   OMA; WQIVSID; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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   Transferase.
FT   CHAIN           1..192
FT                   /note="4'-phosphopantetheinyl transferase AcpT"
FT                   /id="PRO_0000206083"
SQ   SEQUENCE   192 AA;  20871 MW;  C1C257B1707141F3 CRC64;
     MYQIVLGKVS TLSAGQLPDA LIAQAPQGVR RASWLAGRVL LSRALSPLPE MVYGEQGKPA
     FSAGTPLWFN LSHSGDTIAL LLSDEGEVGC DIEVIRPRDN WRSLANAVFS LGEHAEMEAE
     RPERQLAAFW RIWTRKEAIV KQRGGSAWQI VSVDSTLPSA LSVSQCQLDT LSLAVCTPTP
     FTLTPQTITK AL