ID   PPTA_STRMB              Reviewed;         246 AA.
AC   Q9F0Q6;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=4'-phosphopantetheinyl transferase Svp;
DE            Short=PPTase;
DE            EC=2.7.8.7 {ECO:0000269|PubMed:11451672, ECO:0000269|PubMed:18805498};
GN   Name=svp;
OS   Streptomyces mobaraensis (Streptoverticillium mobaraense).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=35621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 15003 / DSM 40903 / B-80-Z2;
RX   PubMed=11451672; DOI=10.1016/s1074-5521(01)00047-3;
RA   Sanchez C., Du L., Edwards D.J., Toney M.D., Shen B.;
RT   "Cloning and characterization of a phosphopantetheinyl transferase from
RT   Streptomyces verticillus ATCC15003, the producer of the hybrid peptide-
RT   polyketide antitumor drug bleomycin.";
RL   Chem. Biol. 8:725-738(2001).
RN   [2]
RP   CATALYTIC ACTIVITY.
RX   PubMed=18805498; DOI=10.1016/j.fgb.2008.08.009;
RA   Schneider P., Bouhired S., Hoffmeister D.;
RT   "Characterization of the atromentin biosynthesis genes and enzymes in the
RT   homobasidiomycete Tapinella panuoides.";
RL   Fungal Genet. Biol. 45:1487-1496(2008).
CC   -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to
CC       a Ser of an acyl-carrier-protein. The enzyme is able to transfer the
CC       cofactor to a broad range of enzymes with acyl- or peptidyl-carrier
CC       protein domains. {ECO:0000269|PubMed:11451672,
CC       ECO:0000269|PubMed:18805498}.
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:0000269|PubMed:11451672, ECO:0000269|PubMed:18805498};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.9 uM for Streptomyces mobaraensis apo-PCP BlmI
CC         {ECO:0000269|PubMed:11451672};
CC         KM=3.1 uM for Streptomyces glaucescens apo-ACP TcmM
CC         {ECO:0000269|PubMed:11451672};
CC         Note=kcat is 11 min(-1) with S.mobaraensis apo-PCP BlmI as substrate
CC         and 86 min(-1) with S.glaucescens apo-ACP TcmM as substrate.
CC         {ECO:0000269|PubMed:11451672};
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily.
CC       Gsp/Sfp/HetI/AcpT family. {ECO:0000305}.
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DR   EMBL; AF210311; AAG43513.1; -; Genomic_DNA.
DR   RefSeq; WP_004954939.1; NZ_VOKX01000009.1.
DR   AlphaFoldDB; Q9F0Q6; -.
DR   SMR; Q9F0Q6; -.
DR   GO; GO:0009366; C:enterobactin synthetase complex; IEA:InterPro.
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   GO; GO:0009239; P:enterobactin biosynthetic process; IEA:InterPro.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   InterPro; IPR041354; 4PPT_N.
DR   InterPro; IPR003542; Enbac_synth_compD-like.
DR   PANTHER; PTHR38096; PTHR38096; 1.
DR   Pfam; PF17837; 4PPT_N; 1.
DR   Pfam; PF01648; ACPS; 1.
DR   PRINTS; PR01399; ENTSNTHTASED.
DR   SUPFAM; SSF56214; SSF56214; 1.
PE   1: Evidence at protein level;
KW   Transferase.
FT   CHAIN           1..246
FT                   /note="4'-phosphopantetheinyl transferase Svp"
FT                   /id="PRO_0000442637"
FT   REGION          223..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   246 AA;  25619 MW;  EA412440A0050767 CRC64;
     MIAALLPSWA VTEHAFTDAP DDPVSLLFPE EAAHVARAVP KRLHEFATVR VCARAALGRL
     GLPPGPLLPG RRGAPSWPDG VVGSMTHCQG FRGAAVARAA DAASLGIDAE PNGPLPDGVL
     AMVSLPSERE WLAGLAARRP DVHWDRLLFS AKESVFKAWY PLTGLELDFD EAELAVDPDA
     GTFTARLLVP GPVVGGRRLD GFEGRWAAGE GLVVTAIAVA APAGTAEESA EGAGKEATAD
     DRTAVP