ID   LP14_BACIU              Reviewed;         224 AA.
AC   P39144; Q939C8; Q93R68; Q9KIG7;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=4'-phosphopantetheinyl transferase;
DE            EC=2.7.8.-;
DE   AltName: Full=Lipopeptide antibiotics iturin A and surfactin biosynthesis protein;
GN   Name=lpa-14; Synonyms=lpaA13, lpaB3, sfp-B;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RB14;
RA   Huang C.-C., Ano T., Shoda M.;
RT   "Nucleotide sequence and characteristics of a gene, lpa-14 responsible for
RT   the biosynthesis of the lipopeptide antibiotics iturin A and surfactin from
RT   Bacillus subtilis RB14.";
RL   J. Ferment. Bioeng. 76:445-450(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A13;
RA   Conrad B., Feesche J., Steinborn G., Adler B., Hofemeister J.;
RT   "The lpa gene of Bacillus subtilis A13 affects a spectrum of antibiotic
RT   syntheses.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BBK-1;
RA   Roongsawang N., Morikawa M., Kanaya S.;
RT   "Putative phosphopantetheinyltransferase gene for biosurfactants production
RT   in Bacillus subtilis BBK-1.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B3;
RA   Yao S., Fuchsbauer N., Hillen W.;
RT   "Genetic loci required for biosynthesis of lipopeptide antibiotics iturin A
RT   and surfactin in Bacillus subtilis B3.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PROBABLE 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).
CC   -!- FUNCTION: May activate the peptidyl carrier protein (PCP) domains of
CC       surfactin synthetase SRF1/2/3 and iturin A synthetase, by transferring
CC       the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine
CC       residue. Required for the coproduction of the lipopeptide antibiotics,
CC       iturin A and surfactin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[peptidyl-carrier protein] + CoA = adenosine 3',5'-
CC         bisphosphate + H(+) + holo-[peptidyl-carrier protein];
CC         Xref=Rhea:RHEA:46228, Rhea:RHEA-COMP:11479, Rhea:RHEA-COMP:11480,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:64479;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily.
CC       Gsp/Sfp/HetI/AcpT family. {ECO:0000305}.
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DR   EMBL; D21876; BAA04883.1; -; Genomic_DNA.
DR   EMBL; AF233756; AAF87219.1; -; Genomic_DNA.
DR   EMBL; AB062550; BAB58965.1; -; Genomic_DNA.
DR   EMBL; AY040867; AAL10666.1; -; Genomic_DNA.
DR   PIR; I39875; I39875.
DR   AlphaFoldDB; P39144; -.
DR   SMR; P39144; -.
DR   PRIDE; P39144; -.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.90.470.20; -; 2.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR   Pfam; PF01648; ACPS; 1.
DR   SUPFAM; SSF56214; SSF56214; 2.
DR   TIGRFAMs; TIGR00556; pantethn_trn; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..224
FT                   /note="4'-phosphopantetheinyl transferase"
FT                   /id="PRO_0000206079"
FT   REGION          158..189
FT                   /note="Peptidyl carrier protein binding"
FT                   /evidence="ECO:0000255"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   VARIANT         15
FT                   /note="G -> E (in strain: B3)"
FT   VARIANT         22
FT                   /note="A -> T (in strain: BBK-1)"
FT   VARIANT         65
FT                   /note="G -> A (in strain: BBK-1)"
FT   VARIANT         69
FT                   /note="G -> S (in strain: A13, BBK-1 and B3)"
FT   VARIANT         195
FT                   /note="D -> E (in strain: A13 and B3)"
FT   VARIANT         216
FT                   /note="E -> A (in strain: BBK-1)"
SQ   SEQUENCE   224 AA;  25467 MW;  B3446073EE0DE24A CRC64;
     MKIYGVYMDR PLSAGEEDRM MAAVSAEKRE KCRRFYHKED AHRTLIGDML IRTAAAKAYG
     LDPAGISFGV QEYGKPYIPA LPDMHFNISH SGRWIVCAVD SKPIGIDIEK MKPGTIDIAK
     RFFSPTEYSD LQAKHPDQQT DYFYHLWSMK ESFIKQAGKG LSLPLDSFSV RLKDDGHVSI
     ELPDGHEPCF IRTYDADEEY KLAVCAAHPD FCDGIEMKTY EELL