ID   FFP_BACIU               Reviewed;         224 AA.
AC   Q9F4F7;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=4'-phosphopantetheinyl transferase ffp;
DE            EC=2.7.8.-;
DE   AltName: Full=Fengycin synthase-activating enzyme;
GN   Name=ffp; Synonyms=sfp;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=F29-3;
RA   Shu H.-Y., Liu S.-T.;
RT   "sfp is required for fengycin synthesis.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May activate the peptidyl carrier protein (PCP) domains of
CC       fengycin synthase by transferring the 4'-phosphopantetheinyl moiety of
CC       coenzyme A (CoA) to a serine residue.
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; AY009114; AAG24257.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9F4F7; -.
DR   SMR; Q9F4F7; -.
DR   ChEMBL; CHEMBL1293248; -.
DR   PRIDE; Q9F4F7; -.
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 ffp"
FT                   /id="PRO_0000206078"
FT   REGION          158..189
FT                   /note="Peptidyl carrier protein binding"
FT                   /evidence="ECO:0000250"
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"
SQ   SEQUENCE   224 AA;  25974 MW;  18F9762185FA54CA CRC64;
     MKIYGIYMDR PLSQEETDRL MSFVSAEKRE KCRRFYHKED AHRTLLGDVL VRSVISEQYQ
     LNKADIRFSA QEYGKPCIPD LPNAHFNISH SGHWVIGAFD SDPIGVDIEK MKPISLGIAE
     RFFSKNEYSD LLSKHKDEQN DYFYHLWSMK ESFIKQEGKG LSLPLDSFSV RLHEDGRVSV
     ELPEHHTPCF IKTYEVDPGY KMAVCAARPD FPEDITMISY EALL