PSF1_BACPU
ID PSF1_BACPU Reviewed; 233 AA.
AC P55810;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=4'-phosphopantetheinyl transferase psf-1;
DE EC=2.7.8.-;
DE AltName: Full=Surfactin synthesis regulator;
GN Name=psf-1;
OS Bacillus pumilus (Bacillus mesentericus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1408;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A-1;
RA Morikawa M., Ito M., Imanaka T.;
RT "Isolation of a new surfactin producer Bacillus pumilus A-1, and cloning
RT and nucleotide sequence of the regulator gene, psf-1.";
RL J. Ferment. Bioeng. 74:255-261(1992).
RN [2]
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: Probably activates the peptidyl carrier protein (PCP) domains
CC of surfactin synthetase by transferring the 4'-phosphopantetheinyl
CC moiety of coenzyme A (CoA) to a serine residue. Required for the
CC production of the lipopeptide antibiotic, 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 AlphaFoldDB; P55810; -.
DR SMR; P55810; -.
DR UCD-2DPAGE; P55810; -.
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..233
FT /note="4'-phosphopantetheinyl transferase psf-1"
FT /id="PRO_0000206080"
FT REGION 161..192
FT /note="Peptidyl carrier protein binding"
FT /evidence="ECO:0000255"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 233 AA; 26510 MW; 6D7BE017D6059889 CRC64;
MKIFAIQLQP LDDKNARKQI EQLKPFVSFE KRAAAERFRF LIDARRTLLG EVLIRHIIHE
MYALPMEQII FETEGNGKPV VRQIPSFHFN LSHSGDWVVG AVDDAPVGID IEEIKPIDLA
IAERFFSADE YQDLLSQPAE RQEAYFFHLW SMKEAFIKLT GKGISYGLSS FTARLSEDGQ
ATLRLPDHEA PCVVQTYSLD PAYQMAVCTR KPAAAEHVEI LTCENMLSRL NNV
