ID   GSP_ANEMI               Reviewed;         237 AA.
AC   P40683;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=4'-phosphopantetheinyl transferase gsp;
DE            EC=2.7.8.-;
DE   AltName: Full=Gramicidin synthase-activating enzyme;
GN   Name=gsp;
OS   Aneurinibacillus migulanus (Bacillus migulanus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=47500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9999 / DSM 2895 / JCM 8504 / NBRC 15520 / NCIMB 7096 / NCTC
RC   7096;
RX   PubMed=7512553; DOI=10.1128/jb.176.8.2458-2462.1994;
RA   Borchert S., Stachelhaus T., Marahiel M.A.;
RT   "Induction of surfactin production in Bacillus subtilis by gsp, a gene
RT   located upstream of the gramicidin S operon in Bacillus brevis.";
RL   J. Bacteriol. 176:2458-2462(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-237.
RC   STRAIN=ATCC 9999 / DSM 2895 / JCM 8504 / NBRC 15520 / NCIMB 7096 / NCTC
RC   7096;
RX   PubMed=2477357; DOI=10.1128/jb.171.10.5422-5429.1989;
RA   Kraetzschmar J., Krause M., Marahiel M.A.;
RT   "Gramicidin S biosynthesis operon containing the structural genes grsA and
RT   grsB has an open reading frame encoding a protein homologous to fatty acid
RT   thioesterases.";
RL   J. Bacteriol. 171:5422-5429(1989).
RN   [3]
RP   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: Activates the five peptidyl carrier protein (PCP) domains of
CC       gramicidin synthase GrsAB, by transferring the 4'-phosphopantetheinyl
CC       moiety of coenzyme A (CoA) to a serine residue. Required for gramicidin
CC       S production. {ECO:0000269|PubMed:8939709}.
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; M29703; AAA58716.1; -; Genomic_DNA.
DR   EMBL; X76434; CAA53988.1; -; Genomic_DNA.
DR   EMBL; X15577; CAA33601.1; -; Genomic_DNA.
DR   PIR; A55218; A55218.
DR   RefSeq; WP_052811850.1; NZ_LGUG01000004.1.
DR   AlphaFoldDB; P40683; -.
DR   SMR; P40683; -.
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..237
FT                   /note="4'-phosphopantetheinyl transferase gsp"
FT                   /id="PRO_0000206076"
FT   BINDING         106
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   237 AA;  27857 MW;  9F0DE1D27AE5AE84 CRC64;
     MIEMLFVKVP NEIDRHVFNF LSSNVSKEKQ QAFVRYVNVK DAYRSLLGEL LIRKYLIQVL
     NIPNENILFR KNEYGKPFVD FDIHFNISHS DEWVVCAISN HPVGIDIERI SEIDIKIAEQ
     FFHENEYIWL QSKAQNSQVS SFFELWTIKE SYIKAIGKGM YIPINSFWID KNQTQTVIYK
     QNKKEPVTIY EPELFEGYKC SCCSLFSSVT NLSITKLQVQ ELCNLFLDST FSENNNF