ID   ACPS_CLOAB              Reviewed;         124 AA.
AC   Q97LR5;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   04-NOV-2026, entry version 121.
DE   RecName: Full=Holo-[acyl-carrier-protein] synthase {ECO:0000255|HAMAP-Rule:MF_00101};
DE            Short=Holo-ACP synthase {ECO:0000255|HAMAP-Rule:MF_00101};
DE            EC=2.7.8.7 {ECO:0000255|HAMAP-Rule:MF_00101};
DE   AltName: Full=4'-phosphopantetheinyl transferase AcpS {ECO:0000255|HAMAP-Rule:MF_00101};
GN   Name=acpS {ECO:0000255|HAMAP-Rule:MF_00101};
GN   OrderedLocusNames=CA_C0489;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM
OS   19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC
RC   13948 / NRRL B-527 / VKM B-1787 / 2291 / W;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to
CC       a Ser of acyl-carrier-protein. {ECO:0000255|HAMAP-Rule:MF_00101}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[ACP] + CoA = holo-[ACP] + adenosine 3',5'-bisphosphate +
CC         H(+); Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9690,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00101};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00101};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00101}.
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC       {ECO:0000255|HAMAP-Rule:MF_00101}.
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DR   EMBL; AE001437; AAK78469.1; -; Genomic_DNA.
DR   PIR; B96960; B96960.
DR   RefSeq; WP_010963811.1; NC_003030.1.
DR   SMR; Q97LR5; -.
DR   STRING; 272562.CA_C0489; -.
DR   GeneID; 44996998; -.
DR   KEGG; cac:CA_C0489; -.
DR   PATRIC; fig|272562.8.peg.688; -.
DR   eggNOG; COG0736; Bacteria.
DR   HOGENOM; CLU_089696_0_2_9; -.
DR   OMA; AAEWQEY; -.
DR   OrthoDB; 517356at2; -.
DR   Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1.
DR   HAMAP; MF_00101; AcpS; 1.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   InterPro; IPR002582; ACPS.
DR   InterPro; IPR050559; P-Pant_transferase_sf.
DR   InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR   PANTHER; PTHR12215:SF10; L-AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE; 1.
DR   PANTHER; PTHR12215; PHOSPHOPANTETHEINE TRANSFERASE; 1.
DR   Pfam; PF01648; ACPS; 1.
DR   SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1.
DR   NCBIfam; TIGR00516; acpS; 1.
DR   NCBIfam; TIGR00556; pantethn_trn; 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Proteomes; UP000000814; Chromosome.
DR   AlphaFoldDB; Q97LR5; -.
PE   3: Inferred from homology;
KW   Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..124
FT                   /note="Holo-[acyl-carrier-protein] synthase"
FT                   /id="PRO_0000175636"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT   BINDING         56
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
SQ   SEQUENCE   124 AA;  13882 MW;  69E0B5C3952E2790 CRC64;
     MIKGVGVDII EINRVKNAID RNYKFIEKLF SRREIAYIKA EKTKAQYIAG RFSAKEAVSK
     ALGTGFRGFS FKNIEIHKDD LGKPIVVLNG GARAIAEGYG KYQVQLSISH DREKAIAYAV
     LEVF
//