ID   ACPS_CALS8              Reviewed;         123 AA.
AC   A4XIB7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   02-SEP-2026, entry version 90.
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=Csac_1038;
OS   Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS   6331).
OC   Bacteria; Bacillati; Bacillota; Bacillota incertae sedis;
OC   Caldicellulosiruptorales; Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX   NCBI_TaxID=351627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A.,
RA   VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J.,
RA   Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M.,
RA   Kengen S.M.W., Richardson P.;
RT   "Genome sequence of the thermophilic hydrogen-producing bacterium
RT   Caldicellulosiruptor saccharolyticus DSM 8903.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000679; ABP66652.1; -; Genomic_DNA.
DR   RefSeq; WP_011916599.1; NC_009437.1.
DR   AlphaFoldDB; A4XIB7; -.
DR   SMR; A4XIB7; -.
DR   STRING; 351627.Csac_1038; -.
DR   KEGG; csc:Csac_1038; -.
DR   eggNOG; COG0736; Bacteria.
DR   HOGENOM; CLU_089696_0_2_9; -.
DR   OrthoDB; 517356at2; -.
DR   Proteomes; UP000000256; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   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   NCBIfam; TIGR00516; acpS; 1.
DR   NCBIfam; TIGR00556; pantethn_trn; 1.
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.
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..123
FT                   /note="Holo-[acyl-carrier-protein] synthase"
FT                   /id="PRO_1000008404"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
SQ   SEQUENCE   123 AA;  13982 MW;  178CBE12567680F3 CRC64;
     MIFNIGIDIV EVERFKNIKR FDSFLKRVFT QKELEYIRSK NFNMLTIAGY FAAKEAVAKA
     LSTGIVFGFK DIEIQKDTNG CPKVKLYNRA KEICENLKIT NIVLSISHQN SVAVACAIAE
     KEE
//