ID   ACPS_BRUA2              Reviewed;         134 AA.
AC   Q2YN04;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   02-SEP-2026, entry version 97.
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=BAB1_0679;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group; Brucella;
OC   Brucella melitensis group.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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; AM040264; CAJ10635.1; -; Genomic_DNA.
DR   RefSeq; WP_002963803.1; NC_007618.1.
DR   AlphaFoldDB; Q2YN04; -.
DR   SMR; Q2YN04; -.
DR   STRING; 359391.BAB1_0679; -.
DR   GeneID; 93016935; -.
DR   GeneID; 99644128; -.
DR   KEGG; bmf:BAB1_0679; -.
DR   PATRIC; fig|359391.11.peg.2993; -.
DR   HOGENOM; CLU_089696_0_2_5; -.
DR   PhylomeDB; Q2YN04; -.
DR   Proteomes; UP000002719; Chromosome I.
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   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; IPR004568; Ppantetheine-prot_Trfase_dom.
DR   NCBIfam; TIGR00516; acpS; 1.
DR   NCBIfam; TIGR00556; pantethn_trn; 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..134
FT                   /note="Holo-[acyl-carrier-protein] synthase"
FT                   /id="PRO_0000228275"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
SQ   SEQUENCE   134 AA;  14645 MW;  95A7F7D426A07BDA CRC64;
     MIVGIGSDLI DIRRVEKTLE RHGSRFRDRV FTEIEQRKSE GRKQRAASYA KRFAAKEACA
     KALGTGIAEG VFWRDMGVVN TPSGKPTMHL TGGAAKQLQK LLPAGTNAAI HLTITDDFPL
     AQAFVIIEAL PVLE
//