ID   ACPS_BACSU              Reviewed;         121 AA.
AC   P96618;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 153.
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}; Synonyms=ydcB;
GN   OrderedLocusNames=BSU04620;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11489886; DOI=10.1074/jbc.m103556200;
RA   Mootz H.D., Finking R., Marahiel M.A.;
RT   "4'-phosphopantetheine transfer in primary and secondary metabolism of
RT   Bacillus subtilis.";
RL   J. Biol. Chem. 276:37289-37298(2001).
RN   [4]
RP   MUTAGENESIS OF ILE-2; ILE-5 AND GLN-113, X-RAY CRYSTALLOGRAPHY (1.5
RP   ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH COENZYME A AND WITH
RP   HOLO-(ACYL-CARRIER-PROTEIN), AND SUBUNIT.
RX   PubMed=10997907; DOI=10.1016/s0969-2126(00)00178-7;
RA   Parris K.D., Lin L., Tam A., Mathew R., Hixon J., Stahl M., Fritz C.C.,
RA   Seehra J., Somers W.S.;
RT   "Crystal structures of substrate binding to Bacillus subtilis holo-(acyl
RT   carrier protein) synthase reveal a novel trimeric arrangement of molecules
RT   resulting in three active sites.";
RL   Structure 8:883-895(2000).
CC   -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to
CC       a Ser of fatty acid acyl-carrier-protein ACP. Also modifies the D-
CC       alanyl carrier protein but fails to recognize PCP and AcpK, an acyl
CC       carrier protein of secondary metabolism. {ECO:0000269|PubMed:11489886}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC         [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:9690, 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         ECO:0000269|PubMed:11489886};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00101};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10997907}.
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; AB001488; BAA19299.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12269.1; -; Genomic_DNA.
DR   PIR; H69772; H69772.
DR   RefSeq; NP_388343.1; NC_000964.3.
DR   RefSeq; WP_003234281.1; NZ_JNCM01000031.1.
DR   PDB; 1F7L; X-ray; 1.50 A; A=1-121.
DR   PDB; 1F7T; X-ray; 1.80 A; A/B/C/D/E/F=2-121.
DR   PDB; 1F80; X-ray; 2.30 A; A/B/C=2-121.
DR   PDBsum; 1F7L; -.
DR   PDBsum; 1F7T; -.
DR   PDBsum; 1F80; -.
DR   AlphaFoldDB; P96618; -.
DR   SMR; P96618; -.
DR   IntAct; P96618; 1.
DR   STRING; 224308.BSU04620; -.
DR   BindingDB; P96618; -.
DR   ChEMBL; CHEMBL4734; -.
DR   DrugBank; DB04447; 1,4-Dithiothreitol.
DR   DrugBank; DB01992; Coenzyme A.
DR   DrugCentral; P96618; -.
DR   PaxDb; 224308-BSU04620; -.
DR   EnsemblBacteria; CAB12269; CAB12269; BSU_04620.
DR   GeneID; 938194; -.
DR   KEGG; bsu:BSU04620; -.
DR   PATRIC; fig|224308.179.peg.490; -.
DR   eggNOG; COG0736; Bacteria.
DR   InParanoid; P96618; -.
DR   OrthoDB; 517356at2; -.
DR   PhylomeDB; P96618; -.
DR   BioCyc; BSUB:BSU04620-MONOMER; -.
DR   SABIO-RK; P96618; -.
DR   EvolutionaryTrace; P96618; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
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   PANTHER; PTHR12215:SF24; HOLO-[ACYL-CARRIER-PROTEIN] SYNTHASE; 1.
DR   PANTHER; PTHR12215; PHOSPHOPANTETHEINE TRANSFERASE; 1.
DR   Pfam; PF01648; ACPS; 1.
DR   SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..121
FT                   /note="Holo-[acyl-carrier-protein] synthase"
FT                   /id="PRO_0000175613"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         58
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   MUTAGEN         2
FT                   /note="I->A: 6% of wild-type activity."
FT                   /evidence="ECO:0000269|PubMed:10997907"
FT   MUTAGEN         5
FT                   /note="I->R: Loss of activity; no trimer formation."
FT                   /evidence="ECO:0000269|PubMed:10997907"
FT   MUTAGEN         113
FT                   /note="Q->E: 14% of wild-type activity."
FT                   /evidence="ECO:0000269|PubMed:10997907"
FT   MUTAGEN         113
FT                   /note="Q->R: Loss of activity; no trimer formation."
FT                   /evidence="ECO:0000269|PubMed:10997907"
FT   STRAND          2..11
FT                   /evidence="ECO:0007829|PDB:1F7L"
FT   HELIX           12..21
FT                   /evidence="ECO:0007829|PDB:1F7L"
FT   HELIX           25..29
FT                   /evidence="ECO:0007829|PDB:1F7L"
FT   HELIX           32..38
FT                   /evidence="ECO:0007829|PDB:1F7L"
FT   HELIX           43..63
FT                   /evidence="ECO:0007829|PDB:1F7L"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:1F80"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:1F7L"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:1F7L"
FT   STRAND          87..91
FT                   /evidence="ECO:0007829|PDB:1F7L"
FT   TURN            92..94
FT                   /evidence="ECO:0007829|PDB:1F7L"
FT   STRAND          95..105
FT                   /evidence="ECO:0007829|PDB:1F7L"
FT   STRAND          107..117
FT                   /evidence="ECO:0007829|PDB:1F7L"
SQ   SEQUENCE   121 AA;  13718 MW;  6C10401DA7116701 CRC64;
     MIYGIGLDIT ELKRIASMAG RQKRFAERIL TRSELDQYYE LSEKRKNEFL AGRFAAKEAF
     SKAFGTGIGR QLSFQDIEIR KDQNGKPYII CTKLSQAAVH VSITHTKEYA AAQVVIERLS
     S
//