ACPS_BACSU
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 03-AUG-2022, entry version 146.
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; Firmicutes; 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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; 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; P96618; -.
DR PRIDE; P96618; -.
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 OMA; DERHYAV; -.
DR PhylomeDB; P96618; -.
DR BioCyc; BSUB:BSU04620-MON; -.
DR SABIO-RK; P96618; -.
DR EvolutionaryTrace; P96618; -.
DR Proteomes; UP000001570; Chromosome.
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; -; 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 Pfam; PF01648; ACPS; 1.
DR SUPFAM; SSF56214; SSF56214; 1.
DR TIGRFAMs; TIGR00516; acpS; 1.
DR TIGRFAMs; TIGR00556; pantethn_trn; 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
