ACPS_STRPN
ID ACPS_STRPN Reviewed; 120 AA.
AC P0A2W6; Q9F7T5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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}; OrderedLocusNames=SP_1699;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH 3'-5'-ADP, AND
RP SUBUNIT.
RX PubMed=11032795; DOI=10.1093/emboj/19.20.5281;
RA Chirgadze N.Y., Briggs S.L., McAllister K.A., Fischl A.S., Zhao G.;
RT "Crystal structure of Streptococcus pneumoniae acyl carrier protein
RT synthase: an essential enzyme in bacterial fatty acid biosynthesis.";
RL EMBO J. 19:5281-5287(2000).
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 = 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00101};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:11032795}.
CC -!- INTERACTION:
CC P0A2W6; P95830: dnaJ; NbExp=2; IntAct=EBI-2207344, EBI-2207079;
CC P0A2W6; Q97SE5: gatC; NbExp=2; IntAct=EBI-2207344, EBI-2207053;
CC P0A2W6; Q97NV3: groES; NbExp=2; IntAct=EBI-2207344, EBI-2206949;
CC P0A2W6; Q97S73: grpE; NbExp=2; IntAct=EBI-2207344, EBI-2207065;
CC P0A2W6; Q97SR4: uppS; NbExp=2; IntAct=EBI-2207344, EBI-2206983;
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; AE005672; AAK75777.1; -; Genomic_DNA.
DR PIR; H95197; H95197.
DR PDB; 1FTE; X-ray; 2.40 A; A/B/C=1-120.
DR PDB; 1FTF; X-ray; 2.05 A; A/B/C=1-120.
DR PDB; 1FTH; X-ray; 1.90 A; A/B/C=1-120.
DR PDBsum; 1FTE; -.
DR PDBsum; 1FTF; -.
DR PDBsum; 1FTH; -.
DR AlphaFoldDB; P0A2W6; -.
DR SMR; P0A2W6; -.
DR IntAct; P0A2W6; 5.
DR STRING; 170187.SP_1699; -.
DR EnsemblBacteria; AAK75777; AAK75777; SP_1699.
DR KEGG; spn:SP_1699; -.
DR eggNOG; COG0736; Bacteria.
DR OMA; DERHYAV; -.
DR PhylomeDB; P0A2W6; -.
DR EvolutionaryTrace; P0A2W6; -.
DR Proteomes; UP000000585; 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 Transferase.
FT CHAIN 1..120
FT /note="Holo-[acyl-carrier-protein] synthase"
FT /id="PRO_0000175713"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:1FTH"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:1FTH"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:1FTH"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:1FTH"
FT HELIX 43..63
FT /evidence="ECO:0007829|PDB:1FTH"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1FTH"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1FTH"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:1FTH"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1FTH"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:1FTH"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:1FTH"
SQ SEQUENCE 120 AA; 13388 MW; 7FFB1848AC63DAEE CRC64;
MIVGHGIDIE ELASIESAVT RHEGFAKRVL TAQEMERFTS LKGRRQIEYL AGRWSAKEAF
SKAMGTGISK LGFQDLEVLN NERGAPYFSQ APFSGKIWLS ISHTDQFVTA SVILEENHES
