ACPS_STRCO
ID ACPS_STRCO Reviewed; 123 AA.
AC O86785;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=SCO4744;
GN ORFNames=SC6G4.22c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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 -!- 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; AL939121; CAA20400.1; -; Genomic_DNA.
DR PIR; T35573; T35573.
DR RefSeq; NP_628902.1; NC_003888.3.
DR RefSeq; WP_003974229.1; NZ_VNID01000016.1.
DR PDB; 2JBZ; X-ray; 1.62 A; A=1-123.
DR PDB; 2JCA; X-ray; 1.98 A; A/B/C=1-123.
DR PDB; 2WDO; X-ray; 1.56 A; A=1-123.
DR PDB; 2WDS; X-ray; 1.35 A; A=1-123.
DR PDB; 2WDY; X-ray; 1.40 A; A=1-123.
DR PDBsum; 2JBZ; -.
DR PDBsum; 2JCA; -.
DR PDBsum; 2WDO; -.
DR PDBsum; 2WDS; -.
DR PDBsum; 2WDY; -.
DR AlphaFoldDB; O86785; -.
DR SMR; O86785; -.
DR STRING; 100226.SCO4744; -.
DR GeneID; 1100185; -.
DR KEGG; sco:SCO4744; -.
DR PATRIC; fig|100226.15.peg.4816; -.
DR eggNOG; COG0736; Bacteria.
DR HOGENOM; CLU_089696_0_0_11; -.
DR InParanoid; O86785; -.
DR OMA; LGVRSWH; -.
DR BRENDA; 2.7.8.7; 5998.
DR EvolutionaryTrace; O86785; -.
DR Proteomes; UP000001973; 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..123
FT /note="Holo-[acyl-carrier-protein] synthase"
FT /id="PRO_0000175711"
FT BINDING 9
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"
FT STRAND 2..12
FT /evidence="ECO:0007829|PDB:2WDS"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:2WDS"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:2WDS"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:2WDS"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2WDS"
FT HELIX 46..62
FT /evidence="ECO:0007829|PDB:2WDS"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:2WDS"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2WDS"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2WDS"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:2WDS"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:2WDS"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:2WDS"
SQ SEQUENCE 123 AA; 12566 MW; C8301B17E510E56D CRC64;
MSIIGVGIDV AEVERFGAAL ERTPALAGRL FLESELLLPG GERRGVASLA ARFAAKEALA
KALGAPAGLL WTDAEVWVEA GGRPRLRVTG TVAARAAELG VASWHVSLSH DAGIASAVVI
AEG
