ID ACPS_MYCS2 Reviewed; 130 AA. AC A0R1H6; I7FI79; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 11-DEC-2019, entry version 86. 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=MSMEG_4756, MSMEI_4636; OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium OS smegmatis). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=246196; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., RA Fraser C.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20; RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.; RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic RT mutations or sequencing errors?"; RL Genome Biol. 8:R20.1-R20.9(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR METHIONINE. RC STRAIN=ATCC 700084 / mc(2)155; RX PubMed=18955433; DOI=10.1101/gr.081901.108; RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.; RT "Ortho-proteogenomics: multiple proteomes investigation through orthology RT and a new MS-based protocol."; RL Genome Res. 19:128-135(2009). 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}. 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; CP000480; ABK75003.1; -; Genomic_DNA. DR EMBL; CP001663; AFP41085.1; -; Genomic_DNA. DR RefSeq; WP_003896157.1; NZ_SIJM01000004.1. DR RefSeq; YP_889014.1; NC_008596.1. DR PDB; 3GWM; X-ray; 1.70 A; A=2-130. DR PDBsum; 3GWM; -. DR SMR; A0R1H6; -. DR STRING; 246196.MSMEI_4636; -. DR EnsemblBacteria; ABK75003; ABK75003; MSMEG_4756. DR EnsemblBacteria; AFP41085; AFP41085; MSMEI_4636. DR GeneID; 4536674; -. DR KEGG; msb:LJ00_23530; -. DR KEGG; msg:MSMEI_4636; -. DR KEGG; msm:MSMEG_4756; -. DR PATRIC; fig|246196.19.peg.4641; -. DR eggNOG; ENOG4105IBS; Bacteria. DR eggNOG; COG0736; LUCA. DR HOGENOM; HOG000014315; -. DR KO; K00997; -. DR OMA; RQKNDGE; -. DR OrthoDB; 1893660at2; -. DR BioCyc; GCF_000015005:MSMEG_4756-MONOMER; -. DR BioCyc; MSME246196:G1H7P-4729-MONOMER; -. DR EvolutionaryTrace; A0R1H6; -. DR Proteomes; UP000000757; Chromosome. DR Proteomes; UP000006158; 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 INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:18955433" FT CHAIN 2..130 FT /note="Holo-[acyl-carrier-protein] synthase" FT /id="PRO_1000008454" FT METAL 9 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101" FT METAL 58 FT /note="Magnesium" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101" FT STRAND 3..12 FT /evidence="ECO:0000244|PDB:3GWM" FT HELIX 13..20 FT /evidence="ECO:0000244|PDB:3GWM" FT HELIX 25..28 FT /evidence="ECO:0000244|PDB:3GWM" FT HELIX 33..39 FT /evidence="ECO:0000244|PDB:3GWM" FT HELIX 45..65 FT /evidence="ECO:0000244|PDB:3GWM" FT STRAND 72..74 FT /evidence="ECO:0000244|PDB:3GWM" FT HELIX 79..82 FT /evidence="ECO:0000244|PDB:3GWM" FT STRAND 83..87 FT /evidence="ECO:0000244|PDB:3GWM" FT STRAND 93..97 FT /evidence="ECO:0000244|PDB:3GWM" FT HELIX 99..104 FT /evidence="ECO:0000244|PDB:3GWM" FT TURN 105..107 FT /evidence="ECO:0000244|PDB:3GWM" FT STRAND 109..117 FT /evidence="ECO:0000244|PDB:3GWM" FT STRAND 120..128 FT /evidence="ECO:0000244|PDB:3GWM" SQ SEQUENCE 130 AA; 14165 MW; 574FE43BAA348A94 CRC64; MAIVGVGIDL VSIPDFAEQV DRPGTVFAET FTPGERRDAA DKSSSAARHL AARWAAKEAV IKAWSSSRFS KRPALPEGIH RDIEVVTDMW GRPKVRLSGE IAKHLEDVTI HVSLTHEDQT AAAVAIIEEP //