ID ACPS_MYCS2 Reviewed; 130 AA. AC A0R1H6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 11-JUL-2012, entry version 47. DE RecName: Full=Holo-[acyl-carrier-protein] synthase; DE Short=Holo-ACP synthase; DE EC=2.7.8.7; DE AltName: Full=4'-phosphopantetheinyl transferase AcpS; GN Name=acpS; OrderedLocusNames=MSMEG_4756; OS Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND RP CLEAVAGE OF INITIATOR METHIONINE. 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 RT orthology and a new MS-based protocol."; RL Genome Res. 19:128-135(2009). CC -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme CC A to a Ser of acyl-carrier-protein (By similarity). CC -!- CATALYTIC ACTIVITY: CoA-(4'-phosphopantetheine) + apo-[acyl- CC carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl- CC carrier-protein]. CC -!- COFACTOR: Magnesium (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS CC family. 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 RefSeq; YP_889014.1; NC_008596.1. DR PDB; 3GWM; X-ray; 1.70 A; A=2-130. DR PDBsum; 3GWM; -. DR ProteinModelPortal; A0R1H6; -. DR STRING; A0R1H6; -. DR EnsemblBacteria; EBMYCT00000046152; EBMYCP00000044489; EBMYCG00000046147. DR GeneID; 4536674; -. DR GenomeReviews; CP000480_GR; MSMEG_4756. DR KEGG; msm:MSMEG_4756; -. DR PATRIC; 18081815; VBIMycSme59918_4641. DR eggNOG; COG0736; -. DR HOGENOM; HOG000014315; -. DR KO; K00997; -. DR OMA; THDGDTA; -. DR ProtClustDB; PRK00070; -. DR BioCyc; MSME246196:MSMEG_4756-MONOMER; -. DR EvolutionaryTrace; A0R1H6; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009059; P:macromolecule biosynthetic process; IEA:InterPro. DR Gene3D; G3DSA:3.90.470.20; G3DSA:3.90.470.20; 1. DR HAMAP; MF_00101; AcpS; 1; -. DR InterPro; IPR008278; 4-PPantetheinyl_Trfase. DR InterPro; IPR002582; ACPS. DR InterPro; IPR004568; PPantethiene-prot_Trfase. DR Pfam; PF01648; ACPS; 1. DR ProDom; PD004282; PPantethiene-prot_Trfase; 1. DR SUPFAM; SSF56214; 4-PPT_transf; 1. DR TIGRFAMs; TIGR00516; AcpS; 1. DR TIGRFAMs; TIGR00556; Pantethn_trn; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Lipid synthesis; Magnesium; Metal-binding; Reference proteome; KW Transferase. FT INIT_MET 1 1 Removed. FT CHAIN 2 130 Holo-[acyl-carrier-protein] synthase. FT /FTId=PRO_1000008454. FT METAL 9 9 Magnesium (By similarity). FT METAL 58 58 Magnesium (By similarity). FT STRAND 3 12 FT HELIX 13 20 FT HELIX 25 28 FT HELIX 33 39 FT HELIX 45 65 FT STRAND 72 74 FT HELIX 79 82 FT STRAND 83 87 FT STRAND 93 97 FT HELIX 99 104 FT TURN 105 107 FT STRAND 109 117 FT STRAND 120 128 SQ SEQUENCE 130 AA; 14165 MW; 574FE43BAA348A94 CRC64; MAIVGVGIDL VSIPDFAEQV DRPGTVFAET FTPGERRDAA DKSSSAARHL AARWAAKEAV IKAWSSSRFS KRPALPEGIH RDIEVVTDMW GRPKVRLSGE IAKHLEDVTI HVSLTHEDQT AAAVAIIEEP //