ACPS_MYCS2
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 03-AUG-2022, entry version 98.
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}.
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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 AlphaFoldDB; A0R1H6; -.
DR SMR; A0R1H6; -.
DR STRING; 246196.MSMEI_4636; -.
DR EnsemblBacteria; ABK75003; ABK75003; MSMEG_4756.
DR EnsemblBacteria; AFP41085; AFP41085; MSMEI_4636.
DR GeneID; 66736069; -.
DR KEGG; msg:MSMEI_4636; -.
DR KEGG; msm:MSMEG_4756; -.
DR PATRIC; fig|246196.19.peg.4641; -.
DR eggNOG; COG0736; Bacteria.
DR OMA; NTCGLGH; -.
DR OrthoDB; 1893660at2; -.
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 BINDING 9
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 3..12
FT /evidence="ECO:0007829|PDB:3GWM"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:3GWM"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:3GWM"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:3GWM"
FT HELIX 45..65
FT /evidence="ECO:0007829|PDB:3GWM"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3GWM"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:3GWM"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:3GWM"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:3GWM"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:3GWM"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3GWM"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:3GWM"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:3GWM"
SQ SEQUENCE 130 AA; 14165 MW; 574FE43BAA348A94 CRC64;
MAIVGVGIDL VSIPDFAEQV DRPGTVFAET FTPGERRDAA DKSSSAARHL AARWAAKEAV
IKAWSSSRFS KRPALPEGIH RDIEVVTDMW GRPKVRLSGE IAKHLEDVTI HVSLTHEDQT
AAAVAIIEEP
