ACPS_LIGS1
ID ACPS_LIGS1 Reviewed; 135 AA.
AC Q1WV15;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=LSL_0357;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABD99170.1; -; Genomic_DNA.
DR RefSeq; WP_003704211.1; NC_007929.1.
DR RefSeq; YP_535253.1; NC_007929.1.
DR AlphaFoldDB; Q1WV15; -.
DR SMR; Q1WV15; -.
DR STRING; 362948.LSL_0357; -.
DR EnsemblBacteria; ABD99170; ABD99170; LSL_0357.
DR KEGG; lsl:LSL_0357; -.
DR PATRIC; fig|362948.14.peg.433; -.
DR HOGENOM; CLU_089696_1_2_9; -.
DR OMA; DICCLND; -.
DR Proteomes; UP000006559; 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 3: Inferred from homology;
KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..135
FT /note="Holo-[acyl-carrier-protein] synthase"
FT /id="PRO_1000008442"
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"
SQ SEQUENCE 135 AA; 15534 MW; F3054169644D8524 CRC64;
MIYGNGIDIQ EIRKIQKAQE KRESFAKRIL TVNELAIFEK YKGNRKYEFL AGRFSAKEAF
SKAYGTGIGK KVGFQDIEIL NDNQTGRPEI VKFPGDNKLQ AKISISHSGE YVVTEVILEK
LTWQTKMKKF LIKQK
