ACPS_STAAM
ID ACPS_STAAM Reviewed; 119 AA.
AC P63468; Q99SI4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, 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}; Synonyms=dpj;
GN OrderedLocusNames=SAV2071;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB58233.1; -; Genomic_DNA.
DR RefSeq; WP_000581197.1; NC_002758.2.
DR AlphaFoldDB; P63468; -.
DR SMR; P63468; -.
DR World-2DPAGE; 0002:P63468; -.
DR PaxDb; P63468; -.
DR EnsemblBacteria; BAB58233; BAB58233; SAV2071.
DR KEGG; sav:SAV2071; -.
DR HOGENOM; CLU_089696_1_2_9; -.
DR OMA; DERHYAV; -.
DR PhylomeDB; P63468; -.
DR BioCyc; SAUR158878:SAV_RS11335-MON; -.
DR Proteomes; UP000002481; 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 Transferase.
FT CHAIN 1..119
FT /note="Holo-[acyl-carrier-protein] synthase"
FT /id="PRO_0000175701"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
SQ SEQUENCE 119 AA; 13634 MW; E2EF3C5A696E7DD2 CRC64;
MIHGIGVDLI EIDRIKVLYS KQPKLVERIL TKNEQHKFNN FTHEQRKIEF LAGRFATKEA
FSKALGTGLG KHVAFNDIDC YNDELGKPKI DYEGFIVHVS ISHTEHYAMS QVVLEKSAF
