ACPS_HELPY
ID ACPS_HELPY Reviewed; 119 AA.
AC O25488;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=HP_0808;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07855.1; -; Genomic_DNA.
DR PIR; H64620; H64620.
DR RefSeq; NP_207601.1; NC_000915.1.
DR RefSeq; WP_000579175.1; NC_018939.1.
DR PDB; 5XUK; X-ray; 2.30 A; A=1-119.
DR PDBsum; 5XUK; -.
DR AlphaFoldDB; O25488; -.
DR SMR; O25488; -.
DR IntAct; O25488; 12.
DR STRING; 85962.C694_04140; -.
DR PaxDb; O25488; -.
DR EnsemblBacteria; AAD07855; AAD07855; HP_0808.
DR KEGG; hpy:HP_0808; -.
DR PATRIC; fig|85962.47.peg.860; -.
DR eggNOG; COG0736; Bacteria.
DR OMA; SHDAGFA; -.
DR PhylomeDB; O25488; -.
DR Proteomes; UP000000429; 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 CHAIN 1..119
FT /note="Holo-[acyl-carrier-protein] synthase"
FT /id="PRO_0000175653"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:5XUK"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:5XUK"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:5XUK"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:5XUK"
FT HELIX 40..56
FT /evidence="ECO:0007829|PDB:5XUK"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:5XUK"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5XUK"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:5XUK"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:5XUK"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:5XUK"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:5XUK"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:5XUK"
SQ SEQUENCE 119 AA; 13004 MW; F6763F8C8554883C CRC64;
MIGIDIVSIA RIEKCVKRFK MKFLERFLSP SEIVLCKDKS SSIAGFFALK EACSKALQVG
IGKELSFLDI KISKSPKNAP LITLSKEKMD YFNIQSLSAS ISHDAGFAIA VVVVSSSNE
