ID   ACPS_NEIMF              Reviewed;         125 AA.
AC   A1KVH5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=NMC1700;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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; AM421808; CAM10879.1; -; Genomic_DNA.
DR   RefSeq; WP_002212541.1; NC_008767.1.
DR   PDB; 5CMO; X-ray; 2.00 A; A/B/C=1-125.
DR   PDB; 5SUV; X-ray; 1.75 A; A/B/C=1-125.
DR   PDBsum; 5CMO; -.
DR   PDBsum; 5SUV; -.
DR   AlphaFoldDB; A1KVH5; -.
DR   SMR; A1KVH5; -.
DR   EnsemblBacteria; CAM10879; CAM10879; NMC1700.
DR   KEGG; nmc:NMC1700; -.
DR   HOGENOM; CLU_089696_3_1_4; -.
DR   OMA; DERHYAV; -.
DR   OrthoDB; 1893660at2; -.
DR   Proteomes; UP000002286; 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   Transferase.
FT   CHAIN           1..125
FT                   /note="Holo-[acyl-carrier-protein] synthase"
FT                   /id="PRO_1000008461"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT   STRAND          2..11
FT                   /evidence="ECO:0007829|PDB:5SUV"
FT   HELIX           12..22
FT                   /evidence="ECO:0007829|PDB:5SUV"
FT   HELIX           25..30
FT                   /evidence="ECO:0007829|PDB:5SUV"
FT   HELIX           33..38
FT                   /evidence="ECO:0007829|PDB:5SUV"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:5SUV"
FT   HELIX           45..62
FT                   /evidence="ECO:0007829|PDB:5SUV"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:5SUV"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:5SUV"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:5SUV"
FT   HELIX           92..101
FT                   /evidence="ECO:0007829|PDB:5SUV"
FT   STRAND          105..113
FT                   /evidence="ECO:0007829|PDB:5SUV"
FT   STRAND          116..124
FT                   /evidence="ECO:0007829|PDB:5SUV"
SQ   SEQUENCE   125 AA;  13677 MW;  64AD823F8529EC6A CRC64;
     MIYGIGTDIV SLKRIIRLNK KFGQAFAGRI LTPEELLEFP QAGKPVNYLA KRFAAKEAFA
     KAVGTGIRGA VSFRNIGIGH DALGKPEFFY GPALSKWLEE QGISRVSLSM SDEEDTVLAF
     VVAEK