ACPS_THEMA
ID ACPS_THEMA Reviewed; 169 AA.
AC Q9WZF6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=TM_0692;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD35774.1; -; Genomic_DNA.
DR PIR; B72345; B72345.
DR RefSeq; NP_228501.1; NC_000853.1.
DR RefSeq; WP_004081065.1; NZ_CP011107.1.
DR PDB; 5XUM; X-ray; 2.10 A; A=1-169.
DR PDBsum; 5XUM; -.
DR AlphaFoldDB; Q9WZF6; -.
DR SMR; Q9WZF6; -.
DR STRING; 243274.THEMA_01205; -.
DR EnsemblBacteria; AAD35774; AAD35774; TM_0692.
DR KEGG; tma:TM0692; -.
DR eggNOG; COG0736; Bacteria.
DR InParanoid; Q9WZF6; -.
DR OMA; DERHYAV; -.
DR OrthoDB; 1581944at2; -.
DR Proteomes; UP000008183; 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..169
FT /note="Holo-[acyl-carrier-protein] synthase"
FT /id="PRO_0000175720"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00101"
FT BINDING 50
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:5XUM"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:5XUM"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:5XUM"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:5XUM"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:5XUM"
FT HELIX 38..56
FT /evidence="ECO:0007829|PDB:5XUM"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5XUM"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:5XUM"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:5XUM"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:5XUM"
FT STRAND 90..108
FT /evidence="ECO:0007829|PDB:5XUM"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:5XUM"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:5XUM"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:5XUM"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:5XUM"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:5XUM"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:5XUM"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5XUM"
SQ SEQUENCE 169 AA; 19291 MW; 5B83A60B76027778 CRC64;
MIVGVGIDVL EVERVPEKFA ERILGESEKR LFLTRKRRRE FIAGRFALKE AFFKALGTGL
NGHSFTDVEF LESNGKPVLC VHKDFGFFNY AHVSLSHDRF AVALVVLEKR KGDIIVEGDE
SFLRKRFEVL ERSVEGWEIE TSLPPFTLKK LLESSGCRLV RYGNILIGE
