ID   PKSC_BACSU              Reviewed;         288 AA.
AC   O34825;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Polyketide biosynthesis malonyl CoA-acyl carrier protein transacylase PksC;
DE            Short=AT;
DE            EC=2.3.1.39;
GN   Name=pksC; OrderedLocusNames=BSU17100;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16757561; DOI=10.1073/pnas.0603148103;
RA   Calderone C.T., Kowtoniuk W.E., Kelleher N.L., Walsh C.T., Dorrestein P.C.;
RT   "Convergence of isoprene and polyketide biosynthetic machinery: isoprenyl-
RT   S-carrier proteins in the pksX pathway of Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:8977-8982(2006).
RN   [3]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=17190806; DOI=10.1073/pnas.0609073103;
RA   Straight P.D., Fischbach M.A., Walsh C.T., Rudner D.Z., Kolter R.;
RT   "A singular enzymatic megacomplex from Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:305-310(2007).
RN   [4]
RP   FUNCTION IN BACILLAENE BIOSYNTHESIS.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
RC   NCIMB 3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=17234808; DOI=10.1073/pnas.0610503104;
RA   Butcher R.A., Schroeder F.C., Fischbach M.A., Straight P.D., Kolter R.,
RA   Walsh C.T., Clardy J.;
RT   "The identification of bacillaene, the product of the PksX megacomplex in
RT   Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1506-1509(2007).
CC   -!- FUNCTION: Involved in some intermediate steps for the synthesis of the
CC       antibiotic polyketide bacillaene which is involved in secondary
CC       metabolism. It catalyzes the transfer of the malonyl-CoA group to the
CC       acyl-carrier-protein AcpK (Mal-AcpK). {ECO:0000269|PubMed:16757561,
CC       ECO:0000269|PubMed:17234808}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC         Evidence={ECO:0000269|PubMed:16757561};
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17190806}.
CC   -!- SIMILARITY: Belongs to the FabD family. {ECO:0000305}.
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; AL009126; CAB13582.1; -; Genomic_DNA.
DR   PIR; A69678; A69678.
DR   RefSeq; NP_389591.1; NC_000964.3.
DR   RefSeq; WP_003231821.1; NZ_JNCM01000035.1.
DR   PDB; 5DZ6; X-ray; 1.44 A; A=1-288.
DR   PDBsum; 5DZ6; -.
DR   AlphaFoldDB; O34825; -.
DR   SMR; O34825; -.
DR   STRING; 224308.BSU17100; -.
DR   PaxDb; 224308-BSU17100; -.
DR   EnsemblBacteria; CAB13582; CAB13582; BSU_17100.
DR   GeneID; 939504; -.
DR   KEGG; bsu:BSU17100; -.
DR   PATRIC; fig|224308.179.peg.1853; -.
DR   eggNOG; COG0331; Bacteria.
DR   InParanoid; O34825; -.
DR   OrthoDB; 9805460at2; -.
DR   PhylomeDB; O34825; -.
DR   BioCyc; BSUB:BSU17100-MONOMER; -.
DR   UniPathway; UPA01003; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IBA:GO_Central.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR024925; Malonyl_CoA-ACP_transAc.
DR   InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   NCBIfam; TIGR00128; fabD; 1.
DR   PANTHER; PTHR42681; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42681:SF1; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   PIRSF; PIRSF000446; Mct; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Antibiotic biosynthesis; Cytoplasm;
KW   Reference proteome; Transferase.
FT   CHAIN           1..288
FT                   /note="Polyketide biosynthesis malonyl CoA-acyl carrier
FT                   protein transacylase PksC"
FT                   /id="PRO_0000388004"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000250"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   TURN            14..19
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           20..23
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           25..35
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           39..45
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           47..52
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           54..76
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           89..96
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           102..117
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   STRAND          121..129
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           132..141
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   STRAND          147..154
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   STRAND          157..163
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           164..175
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   STRAND          182..185
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           198..208
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   TURN            223..225
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           231..233
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           234..240
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           241..243
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           248..256
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   STRAND          262..265
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   STRAND          267..270
FT                   /evidence="ECO:0007829|PDB:5DZ6"
FT   HELIX           271..284
FT                   /evidence="ECO:0007829|PDB:5DZ6"
SQ   SEQUENCE   288 AA;  32464 MW;  AFAE397EAB2FD3C6 CRC64;
     MITYVFPGQG SQKQGMGSGL FDEFKELTDQ ADEILGYSIK RLCLENPYSN LNKTQFTQPA
     LYVVNALSYL KKIRDEEVKP DFVAGHSLGE YNALFAAEAF DFETGLQLVR KRGELMSLIS
     NGGMAAVMGL NEEQVAKALK EYHLHDVDIA NVNAPYQIVI SGKKDEIEKA ASLFETMTEV
     TMVLPLNVSG AFHSRYMNKA KEEFEEFLHA FYFSPPSIPV ISNVYAKPYT YEFMKQTLAD
     QINHSVKWTD SISYLMKKGH MEFEEVGPGN VLTGLIHRIK KDAEAMPR
//