PKSF_BACSU
ID PKSF_BACSU Reviewed; 415 AA.
AC P40804;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Polyketide biosynthesis malonyl-ACP decarboxylase PksF;
DE EC=4.1.1.87;
DE AltName: Full=Malonyl acyl-carrier-protein decarboxylase;
GN Name=pksF; OrderedLocusNames=BSU17140;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / PB1424;
RX PubMed=7704258; DOI=10.1099/13500872-141-2-299;
RA Albertini A.M., Caramori T., Scoffone F., Scotti C., Galizzi A.;
RT "Sequence around the 159 degree region of the Bacillus subtilis genome: the
RT pksX locus spans 33.6 kb.";
RL Microbiology 141:299-309(1995).
RN [2]
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 [3]
RP SEQUENCE REVISION TO 168.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 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 [6]
RP FUNCTION IN BACILLAENE BIOSYNTHESIS.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 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 decarboxylates selectively the malonyl group attached on
CC the acyl-carrier-protein AcpK (Mal-AcpK). {ECO:0000269|PubMed:16757561,
CC ECO:0000269|PubMed:17234808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] = acetyl-[ACP] + CO2;
CC Xref=Rhea:RHEA:24460, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9623,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:78446,
CC ChEBI:CHEBI:78449; EC=4.1.1.87;
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 thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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DR EMBL; U11039; AAA85139.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13585.2; -; Genomic_DNA.
DR PIR; D69678; D69678.
DR RefSeq; NP_389594.2; NC_000964.3.
DR RefSeq; WP_003245287.1; NZ_JNCM01000035.1.
DR RefSeq; WP_009967298.1; NZ_CM000487.1.
DR AlphaFoldDB; P40804; -.
DR SMR; P40804; -.
DR STRING; 224308.BSU17140; -.
DR PaxDb; P40804; -.
DR PRIDE; P40804; -.
DR EnsemblBacteria; CAB13585; CAB13585; BSU_17140.
DR GeneID; 939500; -.
DR KEGG; bsu:BSU17140; -.
DR PATRIC; fig|224308.179.peg.1859; -.
DR eggNOG; COG0304; Bacteria.
DR InParanoid; P40804; -.
DR OMA; GLCTEQF; -.
DR PhylomeDB; P40804; -.
DR BioCyc; BSUB:BSU17140-MON; -.
DR UniPathway; UPA01003; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11712; PTHR11712; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Antibiotic biosynthesis; Cytoplasm; Lyase;
KW Reference proteome; Transferase.
FT CHAIN 1..415
FT /note="Polyketide biosynthesis malonyl-ACP decarboxylase
FT PksF"
FT /id="PRO_0000180350"
FT CONFLICT 168
FT /note="Q -> QQ (in Ref. 1; AAA85139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 45009 MW; F7956D94DCEF7740 CRC64;
MTKCNLPEVV VTGVGVTASI GQGKEDFASS LLSGRHAFDV MKRSGRQKDS RFIGAEIASL
SYPDRLSKKM LRKASFSSRA ALVTLTEAWE EAELDDADSS RIGLVVGGSN FQQRENFEVY
ERYQDRSGFI SPAYGLSFMD SDLCGICTDQ FGITGLAYTV GGASASGQLA VIHAIQQVLS
GEVDTCIALG ALMDLSYMEC EALRALGAMG TDKYADEPEN ACRPFDQNRD GFIYGESCGA
LVIERKETAL RRGLKPYAAL SGWSIKLDGN RNPDPSLEGE IHVIQKALER ARLLPEDIDY
INPHGTGSFI GDEIELKALR ACRLSHAYIN ATKSITGHGL SAAGIVEIIS VLLQMKKSAL
HPSRNLDHPI DDSFHWVNEK SISYRIKNAL SLSMGFGGMN TAVCIQNIEK CGGES
