ID   PKSE_BACSU              Reviewed;         767 AA.
AC   O34787;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Polyketide biosynthesis protein PksE;
DE   Includes:
DE     RecName: Full=Malonyl CoA-acyl carrier protein transacylase;
DE              Short=MCT;
DE              EC=2.3.1.39;
GN   Name=pksE; OrderedLocusNames=BSU17120;
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   SEQUENCE REVISION TO 99-129.
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   [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: Probably involved in some intermediate steps for the
CC       synthesis of the antibiotic polyketide bacillaene which is involved in
CC       secondary metabolism. Probably has an acyl transferase activity and
CC       could also have a flavin mononucleotide-dependent oxidoreductase
CC       activity. {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   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17190806}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the FabD family.
CC       {ECO:0000305}.
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DR   EMBL; AL009126; CAB13584.3; -; Genomic_DNA.
DR   RefSeq; NP_389593.3; NC_000964.3.
DR   RefSeq; WP_003231811.1; NZ_JNCM01000035.1.
DR   PDB; 5DZ7; X-ray; 2.50 A; A=1-288.
DR   PDBsum; 5DZ7; -.
DR   AlphaFoldDB; O34787; -.
DR   SMR; O34787; -.
DR   STRING; 224308.BSU17120; -.
DR   PaxDb; 224308-BSU17120; -.
DR   EnsemblBacteria; CAB13584; CAB13584; BSU_17120.
DR   GeneID; 939997; -.
DR   KEGG; bsu:BSU17120; -.
DR   PATRIC; fig|224308.179.peg.1857; -.
DR   eggNOG; COG0331; Bacteria.
DR   eggNOG; COG2070; Bacteria.
DR   InParanoid; O34787; -.
DR   OrthoDB; 9805460at2; -.
DR   PhylomeDB; O34787; -.
DR   BioCyc; BSUB:BSU17120-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:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
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; cd04742; NPD_FabD; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
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; IPR013785; Aldolase_TIM.
DR   InterPro; IPR049489; FabD-like_helical_ins.
DR   InterPro; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR004136; NMO.
DR   InterPro; IPR014179; PfaD-like_TIM-barrel.
DR   NCBIfam; TIGR00128; fabD; 1.
DR   NCBIfam; TIGR02814; pfaD_fam; 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   Pfam; PF21607; FabD_helical_ins; 1.
DR   Pfam; PF03060; NMO; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 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..767
FT                   /note="Polyketide biosynthesis protein PksE"
FT                   /id="PRO_0000388002"
FT   REGION          1..312
FT                   /note="Acyl transferase"
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:5DZ7"
FT   TURN            14..21
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           25..35
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           39..44
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           54..76
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           90..96
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           102..118
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   STRAND          121..130
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           132..141
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   STRAND          148..154
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   STRAND          157..163
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           164..174
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   STRAND          182..185
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           198..209
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   TURN            223..225
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           234..239
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           248..257
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   STRAND          262..265
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   STRAND          267..270
FT                   /evidence="ECO:0007829|PDB:5DZ7"
FT   HELIX           271..280
FT                   /evidence="ECO:0007829|PDB:5DZ7"
SQ   SEQUENCE   767 AA;  85743 MW;  C97C8825E3DE8881 CRC64;
     MITYVFPGQG SQQKGMGQGL FEQYQHLTDQ ADQILGYSIE KLCTEKSYLD VNHTEYTQPA
     LYVVNALSYL KRVEETGRKP DFAAGHSLGE YNALMAAGAF DFETGLRLVK KRGELMGRIT
     GGGMAAVIGL SKEQVTAVLE EHRLYDIDVA NENTPQQIVI SGPKKEIEKA RAVFENTKDV
     KLFHPLNVSG AFHSRYMNEA KQVFKQYIDS FQFAPLAIPV ISNVYAEPYH QDRLKDTLSE
     QMDNTVKWTD SIRFLMGRGE MEFAEIGPGT VLTGLIHRIK NEAEPLTYIP KKNPAISAHL
     KEQRNVQAGI TAESLGSAEF KQDYHLTYAY LAGGMYRGIA SKEMVVKLSR AGMMGFFGTG
     GLSLKEVEDA IHAIQGELGK GQAYGINLVH NMKHTESEEK MIDLLLRNQV SIVEASAFLS
     VTPVLVRYRA KGVKRNQNGD VICSNRLIAK ISRPEVAESF LSPAPENMLQ KLLGENKITM
     NEAELLRCIP MADDICVEAD SGGHTDGGVA YSLMPAMTSL RDEMMKKYQY RKKIRVGAAG
     GIGTPEAAMA AFMLGADFIL TGSINQCTVE AATSDKVKDL LQQMNVQDTA YAPAGDMFES
     GSKVQVLKKG VFFPARANKL YELYQRYGSI RELDAKMLAQ LEEKYFKRSI EDIYKDIALH
     YPAADIEKAE QNPKHKMALI FRWYFRYSSK LAISGSEHSK VDYQIHCGPA LGAFNQWVKG
     SQLENWRNRH VDEIGKKLMT ETAVLLHERM QSMYQPSHET DNIKIKV
//