PKSE_BACSU
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 03-AUG-2022, entry version 125.
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; Firmicutes; 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 / 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 [4]
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: 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; O34787; -.
DR PRIDE; O34787; -.
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 OMA; SIRFLMG; -.
DR PhylomeDB; O34787; -.
DR BioCyc; BSUB:BSU17120-MON; -.
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; -; 1.
DR Gene3D; 3.40.366.10; -; 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; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR004136; NMO.
DR InterPro; IPR014179; PfaD_fam.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF03060; NMO; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR00128; fabD; 1.
DR TIGRFAMs; TIGR02814; pfaD_fam; 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
