ID   THAQ_BURTA              Reviewed;        2082 AA.
AC   Q2T4P1;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Polyketide synthase ThaQ {ECO:0000305};
GN   Name=thaQ {ECO:0000303|PubMed:20853892}; OrderedLocusNames=BTH_II1664;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
RN   [2]
RP   NOMENCLATURE.
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=20853892; DOI=10.1021/ja105003g;
RA   Ishida K., Lincke T., Behnken S., Hertweck C.;
RT   "Induced biosynthesis of cryptic polyketide metabolites in a Burkholderia
RT   thailandensis quorum sensing mutant.";
RL   J. Am. Chem. Soc. 132:13966-13968(2010).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=29914944; DOI=10.1128/aac.00463-18;
RA   Wozniak C.E., Lin Z., Schmidt E.W., Hughes K.T., Liou T.G.;
RT   "Thailandamide, a Fatty Acid Synthesis Antibiotic That Is Coexpressed with
RT   a Resistant Target Gene.";
RL   Antimicrob. Agents Chemother. 62:0-0(2018).
CC   -!- FUNCTION: Involved in production of the polyketide antibiotic
CC       thailandamide. {ECO:0000305|PubMed:29914944}.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00258};
CC       Note=Binds 2 phosphopantetheines covalently. {ECO:0000255|PROSITE-
CC       ProRule:PRU00258};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:20853892}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: No longer inhibits growth of Salmonella in an
CC       overlay assay, suggesting it does not produce thailandamide.
CC       {ECO:0000269|PubMed:29914944}.
CC   -!- MISCELLANEOUS: Thailandamide is a polyketide that is toxic to human
CC       cell lines but also has antibacterial activity on E.coli, S.typhimurium
CC       and S.aureus. It probably acts on acetyl-CoA carboxylase in the fatty
CC       acid synthesis pathway, which is rarely found to be an antibiotic
CC       target. These data suggest it might be a good starting point for
CC       engineering of novel antibiotics. {ECO:0000305|PubMed:29914944}.
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DR   EMBL; CP000085; ABC34599.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2T4P1; -.
DR   SMR; Q2T4P1; -.
DR   ESTHER; burta-q2t4p1; 6_AlphaBeta_hydrolase.
DR   MEROPS; S33.010; -.
DR   PRIDE; Q2T4P1; -.
DR   EnsemblBacteria; ABC34599; ABC34599; BTH_II1664.
DR   KEGG; bte:BTH_II1664; -.
DR   HOGENOM; CLU_001565_0_0_4; -.
DR   OrthoDB; 1282004at2; -.
DR   Proteomes; UP000001930; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1200.10; -; 2.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 2.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020803; PKS_MeTfrase.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00828; PKS_MT; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF47336; SSF47336; 2.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   PROSITE; PS50075; CARRIER; 2.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Cytoplasm; Multifunctional enzyme;
KW   Phosphopantetheine; Phosphoprotein; Repeat; Transferase.
FT   CHAIN           1..2082
FT                   /note="Polyketide synthase ThaQ"
FT                   /id="PRO_0000452506"
FT   DOMAIN          470..546
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1669..1743
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1792..2022
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   REGION          398..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1250..1269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1603..1653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2045..2082
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..628
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2067..2082
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         507
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1703
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2082 AA;  220448 MW;  F4B548593FFDF72E CRC64;
     MRRAMRDGGK PDRIGAAAPL RRAPLTATSG IDMNVQESIF PITPNGFAGH SMDDLMQRWL
     LAQLQATGIL ADGRAHAFDA LAGRVQPLYR RWLEESLRLL RDAGLVRDDA QGWRAAERAP
     IDARDAQRHW DASRDAWLAD RERAVYVVLI EAVLAQLPAI LTGRRRATDV LFPNGSMARV
     QGVYTGNHVS DHFNRVLVDH AVRYVAGCAA RRADAKLRFI EVGAGTGGTT EGLLAALAPH
     ARHVGEYCFT DISKAFLNHA QRRFGEGAPF FGARVLDIEQ PIDAQGFEPG AYDALVATNV
     LHATRDIRTT LRHCKALLKH NGLLFINEMT GSVPYLHLTF GMLEGWWRFT DDALRVAGCP
     AVAPQTWDRV LREEGFSSVI FPARDAHGQG QQIVIAQNDA RRAGSARRDA RASNGDAQHG
     ARHEAAHDAQ QDASGDTQAD AHDSAHDSAH DSAHDSAHDS AHDSAHAAAA LRREGRAYLR
     ARAAELLGMP AGAIDPDEGL HAYGLDSILA SQFAAQLAEA FDGFDGALLF EHKTINALLD
     HLLAAHADAL ARLLPPAGGA PARGVGARAQ AAQASGEGRA APPAAPHADA RSDTPSSAPS
     SAPARPDQPA PSGPPAQPAQ PAPRADTPPP AASAGHRGEA RASDTRYAPR APHPDAAAEP
     VAIIGISGRY PGAYDVPAFW RNLLAGACAI TEVPAERWDW RAHYRADAAE AAREGKSYSK
     WGGFVDDVGR FDPAFFGMTP QDAQHTDPQE LLFLEMCWHA LQDAGQTPAL LPGDVRRRAG
     VFAAITKHYA FPPTSFASLA NRVSHALDFG GKSLAIDTMC SSSLVAVNEA WEYLQRDGRL
     AVVGGVNLYL DPQQYAHLSR FRFASSGPVC KAFGEGGDGF VPGEGAGAIV LKRLSDAERD
     GDPIHAVIRG CAVNHNGRST SFTASDPARQ ADVVRDALTR AGVDPRTIGY VEAAANGHAM
     GDAIEMTGLG KVFAACDGVS GTRAIGSVKA NIGHCEAASG MSQLTKVVMA MRDGVLAPTL
     RDGTRNPNIA FERLPFEVQE QAAPWRRLIV DGSEVPRRAG VTSIGGGGVN AHVVLEEYVA
     PPRAARPGAG TDDEVLFVLS ARTREQLGAY AERWAGYLEA HPDCDVDAIA HTVRTAREPM
     AHRLAVLAHG RGELAALLRG WAAGGAASGA ASGAASDQVF YGDVKQHRVV LSDALVQAAR
     REGAASLAKL WVLGNALGAA HGADEPAPRR VGLLPPYPFE RRLVWTSAHA PGTRHASAGE
     ATEAAEAAEA AEAGAAAVAE SAEAGAPAAA GDARLQPAPA SNAEAFYSLS TLNASKDFQE
     QYLTLCPFPE RIPGFSMTRM FIEPQKYPNE FALMQARQIE MRQVLFGREH FERISRVLDI
     GCGMGTDVIQ LAKRFAHLRT TGYTITRAQA ELGAGRIARE GLQGRAEIRH GDSAKDPFPG
     KYDLVIGIEV ICHIQDKHGV FGNIARSLDD DGHVLLMDFV ANGRGRISSP EIDIDIGTRQ
     DWIDVAAAHG LVVDEVIDVS PQIANFLHDP EHERNIAALP GVAQASFRNF ANTCVSLEKG
     WVSYCLLRLS KASRLSEAER RRLNAERFGA SVAYPDALKA MHARGPAPYP RSPDAQPPAA
     RAQAGVDGGV EASAPAGVKA DSKAGPKSEV KSDAAARASR ADIAASVAAS VAASVEDAFE
     ASLGLRRADL ERADDLRALG IGSIQAVMLA EAINERLDLA LPSRFVLEHA TFGALVRAVA
     EAVAGGRGSS RDAPARELAY LSLLEPGGAM TAELLELPGG ARAEILRGGR GPRVVLIPGL
     GMAGTVFRDL CRALTRRHEV IVYHYPGLGR SDPVAPIDVD AAAAHLYRTL DACGGDGAAA
     LLGWSFGGVI AQRAALMRPR AWRALVLVNT LGAYRPLAPQ FLTPGASRDG EPRGLGGLYQ
     TDLDFVFAGD APPAALARKD ACAALMRDSL ALDAAQAIDY LDALVRFDAT AQLPSLRMPT
     LVVAGTADHF GDPAHAEQLV SLIPNARLAR IAGAGHAVFL THGEAFEPAV LAFLDETLRA
     AEAGGAAESV ESVEATEAAE AARSPAVARR RATDDAPVGS DA