ID D7CDZ6_STRBB Unreviewed; 1649 AA.
AC D7CDZ6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Putative type I polyketide synthase {ECO:0000313|EMBL:ADI04661.1};
GN OrderedLocusNames=SBI_01540 {ECO:0000313|EMBL:ADI04661.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI04661.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI04661.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI04661.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CP002047; ADI04661.1; -; Genomic_DNA.
DR RefSeq; WP_014174140.1; NC_016582.1.
DR STRING; 749414.SBI_01540; -.
DR KEGG; sbh:SBI_01540; -.
DR PATRIC; fig|749414.3.peg.1585; -.
DR eggNOG; COG1309; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_7_11; -.
DR Proteomes; UP000000377; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.11460; -; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 1.10.357.10; Tetracycline Repressor, domain 2; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001647; HTH_TetR.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08990; Docking; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF00440; TetR_N; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50977; HTH_TETR_2; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00335};
KW Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT DOMAIN 33..458
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1454..1514
FT /note="HTH tetR-type"
FT /evidence="ECO:0000259|PROSITE:PS50977"
FT DNA_BIND 1477..1496
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00335"
SQ SEQUENCE 1649 AA; 173068 MW; 5FDE70AD66B19CA5 CRC64;
MANEEKLRAY LKRVTGDLHQ ARQHIMELET ANSEPIAIVS MSCRYPGGVN SPEELWQLVA
SGTDAISDFP QNRGWAEDLY DEDPERPGKS YTREGGFLHE SDRFDPAFFG ISPREALTID
PQQRLLLETS WEAFERAGIV PATLRGSHTG VFAGVMYNDY GTRLYGTLDS FEGYLVNGSA
GSVASGRVAY TFGLEGPAVT IDTACSSSLV TLHLAAQALR RGDCSLALAG GVAVMSTPEI
FVEFSRQGAL SPDGRCKSFS DGADGTAWAE GVGMLLLERL SDARRNGHPV LAVVRGSAVN
QDGASNGLTA PNGPSQQRVI RQALASAGLT SSQVDAVEAH GTGTTLGDPI EAQALLATYG
QGRSGGRPLW LGSLKSNIGH AQAAAGVAGV MKMVLAMRYG VLPRTLHVDE PSRQVDWESG
AVELLTEERE WPEGEHPRRA GVSSFGVSGT NAHVILEQAP EVVAESEDSA AVAPVVVPWV
VSGRGVEALR GQAARLLSHV EGGGGLSPMD VGWSLAVGRS VFEHRAVVFG GDGDGLRVGL
DGLARGVDVP GVVVGPVSGM SVAGGRVVLV FPGQGSQWAG MAVELLDSSA VFAERFAECG
EALAEFVDWS LEDVLRGVAG AVSLERVDVV QPVLWAVMVS LAELWRSFGV VPAAVVGHSQ
GEIAAACVVG ALSLRDGARV VALRSRAIAE GLAGLGGMAS VSLAAEEVAE RVAAWGGRLS
VATVNGPASV VVAGEVGALE ELLAGCEAEG VRARRIAVDY ASHSVQVEVI EGRLAEVLAG
VESRSSSVPF YSTVTGGLVD TAELGAGYWY RNLRQTVRFE ETVGAILDGG DAVFIEVSPH
PVLVVGVQET VEARGAEGSV VVGSLRRGEG GLARFVTSVA EAWVHGVAVD WAGVFAGASR
VDLPTYAFQR KRYWLEAPAG AKGDVSGLGL SIAEHPLLGA VADLPDSAGV VFMGRLSLRS
HGWLADHAVG DTVLLPGTGF VELAVRAGDE VGCDVVEELT LETPLVLPEG SGVQLRLTVA
EPDDAGRRTF RVYSRLEDAA FDEAWTCHAT GVLAQGAAQH TGDLTEWPPK GAEALDVDSL
YEDFATAGYG YGPVFQGLRA AWRRGEEIFA EVALAEEQQA EAARFGIHPA LLDAALHGVR
LGAYFGDPDQ VWLPFAWRGV TLRAAGATEL RVALAPAGVG AVSLSVADGT GAAVATAESL
ALRPVDPSQL AGARRNDSLF RIEWQALAES AVGSPEPPAA WVAVGAPEGL AELGLAAPGS
VAYADLDALG AAVDTGSVGL PPAVLVPMPS PSAEMPSAVR QSVHQALALV QKWLADERFA
ASRLVVVTGG AVATEPDEGI RDLAAAPVWG LLRSAQSENP GRFVLLDIDG NALSPETLVS
AVAADEPQVA VRAGRLRVPR LERMVAPMAD AIPSFGGGTV LVSRTNSRTA GTLHRVERVA
IPLGRLRGER ADAARNRELL LRTTREMIAE LGVDKVTMDG LAERSGLGKG TVYRRFGTRA
GIFHAVLDDD ERAFQEHVLS GPAPLGPEAE PVARLIAYGR ARISFLLARI AIARAALDRN
RPVPAGEGSV SQFHIRMLLR QARPGFADLD ALAVQLTAAL EGPILLYLSM PEETDPSRHV
ERLAGSWESL VARICRTNRD NPDHISKSD
//
