ID   A0A1Y0ISX8_9BACL        Unreviewed;      1502 AA.
AC   A0A1Y0ISX8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ARU63631.1};
GN   ORFNames=CBW65_23395 {ECO:0000313|EMBL:ARU63631.1};
OS   Tumebacillus avium.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1903704 {ECO:0000313|EMBL:ARU63631.1, ECO:0000313|Proteomes:UP000195437};
RN   [1] {ECO:0000313|Proteomes:UP000195437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR23208 {ECO:0000313|Proteomes:UP000195437};
RA   Sung H.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004789}.
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DR   EMBL; CP021434; ARU63631.1; -; Genomic_DNA.
DR   KEGG; tum:CBW65_23395; -.
DR   OrthoDB; 9765680at2; -.
DR   Proteomes; UP000195437; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
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; 3.40.50.1820; alpha/beta hydrolase; 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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR049490; C883_1060-like_KR_N.
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; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF21394; Beta-ketacyl_N; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..436
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1393..1468
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1502 AA;  162102 MW;  DADE743284B07699 CRC64;
     MSHEKENQLL EGIAIVGMSG RFPGSKNIAE FWAHLQNGDE TITEFTEEEL KAAGVDSDLL
     QDPQYVKRGG LLQDRDMFDA NFFDYTAKEA EVTDPSHRLF LETAWEALET AGYDAEQYPG
     RIGVYGGVGQ NSFSYHLYSN QGLFGQIGAL QATLATSYDF LATRVAYKLN LTGPALTVQT
     ACSTSLVAVH QACQQLLMHE CDMALAGGVA IKLLEAEGYL YQEGSILSPD GHCRAFDERA
     QGTIGGDGVG VVVLKRLEDA LEDGDQIYAV IRGSAVNNDG AGKIGFTAPS VDGQAQVILD
     ALAVAGVDAD TISYIETHGT GTPLGDPIEI SALTNAYRDS TDRVGYCALG SLKTNMGHLD
     AAAGVTGLIK AALMLKHGQL VPSLHFEKAN PKLGLDSSPF YVNTELKEWA AGESPRRAGV
     SSFGMGGTNA HVVLEEAPVL DSSSESSRKW KLLVLSAKTG TALNAATENL AAHLQANPQG
     DLADVAFTLQ TGRRAFDHRR VVAVESHEDA VAALEAMDGK RVVTGESQTR DRSVVFLFPG
     QGAQYVNMGL ELYREEPVFR EQIDFCADAL RSAIGVDLRE VLYPAADKAE EASELLRQTY
     ITQPALFVIE YALAKLWMEL GVQPDAMLGH SIGEYVAAVL AGVMSLEDAL KLVAVRGKLM
     QSLPAGTMLA VPLAEADVLP LLGEGLSLAA VNGPQACVVA GTFAAMEVLE QKLQAQEVEC
     RRLVTSHAFH SAMMDPILEQ FTEAVRSVEL HAPQMPYLSN VSGTWITAAE ATDPAYWAKH
     LRGTVRFAAN VRELLQEPGR LFLEVGPGRS LIGLTRQQVA QEGAQEVLLS SLRHRDEQVS
     DAAFLLTALG KLWLSGLKID WTLLYAGEMR HRLALPTYPF ERKRYWLERK HSTVAKLQRK
     KADVADWFYV PTWKKSLLIA DPATDAQNWL LFLDETGVGA KLAERLTSAG HRVVTVAAGA
     DFAKTEAGAY TVRPADREDY SKLLDELAAA ELLPHKIAHL FGVIAEAGEY EQLQGKGFYS
     LLALSQALGE QTLAHGVQLG VITNNLQDVL ADTVTAPARA TALGLCKVIP QELTGVTTCA
     IDIDGGTDVD QLIAEFSADA SDSVIAYRRN LRFTQTFEAA RLPKRSATLR DNPVVLITGA
     SAPNAQSVAS FLASTTNAKL VLVTHDAEAA SLTGGEDDGH LYFTADITDL GQMQAIVQQA
     TARFGEITGV VHAEDPRGTG MLQLKTQEMT SAVLDPKVKG ALVLEQALAD AKLDFFLLYN
     STVAATGGFG QSDNCAAGAF LDAFAASRAN THSVSWGIWK WDDWQEQQLA GVAELHQQLR
     EARETFGITD GEGIEALNRM LSFGLPQTVV STQDFHDVLQ ASQSFTAAGF LEALEESRQA
     ALAGAQSNSN YVAPRTDLEA TIAGFWAELF GVQQPSVQAD FFDLGGNSLV AIQLVTRMRK
     QFGMDFPINT IFESPTIEAL AQMVENNQLG QEKLDALDEL LKQIEGMSDD DLLAKMLEEE
     TK
//