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Database: UniProt
Entry: A7GTF8_BACCN
LinkDB: A7GTF8_BACCN
Original site: A7GTF8_BACCN 
ID   A7GTF8_BACCN            Unreviewed;      3099 AA.
AC   A7GTF8;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ABS23416.1};
GN   OrderedLocusNames=Bcer98_3193 {ECO:0000313|EMBL:ABS23416.1};
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS23416.1, ECO:0000313|Proteomes:UP000002300};
RN   [1] {ECO:0000313|EMBL:ABS23416.1, ECO:0000313|Proteomes:UP000002300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC   {ECO:0000313|Proteomes:UP000002300};
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004789}.
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DR   EMBL; CP000764; ABS23416.1; -; Genomic_DNA.
DR   STRING; 315749.Bcer98_3193; -.
DR   KEGG; bcy:Bcer98_3193; -.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000402_0_0_9; -.
DR   OrthoDB; 9765680at2; -.
DR   Proteomes; UP000002300; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd00833; PKS; 2.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
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; 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; PF00501; AMP-binding; 1.
DR   Pfam; PF21394; Beta-ketacyl_N; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 2.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 2.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
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; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 2.
DR   PROSITE; PS52004; KS3_2; 2.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        95..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          609..686
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          709..1165
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2134..2208
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2231..2693
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   3099 AA;  347353 MW;  13A3CEB16EC52D56 CRC64;
     MKRVKREKNC KLSIAIGKNI EGELYKKENI GRLLMEAADE RKDSGITFIQ NDGVEDFLSY
     ESLLNRAVRC LGGLQKKGIQ QGQHVMLVLE DSRDFIISFW ACILGGIIPV PLVYPTSLKM
     KNSILDKLFV VWNLLEKPVI LSDDHVVNHH EKIESLLAVK GMEFLSISTL YSANEGGEIN
     LAPSDTPAFI QFSSGSTSVP KGVILTHRNL LTNIEAMIAG IHLNHEDKSF SWMPYHHDMG
     LIGFHLVPTA KGIHQFNMSP MKFVKRPNLW LDYITKHRIT LTGSPNFGYR LLLSRAKEEQ
     FKKWDLRSLR LIFNGAEPIS VSLMREFMSK LKQCHLRKEA MFPVYGMAEA CLAVSFPKWN
     DEPFVNCINR KTLVSESRVE KCLETDRQAM LLVEEGSPVA GMKIRIVDEV GNVVPEGIVG
     EVQIYGENVT DGYIYNDRVT KESIQDGWLK TGDTGFLLND RLTIVGRIKD IIFVNGQNFY
     AHDIEGIIEK IEGVKPGRIA ICGWHDEKEE KDKVALFSSL PIKQKDTNKI YSKIVSRVNE
     LIGIPIDYVV LTPSIPKTTS GKVQRFVLID AFKNNKYEGK VLSRTDLSVG LQDENIVEKQ
     EKKEKQKTME FGKYAEKIRE IWSEVLEIPL EHTPYNESFL SLGGTSIKAI QILGYLEDEL
     SLTLSHDILI NCRTVNEMDE YIVKVVQGNE GIESGKVKVS SRKMSEEYEG DIAVIALSCR
     FPDASTPEAF WENLVQGKCS IKEIPSDRWS VKDYYNQIPQ FGKTYCRKGA FIQNPYAFDA
     SLFNISEEEA AIMDPQQRMI LELTYELIER AGYTTQMVDG EKVGLFIGAG MNSYYEYHLS
     TLNRQNLQTF DSFKALPKVQ QEAIMNEWKK KFGIMAAHPN ILVDNILNMI AARTSQEFNF
     KGPSMVVDTA CSSSLVTLHM AYESLKRGEC EVAIAGGINL LLTPAPYIFF SHAGALSSSG
     RSMVFDEQAD GFVPGEGAGL VMLKTLKKAK ADGDKVLATI KASTINNDGR SIGVMAPNPD
     GQREVIESLY VENEISPQTI QYVEAHGTGT RVGDPSEVRA IDTAFRKWNV GQQSIAIGSV
     KANIGHLLGA AGIGSFIKVI MSLLYRKMPP NINIFTPNPM IKLEQTPFYL LDEPKEWSKE
     KGVPRRAAIN SFGFGGTNCH LIVEEASETK EVKVNQAIEL PKHVLCLSAH SESALQQKVT
     NLIACLEDSY EYSLGDVCYT ENVTRTPLKH RYSVIASSID DLIEKLKNSS LDNTMVQASP
     KVALMFTGQG SQYAGMARQL YKLVPRFKKY VDDCSEAFYP ILNQSIVDLL YVEANESLLA
     QTHITQPVVF TIDYALGKLL LDLGVKPACM LGHSVGEWVA ACLSEMITLQ DAARLVAIRG
     ELMNEIQTTG AMTAIFSSIA TIEPLLEPFK DSLWFAGYNI THQVISGQAE AMEKFLSLLE
     KKGIVFKKLK VSQAFHTPLM ETMLAPFKKE LSAITFNKPK IPIVSNVTAE YISQPIHPEY
     WLEHILGTVK FEQSMKYVLD KGINIFVEAG PDKVLTSMAN GLISYKDKCL ISMIERKKEN
     WDVYVNAVSK LYTLGVNIDW KTFMKDYGNE RVILPSYPFE HKIFKPDFGE ELRFMDWLYE
     WKWEMETPLY IENDKRGSIL VFDDEQQVGK EVCGILEQIN TSVYVVIPGN EFHYDGDTRF
     TIRPESIEDY MMMLQHIQGD SISIIHLWNG TKESVTPTLF LQDESALFQT SYSIILMAKA
     LKIKAYKNVE FIVVTDRAFA VLQDEEIQKP QQSISAVIGQ VIDQENSEFS SCILDVDNRA
     YENKFAELAE LIVRELSMGR QEEAIVAIRG GKRFVRKLER IVPSKKQEIT IQDNETYVIT
     GGTGHIGGEI ARAFFKKAKV NLVLTGREQL PSREEWKKGN LSSKVVSKIN VIQDLENQGA
     KVEYFAVDVT NEQKMKEMIQ AVKQLYGSIH GVVHAAGTIH HSAGKLLSKD LNDIQQVMSS
     KVQGTIIADM VTRQEPLKFF VTLSSISASK KIWAANLGDY AAANAFLNGY SQYRKNTGAP
     GRSLSINYSL WADKGLSEMF GDLSALAVKA QKLNPLSSEG GTQAFFEVLQ YEGKSVVHIL
     DRQEDCVANN VAEKVVVLSP SNEPAHPVRY KTAKEIKEIV YQVIAAEINC DAESLEVTKN
     FLELSIDSLK ATKVIAEIGK QLNTELYPTL LFEYQTPEAL AEYIEKTYAV NRQEKVEVRQ
     KEKIGKDEES VKDIAIIGMS VRIPGANNLE EYWKILREGE CMIQEVPEDR WRKEYHYSSD
     QGILHKTYSK HGGFIERPYD FDPLFFGMSP KEAEATDPQQ RIFMQVAWEA LQQAGYGGKH
     RTNQIGVFVG CEQNTYMEHF IGYRYYMMMK DVLEKENTFA HLPLSDRQNL LKQMVRILEP
     GQLVADAIAG NGLNEVAARV SHCLNLTGPS MIVNTACSSS LVALHHACQS IRQGETNMAI
     AGGVNLNLSP TPFVSLSRVT ALSSNGNCYP FDARANGMVL SEGAGAVLLK SLEQAMEDGD
     HIFAVIKGSA INNDGRSQGI TAPRPQGQAE VIRSAYLNAN VHPETVSYIE THGTATPLGD
     PIEVEGMTRA FRTFTDKEGF CGIGSVKSSI GHMLSAAGIV SLVKVALAMK HKVIPHTVNY
     DTPNPNLDFQ HSPFYVVAKQ PQIWGDEKQN HPLRAGVNAF GFGGTNAHVI LEEAPILQRK
     VNHSVPEMKR PSLLLLTGRT EKVIQNVAMR LKEHIKQNPD LCVPEVCYSM NSSQKELSCK
     VATVIKSKEH LYSVLEAIEM GRERSEVIKG RSNPNKRMTT HFLFDGTLCL DKAHIKQLND
     TFSIFHAAYK KCLDVFETEE NENSTSYRQI QSFSCQYAIG KLLLHSGIQP KSFVCEGIGI
     LVGAACTGII TVEAAIQFIK GNKNLTSEIL QNRNDTEYKY TIITPMGIIH KEHTDILKSL
     CMTDMQYTIT TKDIAEYVDK NDVVIQCGIS KSDLQGRLIS MDIGKVSDSV HELLLCMAKL
     YTLGVNYNSV AFFEGNENRI PLPTYPFENK MYKVTFEDEN IYKEALSNTE LHQKSNLVER
     DVHKLVPLHL DETVQDSEKS KNMKQLNHDL VMLFGNIIQ
//
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