ID C3GTB6_BACTU Unreviewed; 3508 AA.
AC C3GTB6;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEM74454.1};
GN ORFNames=bthur0010_55330 {ECO:0000313|EMBL:EEM74454.1};
OS Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527029 {ECO:0000313|EMBL:EEM74454.1};
RN [1] {ECO:0000313|EMBL:EEM74454.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM74454.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004789}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEM74454.1}.
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DR EMBL; ACNH01000126; EEM74454.1; -; Genomic_DNA.
DR RefSeq; WP_000365660.1; NZ_CM000755.1.
DR HOGENOM; CLU_000283_0_0_9; -.
DR Proteomes; UP000006660; Chromosome.
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:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR013217; Methyltransf_12.
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; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
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 NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1012..1086
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1130..1567
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3071..3501
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 3508 AA; 396862 MW; 502E3B5801C7CE56 CRC64;
MDLQKVYELV SNKKITPEEA IFMLEQENWD KNSINVAKDV EFPLSEGQKA LWITHQLNRE
NYAYNVPAAF WLSPTTDLLK LKNILQKMTK YHSALRTKLK VINGQPHQYF SEDFEIDFIE
ESIDNLNNEE LDRVLQKEIK KPFDLKKDNL FRIHLYKQKN GKNLLLFVFH HIIFDGISSQ
IFIEDLERFY QKEDKTSLVS SSLNSLDFQD FVLMQKVMLA SEEGEEHKKY WLGQLQDVDG
VLDLPLDKPR PIYPTFKGSS FEHEIKGALV HQLRSLAQRN NTTLFSVMLS AFKGLLYRYC
NVPNISVGIP MAGRMNYNFE KIIGNFMNVV VIKSGLAPDL PFNILLQNVQ DTVFEAMEHS
DYPLFTLTQD LRALNSNSQL FNVSFYFQNW LDTPENVEES SLIIDTYKGL HQEGESDLTL
EIVEEDEKYL LCFKYNPDLF EEETLIQMKD NYLNVLSCVT EDEEVKLADI ELLRKKEIET
LSMEENIFDL FVKQVEKSPN ALAVVFNNEL ITYQELYQKS SKIAVYLQSK GIKQGDLVGI
FMNRSADLLA IILGVLRSGA GFVPLDPIYP TNRLSMMIED SKLDYVITES MLLDKLPLGN
FDIIQYDIEY EKIKLMENEL IVHRDANSVA YVIFTSGSTG RPKGVEVLHK GLTNFLYSMA
EKPGFTSNDR ILAITTICFD IAYLEIFLPI VTGGVVEIVA SDIINDGIKL KEKIENTSFS
VMQATPATWK MLLQAGWRKE LPIKILCGGE ELSNELADNL LNLSREVWNL YGPTETTIWS
AVAKIEDKQD ITIGNPIMNT QLYVLDNNLN SCPIGAVGEL YIGGEGLAKG YINNTEETSK
KFLSNPFSLN ESQKIYKTGD MARYREDGKI ECLGRIDNQV KIRGFRIELN EIEKALQEVD
GVIDAVVLLR NEDIQNKRLT AFVIAENSIE EISVSFFHKL LSDKLPKYMI PAQFIRLSNF
PSTLNGKFDR KTLSSKKISE IQQLYYNKEL INKSEHTSSL NQEYQKNNHY QEIIVQDLTK
IIVSILGIDG SIISTDKHFG EYGFDSISFT SFGVAINDLY NIQVNATLFY EYSTLDSLAE
YLFQNYESYV RIYYQKLVQE SKELARNDKQ VIQNDILSTQ NKEQSNIESD EKVAIIGISG
QMPGSANLKQ YWNNLVRLKD LISLIPKDRW DYKLYTSDLK GRKSTSYSKW GGFMSDVYHF
DSLFFGISPR EAEIMDPQQR LFLQTTWEVI EDAGYKPSDL SGTDTGIFVG CTGTDFLDVL
HESNHDIEAH SISGISRTII PNRISYLLNL HGPSAVIDTA CSSSLVSIHR AVNSILSGEC
SMAIAGGTNV ILSPVAQDAL SKSNMLSSDG RCKVFDKSAN GYVRGEGVAA ILLKPLSKAI
EDGDNIYGVI ASTSENHGGK TNSLTTPNVN AQTELLVEAY RKAKINPSTV TYLESHGTGT
ALGDPIEINA LKKAFNSLYK QADETFKGKP YCGIGSVKSN IGHLEASAGI AGVLKVILAM
KHGVIPGNLH LNEVNPLIEL NDTPFYLLKN TQEWKHLVDE KGEEIPFRAG ISSFGFGGVN
AHIVLEEFKK QRGTYNYLLD SYIIILSAKN EDGLYRYAKQ LLQYLEDDYN EKEVSLGDVA
YTLQIGRESY EERLALIVNN SSELHEKLVA FCSGDKKIPN LFRGSKEDNK NKLSLVLEGE
EGNEYIRNLV TNRKDSKLTL LWINGMDIDW KLLYEGSPSR VALPTYPFAK TEYKISLDFN
NEIRNGKNCS LPLIDNMHPT SEHEILLCFR KELCRNEVIL QHHEVDGQAI LPAVGYLEMI
CEAVSLFRKG TYRFSKVTWL APLTVQNETK EVFVIFKAQK QNMIQYEVRS SKIDGMIHAQ
GSIQFLDNEE SPSKTSISID EIKDKCENVL DKEIFYTHVR EAGINYREYF QVMETVWSND
TSALGFLKLP INYVKEFSRY KLHPAIMDGA LQVMAMLSKG NNKPKVPFSV ERIEVIQSPT
EECYAYVQKN TEESFNIILL DKDGNICVKF KTLLSREIKG KHKNMYYYPT WVKVPLTNVN
ISSNDSSVLI ITSERPTGIE TKLKEHFKEA IEVRLGKKNR EIKENIYEID SENPFAIHQM
IDKLVNIQQV YYLGAIHRTG YELQDLSLIG KMEEDSIVNF FRLCKALDEQ DLFRKNIKLT
VVTNDSVNIV GSENTTPFGS GIYGFAMSAA VEFPYWNIQC VDVSFEINSQ ESICKKLIEL
SHYPQNKENE FLALREQNFY KRVIKDLELK PSTFSSFKNS GVYFIVGGTG GIGLSLGKYL
AKNFKAKLVL TGRSELTGEL EEKIKEIESF GSEVLYLQAD VTSIKDMEYA VEEATIRFGK
VDGVIHSALV LKDQSIRSMS EDILREVMAS KIRGSVILYK VFEKKKLDFM LFFSSTCSFL
KSAGQSNYSA GCMFQDMFSA VLHDVAPFPV KTINWSYWSE AGVVANKKYV EKLTSQGILG
IKIEEGIQAI EEVLSSGVKQ TIVQKTSKDI LDNMNYDTSY NVRSYPPKIP GLANQYDNYS
PDTKEQGLIL DIVQGIQRIE EYGVLLLWKT LQEMGCFKTK QMTYNKAELR KQINIINNYE
NLFEAILIIL EKYGYISIKG ENILVVSTPN IKHINEDREQ ICLSYPSLLP YIDLLEACLF
SYPEVLTGKK DHMSVMFPNG SKMLVEPIYK GNELVDFYNK TVASIIENYV TKRLEQDKNS
TINVLEIGAG TGGTSAFVFE KLKKFKNNVN YCYTDISVGF TRYGKAEYGN KFGFGTFKVL
DIEKDIKNQG FLENNIDLCF ATNAIHATSD ISNALENVKI LLKSNGIFIL NELTKLQIFS
TLTFGLTNGW WLFKDPSSRI KASPLLSPRQ WKTQLSQQEF KNIKLIDVFN SEEIEKAQSI
IIAESNGIVK LKKDMVHKHQ LDVEDTKHVN RVTDKVIKKE RKSRDKVYNA LSDFELYNKM
YEYLEATFAN ILKIEVSILK NDVPFEKYGV DSLIIIELNK IFEEEFNDVP TTVLFECVTL
KDLTQYFITN HLEEIKNKFR VEAEVIEEIA ATSEDDVVIS NEDEFINVEN NNPDIKIENS
DMEIKLPYQS NDEIAIVGVA GRYPLADSVE EYWDNLVEGR NCITEIPKER WDLKGFYDAT
SNEHGKSYSK WGGFIKDIDK FDADFFGISE GLASEMDPQE RIFLELTWHL LEDAGYPYHS
LSSKGYRTGV FCGVMYGTYG TMGTVLSEQG IYTGAQSSYW LIPNRVSHYF NFNGPSFSID
SACSSSLTAI HLACESIKRG ECDTAVVGGI NLILSPRHFL RLSNLKNLSS SDETKTFGSG
ADGFVVGEGA GAILLKPLSK AIQDNDKIYG VVKGSFINST GNSGGFMAPN PVSQANLIEE
ALKKSGVDPR TISYIEAHGT GTILGDPVEI SGLTKTFRKF TLEKQFCAIG SVKSNIGHLE
AAAGISALTK ILMQMKYKKL VPSLHAGEVN PYIKFEDTPF YLQKTLSDWN APIIEGKLYP
RRAGVSSFGA GGANAHLIVE EYLENEGE
//
