ID C3GTB5_BACTU Unreviewed; 2796 AA.
AC C3GTB5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEM74453.1};
GN ORFNames=bthur0010_55320 {ECO:0000313|EMBL:EEM74453.1};
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:EEM74453.1};
RN [1] {ECO:0000313|EMBL:EEM74453.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM74453.1};
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 -!- FUNCTION: Involved in some intermediate steps for the synthesis of the
CC antibiotic polyketide bacillaene which is involved in secondary
CC metabolism. {ECO:0000256|ARBA:ARBA00003299}.
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 -!- 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:EEM74453.1}.
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DR EMBL; ACNH01000126; EEM74453.1; -; Genomic_DNA.
DR HOGENOM; CLU_000022_53_1_9; -.
DR UniPathway; UPA01003; -.
DR Proteomes; UP000006660; 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; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 1.10.1240.100; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 4.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2.
DR InterPro; IPR036736; ACP-like_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; 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; 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; 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; PF21089; PKS_DH_N; 2.
DR Pfam; PF00550; PP-binding; 4.
DR Pfam; PF14765; PS-DH; 2.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 3.
DR SUPFAM; SSF47336; ACP-like; 4.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 4.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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 278..357
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 408..843
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1807..1883
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1922..1998
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2059..2479
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2664..2741
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2016..2050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2018..2047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2796 AA; 316979 MW; DD55DE0E221BADE9 CRC64;
MLRKDAFYLQ DHIVNGQVTL PGVVYLEMAR MAGTLASPSQ SVIGLQNIVW TQPIHLSEDK
EEVSIELQSK DEQIFYNIYK EESTVCSQGN IIYGTLKDIA TEWMDIDKIH RNFNQKIERQ
SLYPLFEKAG FMYGESFKPI NHIYFNEKEA LAEIQIAKEI QASAKDFLLH PSLLEGALQT
AGYLVNTVMQ TTNTYVPFAL GKLEIYGELP EKCYAYASLS ATEGNVMKMS VMLLDEFGQV
LIKIEDYMVR SFSKEKYSRR TVIKTKDEKK KVLQDSTGVL NYVKEGLVKI VARIVEIPED
KIDLNGDLDK YSIDSIVLTE LSNSINTHFQ LDITPAFFFE NAEFTIQNVA TSLYEKKKEE
LENLYQHKVE KNQVSNFSNV RIMEEKKNKE SNAKFQIEKK EKTYSRRNEP VAIIGISGKL
PKSNNLEEYW KHLYSEEDLI SEIPIDRFDW KDYYGDPMKE PNKTNSRWGG FMKEVDAFDA
SLFNITPAEA MYMDPQQRLF LETVWGVIED SGYTPSELSG SKTGVYVGVS NLDYGDLLVD
HKLDALGMTG NNHAMIANKV SYFFNFTGPS EPVDTLCSSS LVSIHRAVED IQNGMCDMAI
AGGVNVILSP KLYITYSNAG MLSSDGKCKT FDKNANGFVR GEGVGAILLK PLRKALEDND
NIYAVIKGSA TNHGGRAKSL TSPNPIAQAD VIKAAWGKSG IDPSTVTYIE THGTGTALGD
PVEVNGLKLA FKELYNDWGK KFESLPICGL GSCKTNIGHL ESAAGIAGVL KILLALKYKT
IPGNLHLEEI NPYVDLKDSP YYIVEKTQPW EQLKDIAGDN IPRRAGISSF GAGGVNAHIV
FEEYQSITRK EYNSDEQEKE HIFILSAKDK ETLKKYSSNV IRYLKDSNYG LEDIIYTSQL
AREEMDERLA IIVSTKLELI NKLEEYYNNN IQNLFVGNVY HDEDKDLKFS LNESIECLIE
KRNLEEIAYS WVNGAKIDWK QFYKNTSLLK IDFPKYPFSR SRFWLQNKSR DISKENTFNI
INKISCENED KTKFKVNFHA NDLYIKEHVV NGEQIVPATA YLDIIRYAVQ QTTKRTVVGL
EDVIWIDPLD IKGNYKEAYI SLTTMETNEN VIKFEIYSSK SIESVSLHCQ GRVRLDNYIY
TNQSKISVAD IKRRCIGDDG EKYYPIFKKM GFSYGESFKT IKEVYKNSEE VLVSLELPQS
INEQDSNILF STLIMDGALQ SSMIMGMEEQ DREIHLPFSV ENLNWYNAIP PKCFAYITRT
GELNQFSKIK KYSLYILDEE GNILIEFVNF TKKIVPIADK SDQPYLVCAP VWKEEKLVYE
NSDINLGDTL ILSSNLSLYE EWRKRIGSDR NLVFVTPGTK FTELGDLKYT INPSCYEDYE
KLWHSLKRQD VYPDNLIQEL STIREDNYLY QSFYPVVYMV QSFIKEMKTR SIRLLYVYEN
LEDSSYPYYA GIKSLLKTIV LEHNNFKCSS VELDSKMNLT QRCMLELFAL AKETSRKVKE
VQWRGNNRYV GNLVEHDIVS SRESLNVGFQ KEGVYIISGG LGGIGLLLCK HLLTAYQAKI
VVFGRSALNE TKQRALQDVM DNGGEVIYMC GNVSNKQDVS LIIKETKQRF GKINGVFHMA
GVIRDNYLMK KTESEIQEVI EPKILGSIYL DELTKEEPLD FFVLFSSISG LLGNIGQCDY
AFANNFMDHF VEIREQRRRT NQCNGKTLSI NWPLWEEGGM NVDSEIKQAI KNSTGMDALA
SKDAFTILER GLRSKLNQFT IFTGDLEKIK SLFNIQNKSI LVSNEKNITL EESNIMNVSR
NDISEENLKT LTIQLLKEII SKVSEIPIKD IKEKLPMDRY GLDSIIILKV GNELEDYFDD
LSKSIFFQYE TIFELCEYLI QNYKDRLQDI FSEEEREVKE EQQELGSIKS YSSSNSIQDE
KELKLLTTQF LKEIISKVSE IPIKNIKEKV PMDRYGLDSI IILKLGNELE EYFNNLPKSI
FFEYQTITDL SGYLVENLKE ELLSIFKLDG LSMMQGKRNN NKEDKSNDDT KKDVKSDKAK
EIHGMDSQSR EYQPSVYESE EIAIVGISGK YPLSENSDTF WKNLKNGKNC ITEVPTERWD
AELYFNTEKG VTGKSYTKWG GFINEVDKFD PLFFNISPAE AELMDPQERL FLEIVWATLE
DAGCTRDSLG TEVGVFVGSM YKHYPWIAKD TEAESLLSST SYWAIPNRVS YLYDFQGPSI
AIDTACSSSL NAIHQACQSI KLGECKAAIA GGVNLSIYPE KYVGLSRTGM IGSSEKSKSF
GDGDGYVMGE GVGAVLLKPL SKAVEDGNHI YGIIKSSASN HGGKTNGFAV PSLNAQVNLI
EKVIKSANIP AETISYIESA ANGSVLGDMI EVNALNKVFK NVTNRKNTVP IGTVKANIGH
LEAASGISQL TKVLLQIKHK SLVPTISARP INPHIELENS PLYISDREEE WKVTNGVPRR
ALINSFGAGG SNTALIVEEY VDGHVMKKGT DSESSLLFVF SAKNNEQLKD VVKGLVEYIK
NTNITSLKNI AYTLMDGREW MESRLAIIAK DEKDLLEKLE SYLEGSKGDL EVFYGHVEEE
QLYSQDTAKE EFDGLVLNNN LKTLAQIWVG GIQFNYKKLP QFLDCRHVSL PTYPFARQSY
WVTDTAVNQE LEVVDKNTQK VDGDVEQVAE QVLIEAISGI LKVPMNSMNV NEKLSRYGFD
SLSGMRFINW FQEQHGGEIP ISAFLKYPTI KELAKYLVSQ ELFGCIKSNT VDEPRSVKTG
NGNKMLNMIL QSIYSGKVSP EEAILLQKKL INNTRE
//
