ID Q0PEX6_BACIU Unreviewed; 1906 AA.
AC Q0PEX6;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=PksC {ECO:0000313|EMBL:ABH03697.1};
GN Name=pksC {ECO:0000313|EMBL:ABH03697.1};
OS Bacillus subtilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423 {ECO:0000313|EMBL:ABH03697.1};
RN [1] {ECO:0000313|EMBL:ABH03697.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B11 {ECO:0000313|EMBL:ABH03697.1};
RA Wu X., Duan C., Li Q., Tang J., Feng J.;
RT "Cloning and identification of genes involved in biosynthesis of
RT antagonistic substance from Bacillus subtilis strain B11.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; DQ844599; ABH03697.1; -; Genomic_DNA.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
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; 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; 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; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 2.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS52004; KS3_2; 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 323..397
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 423..500
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1020..1442
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 1906 AA; 214239 MW; 7564F8A25660243D CRC64;
MRQVASNQNY QFTLTIKHTD YIVRDHRVHG TRIIPGVTFL DMIYRMALSK GLPIEELECQ
NILYLEPVAT SDTFDREIRI RFQGLEQGWE IQAKSRKVKD DRILDESWDE NMNCRLMQKF
PESMSSIHID EIKHVSVREA DMEICYDYLK KVDIEHFEFM KSLGKVYASD HSVLAELSLS
QIAKQYTGYF QLHPTFLDAS TIISILYQAC PEYFTQGSPA SRMKTYIPIH IESFRMTKRL
EDRCYVYIEK QDQNHDSGDV IQVSYGLYDA HGEMIAYFTR LSVKHIRSKD LIENLKQTRL
ETEAASQPKD GLMRKDSIID RSESIETHLK ELISGVSNID LRDIRTDIGF YEQGLDSASL
LAIVKELENK TGEQLYPTLL FEQKTIRELA AYIKENQKMS SYFLTQNQPA EKPDMKESKN
ENLSALITEG DIQQLIADIK GTAPETLSVV KGFYEQGLDS VTLMQAVKAL EEKTGRELYP
TLLFEYPTIQ KLANYFAESG EKTSVDKDLP LHHGENHTAL TYLTPYWRQK AAAWDPHCGN
KKKRTCLLFQ YDRKLFHFMR ENAENGFENT QIILVLSGNR FSYHGDGIYE IDHREEAHFD
RLAADLKKRG QMPDTVVYGW PEGSFAGPEK ISEQLSKGAY PLFFFSRALM RSKAEKKVVS
LFLYPADHKN DQPLYASVHG AGQSILLENP KLALKTIGIS VSDKTSLPAL TAEIIRCEST
EAHPGETDLY YEGNVRWVRA LREAEPAQNS DFSFKENGVY MITGGAGGLG LIFAEHIAAQ
TKANIILAGR SELTEDKKNK ISRMKAGGSS VQYIRGDFSD SRDAERIIKT IKKKFGEING
VIHSAGVTHD ALLIQKSKDE IQEVIAPKIN GTVLLDSLLQ TEPLDFFVMF SSSSSMYGNI
GQTDYALANR FIDLFAEWRE GMRRKKERSG VSVAIGWPLW EDGGMKVDKQ TEKWMKQKIG
MVPLSKTNGI KAFQDSLSMN ASQLIVFEGD KEKLESALQD TFKEDESREI QINETADTRH
QDIAIIGLSG KYPMAEDLPE FWENLKSGKD CITEIPPDRW NIDDFFSEDR DMKGKSYSKW
GGFISGADQF DPLFFHISPR EAELMDPQER LFLETAKNCF EDSGYPRNML EKMKVGVFVG
AMWGQYQLFE GEENGAAFSP ASVYSSIANR VSYYFHLKGP SLALDTMCSS SLTSIHYACQ
SIHCGESDMA LAGGVNLSIH PNKYKFLSMG QFLSSDGRCR SFGKDGSGYV PGEGVGAVLL
KPLKKAIEDQ DQIYGVIKGS AVNHGGKTSG YSIPNPDAQA EVISEALRKA DIDPNTVNYI
EAHGTGTSLG DPIEIQGLKD SYQLNHPCAI GSVKSNIGHL ESAAGIAAVT KVLLQMKNKQ
LVPSLHSDIV NPFIDFDQVP FQVQRKAAEW NIPQNSHAVH PLRAGVSAFG AGGTNAHLIL
EAYEPPKAFD HQSGRVIFVL SAQDKQRLIK YAKVMADFLS ENESKDNNHK LRLQDIAYTL
QTGRDHMEER LAIVADSGQV IAEELSAYIR GEKSSLSHTG NTFESEVHNE MPHVCSDYAE
AASKWVNGRK IDWETFEVNR NARRISIPGQ PLIKQRYWIA EKGEALVSAD VSKTGHPFLG
SNTSDFNQFS FTKKISRNHP FALSLSEGNV SFFPYASLAE MAIVNAAAAF GQPVQTLTDL
LWTESMNGMT DIRELMITLT PERDFARFDI YANTKNENKV RLASGNAHMV KPESGMLPEA
LDIAEVKSEM TEHPAEAPFV IESAKNSYGM LSLHSMPDEL YAKRENFTIS PEALESAIQA
SAFFVSGETF PELIGMGAAD VYQPLAQNFY VYTQKVNRQN SRDVTCHMTF TDGNGSILAE
CRDVRFRYGH EKDTVQTDDE LISLLRQLET NDIDQKAVLK QLMGEE
//
