ID   A0A1Y0ISE7_9BACL        Unreviewed;      3166 AA.
AC   A0A1Y0ISE7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Non-ribosomal peptide synthetase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CBW65_22910 {ECO:0000313|EMBL:ARU63538.1};
OS   Tumebacillus avium.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1903704 {ECO:0000313|EMBL:ARU63538.1, 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   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000256|ARBA:ARBA00029443}.
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DR   EMBL; CP021434; ARU63538.1; -; Genomic_DNA.
DR   KEGG; tum:CBW65_22910; -.
DR   OrthoDB; 9765680at2; -.
DR   Proteomes; UP000195437; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd17646; A_NRPS_AB3403-like; 1.
DR   CDD; cd19531; LCL_NRPS-like; 2.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.980; -; 4.
DR   Gene3D; 1.10.1200.10; ACP-like; 3.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
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; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
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; IPR025110; AMP-bd_C.
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; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 2.
DR   Pfam; PF00668; Condensation; 2.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 3.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 3.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 3.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR   PROSITE; PS00098; THIOLASE_1; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          967..1042
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1068..1495
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2010..2085
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          3070..3147
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1045..1067
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3147..3166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3166 AA;  348938 MW;  E64BF256E40748D2 CRC64;
     MAVLYAFPVS FAQQRLWLAD GVLPGSSAYH IPAVLQIEGD LNEEALGRAL TEIVDRHESL
     RTSFGMLDGQ LMQKVHTERE QELVTVDLCN VPLDEQHAAV ERLTHEELVR PFDLAAVPLV
     RMTLYKLSEQ KHVLMVVIHH IVSDGWSTGV LIRELSALYT AFAAGEESPL EPLAIQYADY
     SQWQHDDLET GVLDEHMAYW REKLGGELPV LKLPTDRPRP PHRTDAGDSV QVKLSQELSE
     RIKEAGRKEQ ATLFMTLLAA YQVLLSRYTG QDDVLVGSPI AGRNQPDVHG LIGFFVNNLV
     LRSDLAGNPT FLELLAEVRQ TALEAYQHAE VPFDMLIQEL VPDRDISVSP LFQTMFVLRD
     QVAPIELPGL TTSLVDLEIK AVKYDLALEV INAADGLLIT WRYKTDLFDP ATIERISANF
     VVLLEGIVNH PHEKVAYLPL LTEAEQKQVV EVWNDGAETV YQDLTLHAFF EEQAEKTPDR
     VAVVFEEESV TYREFNERAN RLASRLLKLG VQANEFVGVS MERSIEMLVA VYAVVKAGGA
     YVPIDPTNPP ERVAYILADA QVNVLLTQEY LLERLPDLAG TQVICVDRED FSGESAANPA
     LAVPTDGLAY MIYTSGSTGK PKGAMVPHKA IVNQILWRQE TYRLTESDRI LQKTPVSFDA
     SVWELFWALM VGARIVMARS EGHKDSAYLR EVIKEQGVTT LHFVPSMLQM FAEEKGIEEC
     TSLRRILCGG EALPADLQAR VFARLPHVEL HNLYGPTEAA VDVTYWFCER ESSRKTVPIG
     RHIANTKLYV LDKHLQPVPL GAAGELHIGG VQLAYGYHNR PELTAEKFIA NPFGAGKLYK
     SGDLVRLQPD GVFEYLGRLD HQVKIRGFRV ELGEIEALLT QHPQILEAVV MPKGDGLAAY
     VVADSSGDAV DAQELRRYLQ EALPVYMVPG SFAFLEKLPL TPNGKTDRQK LVALETTSPV
     SDALYVPPQS ELEQGIAAIW QEVLEVEQVG LYDNFFELGG HSLAIMRVHR RLQEKYEFEI
     SVVQLFQYPT VKELAEHFAA QRPEAVQAEA DANDGGSKKQ DAQRTGEKQD IAVIGMAGRF
     PGAADVESFW RNLQDGVESI RQFSDEELLA EGHDPHVLQA PNYVKAGGYL GDIEYFDADF
     FGINPREAEV MDPQHRIFLE TAWQALETAG YDSEAFDGDI SVFGGAGLSR YLLVNLVPNR
     HLAASVGEHT VMIGNGPDHM VGRVAYKLNL TGMSHAVSAT CSTGMVAIHQ AAQSLRNGDC
     DMALAGAVGL AVPQKNGYFH VEGGISSPDG HCRTFDADAQ GTVPGSGAGI VVLKRLEDAL
     RDGDRVMAVL KGSAVTNDGS RKVGYTAPSV DGQKAAILKA LEKADVEPES VAYIEAHGTA
     TPLGDPIELT ALTQAYRTLT KKERFIAIGS VKSNIGHLDA AAGAAGFIKT VLALHHGQLP
     PSLHFRNPNP KINWERSPFF VNTELRDWSR GELPRRAGVS SFGLGGMNSH AILEEAPLQE
     SSESLRPAHL LVLSAKTETA LEAATANLKQ HLAQHPEQKL ADVAFTLQLG RRPFAHRLAL
     VVTGHEDALE VLDTLHPRRL MQGHADLTDH ARPVAFLFAG TGDHYVEMAS ELYETEPVFK
     RVVDQCCEIL ETHLNVQLKE VLYPNGVGET QRPTGQETPA FDLRKMLRRE EGADLGQLNQ
     TEYAHPALFV IEYALTQLLL EWGIRPQALL GYSLGEYVAA CVAGVFSLED ALVLVAQRAK
     MIQELPQGAM LAVPMGEAEL RPLLNSDLSL ATVNTQQHCV VSGTKEAVAR LEQTLLAQGI
     ACLPVKSSHA FHSHMMEAIA EPFAELVRSF QPQAPKTPFV SNVTGTWITA EEATDPAYWA
     RHLCQTVRFA DGVRELCQDP NLLLLEIGPG QTLTSFALQL QTNGERIVLP TLRPAYEKRS
     DTSFLLSTIG QLWLSGVAVK WPGLYTHEQR LRVPLPTYPF ERKRYWIQAK KGAAAQPSSG
     AHLIREEEDT STQMLDTGHA RPHLSTAYAG ATNREEQAII GIFQELLGIQ GVGIHDNFFQ
     LGGNSLLGTQ LMSRLRSAFG IDLPLRTLFE RETAAELAAI IAKQTAPAAT SASTQTSQIP
     RRPEANSPLS FSQERIWVME QLAPHGAVYN IPAALEMTGP LDLDLLTESI NEVISRHETL
     RSTFRLADGE PYVGYAPELS LTLGQQDLRA LPDEERRTEA ARLADELARQ PFDLQQGPLL
     RATAMRMADD RHILVLVIHH IIADGWSLGV LISEIAKLYA AFSQGTASPL PELPLQYGDF
     AHWQKLPGQQ AELHRHLAYW KQQLGDAHEP LALPTDRPRP AMQTYRGARQ SFTLSKGLSD
     ALQQLSAREG TTLYMTLLAA FQSLLARYSG QTDILVGSPI AGRSLRETEE LIGVFVNTLV
     LRGRVEDGLT FQDLLQQVRQ TSIDAFAHQD LPFEKLVAEL QPERNMGVSP LFQVMFNMLN
     APMKLTVPGG LTLETVELNS GTAKFDITLA MSEREHGLIG EWEYNTDLFD AATITRMITH
     FQTLLESVVQ RPEQLLQEIP LLSPAEQQMM LRDWNNTEAV YREDACLHQL FEEQAERTPT
     AIALVFEDQE ITFAQLNSRA NALAAQLQAM GVGPDDLVGI CMERSPEMVI ALLAAHKAGG
     AYLPLDPNYP PERLAFMIAD AKPKAILTQP ALANQLPSQD AHVLAVTSEE RHGHALHPNV
     TSPVQPDHLA YIIYTSGSTG LPKGVMVTHR NAVNHFTGMD QMVGCTADDV MLAVTSIGFD
     ISVPELFWTM ASGAKVVLLS EREIIEAGVS NSPYSFRAQL ERHRATMLQS TPSFLWSFTS
     NAEGLAAVQN LQKILLGGEA LPSALADRLH TQTTARVFNL YGPTEATVYA TGYEVRESGL
     TTVPLGRPLA NCELYILDRH LQPVPIGVAG ELHIGGIGVT KGYLGREELT GERFIPHPFG
     QGTLYKTGDL ASFLPDGTVL GQGRLDQQLK VRGYRIEPGE VEAALLAHDS IREAVVIARD
     NTLLAYVVAV GGILPETEAL HSFLRATLPA YMVPGHIVPL DRLPRTPNGK IDRRALPAPF
     AAAPQREYVA PQTPTERLLT AMWAELLQLE PEVLSVHDNF FHIGGHSLMA TQLIARVQKE
     FGVALPLRDL FEKTTIAELA QAVEQADSHH EAQIMRQERV RSSRKR
//