ID   TES_ALTAL               Reviewed;        5161 AA.
AC   A0A144KPJ6;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   08-JUN-2016, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Nonribosomal peptide synthetase TES {ECO:0000303|PubMed:27490569};
DE            EC=6.3.2.- {ECO:0000305|PubMed:27490569};
DE   AltName: Full=Tentoxin synthase {ECO:0000303|PubMed:27490569};
DE            Short=TES {ECO:0000303|PubMed:27490569};
GN   Name=TES {ECO:0000303|PubMed:27490569};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, DOMAIN,
RP   AND PATHWAY.
RC   STRAIN=ZJ33;
RX   PubMed=27490569; DOI=10.3390/toxins8080234;
RA   Li Y.H., Han W.J., Gui X.W., Wei T., Tang S.Y., Jin J.M.;
RT   "Putative nonribosomal peptide synthetase and cytochrome P450 genes
RT   responsible for tentoxin biosynthesis in Alternaria alternata ZJ33.";
RL   Toxins 8:0-0(2016).
RN   [2]
RP   FUNCTION.
RX   PubMed=7881545; DOI=10.1099/13500872-140-12-3257;
RA   Ramm K., Ramm M., Liebermann B., Reuter G.;
RT   "Studies of the biosynthesis of tentoxin by Alternaria alternata.";
RL   Microbiology 140:3257-3266(1994).
CC   -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC       that mediates the biosynthesis of the phytotoxin tentoxin, an inhibitor
CC       the F1-ATPase activity of chloroplasts, resulting in chlorosis in
CC       sensitive plants (PubMed:27490569, PubMed:7881545). Tentoxin is a
CC       cyclic tetrapeptide that consists of four amino acid residues: glycine
CC       (Gly), alanine (Ala), leucine (Leu), and dehydrophenylalanine (DPhe)
CC       (PubMed:27490569, PubMed:7881545). In addition, both the Ala and DPhe
CC       residues are N-methylated (PubMed:27490569, PubMed:7881545). The
CC       nonribosomal peptide synthetase TES assembles tentoxin from the four
CC       substrate amino acids (PubMed:27490569). The adenylation domains of
CC       each of the 4 modules are responsible for the activation of Gly, Ala,
CC       Leu and DPhe, respectively (PubMed:27490569). In addition, the N-
CC       methyltransferase domains in the second and fourth modules of TES could
CC       be responsible for N-methylation of Ala and DPhe residues
CC       (PubMed:27490569). Finally, the condensation domain located in the
CC       termination module probably catalyzes the formation of the
CC       intramolecular macrocyclization and then the release of tentoxin
CC       (PubMed:27490569). The cytochrome P450 monooxygenase TES1 is predicted
CC       to be involved in the formation of DPhe (PubMed:27490569).
CC       {ECO:0000269|PubMed:27490569, ECO:0000269|PubMed:7881545}.
CC   -!- PATHWAY: Phytotoxin biosynthesis. {ECO:0000269|PubMed:27490569}.
CC   -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC       (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC       (C) domains) which when grouped together are referred to as a single
CC       module (PubMed:27490569). Each module is responsible for the
CC       recognition (via the A domain) and incorporation of a single amino acid
CC       into the growing peptide product (PubMed:27490569). Thus, an NRP
CC       synthetase is generally composed of one or more modules and can
CC       terminate in a thioesterase domain (TE) that releases the newly
CC       synthesized peptide from the enzyme (PubMed:27490569). Occasionally,
CC       methyltransferase domains (responsible for amino acid methylation) are
CC       present within the NRP synthetase (PubMed:27490569). TES has the
CC       following architecture:A-T-C-A-M-T-C-A-T-C-A-M-T-C (PubMed:27490569).
CC       {ECO:0000269|PubMed:27490569}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of tentoxin
CC       (PubMed:27490569). {ECO:0000269|PubMed:27490569}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KT947104; AMT84997.1; -; Genomic_DNA.
DR   SMR; A0A144KPJ6; -.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   Gene3D; 1.10.1200.10; -; 4.
DR   Gene3D; 3.30.300.30; -; 6.
DR   Gene3D; 3.30.559.10; -; 4.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   Gene3D; 3.40.50.150; -; 2.
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.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00501; AMP-binding; 4.
DR   Pfam; PF00668; Condensation; 4.
DR   Pfam; PF00550; PP-binding; 4.
DR   SMART; SM00823; PKS_PP; 4.
DR   SUPFAM; SSF47336; SSF47336; 4.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 4.
DR   PROSITE; PS00455; AMP_BINDING; 4.
DR   PROSITE; PS50075; CARRIER; 4.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 4.
PE   3: Inferred from homology;
KW   Isomerase; Ligase; Phosphopantetheine; Phosphoprotein; Repeat; Virulence.
FT   CHAIN           1..5161
FT                   /note="Nonribosomal peptide synthetase TES"
FT                   /id="PRO_0000438987"
FT   DOMAIN          569..645
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:27490569"
FT   DOMAIN          2068..2141
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:27490569"
FT   DOMAIN          3139..3215
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:27490569"
FT   DOMAIN          4643..4725
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:27490569"
FT   REGION          37..436
FT                   /note="Adenylation 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:27490569"
FT   REGION          659..1098
FT                   /note="Condensation 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:27490569"
FT   REGION          1122..1522
FT                   /note="Adenylation 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:27490569"
FT   REGION          1630..1742
FT                   /note="Methyltransferase (M) domain 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:27490569"
FT   REGION          2179..2593
FT                   /note="Condensation 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:27490569"
FT   REGION          2614..3010
FT                   /note="Adenylation 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:27490569"
FT   REGION          3232..3668
FT                   /note="Condensation 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:27490569"
FT   REGION          3694..4098
FT                   /note="Adenylation 4"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:27490569"
FT   REGION          4203..4329
FT                   /note="Methyltransferase (M) domain 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:27490569"
FT   REGION          4785..5093
FT                   /note="Condensation 4"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:27490569"
FT   MOD_RES         606
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2102
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3176
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         4680
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   5161 AA;  576696 MW;  66193A5E4EA480FF CRC64;
     MPGSLLFDVN KLDVEKIWER NRGPLRAVNR CVHSLYEEQA IARPNACAIH AWDGNMTYEQ
     LNQHSTRLAS YLVTQGIGTE VMVPLCFEKS IWAIVAMLAV LKAGAAFVPL DPMHPRARHE
     EIFKQTNAKL VLTSVQHAAL WPNSGLQFLA IDKTFVDQLP WETKIRSKVK PIDAVYVMFT
     SGSTGVPKGV VLEHRAIATS CLAHGMEMKL GSDSRALQFA AYTFDICIAE IFTTLIFGGC
     VCVPSEDDRR NALSEVINNN NINWAQLTPT VARLLDPSTV PSLRVLVLGG ERVDEADWKR
     WGDDIVKVNV YGPTECSIWC TSYSNTDREF RSGTIGTSMA SFSWVTDPED HNKLVPFGTI
     GELLIEGPIL ARGYLNDISK TEAVFVDGPL WLRQGNRNDE STRRQGRLYK TGDLVYYDAD
     GNLVYAGRKD SQTKVRGQRI ELGEIEHHLN QCMSGIKQVA AEVILPSGDQ AKAMVAAFVQ
     LSEEPRHALV QQTSNGDLEV RVIFPTYLDE LLVQCLPKDM VPEVYFAVAE LPLTTSAKVD
     RQKLRKIGAS FSAQQLAQLR TYSDDPKRQP ETEKEQILHH LWAQVLSIDA SSIGMDDSFF
     DLGGDSIAAM KLVGEARRSG IYITVAVVFQ NPTLDKLTSA AIPSVDVSNT TIPPVGHDGH
     VAQSFAQGRM WFLEELHPGL TWYLMPVVVR MRGPLELTAL QSALNAIESR HETLRTTFET
     IGDTSMQLVH PYHAKELSII DIDIKSLEEV LHRDQISPFD LRKEAGLRVS IYRIGSEEHV
     LSVIMHHIIS DGWSTDVFTR ELGAFYSASI RGHDPLVQVQ PLPIQYRDFS VWQRQQAQID
     KHRSQLNYWF NVLNTSRPAE LLCDKARPAA LSGEASKQTI QIDGPLYIQL LQFCKAKGVT
     KFMVLFAAFR ATHFRLTGQN DATIGTVNAN RDRWELKDMI GFFVNLQCLR TTIDADESFE
     ELVQQVYEAT IASLANADVP FENIVSKLKN SRDLSRHPLV QLVFAMHSQR NLGQLKLEGL
     ETESLDNAPK SRFDLEFHFF QQEDSLKGEV VYSTDIYSPE AIDNMLSIFQ IVLEGCLQEP
     KAAIASLSLL CDVELSKLNS MGLIQVEKTD YPRESSVVDL FRQQTSLCPS RIAVKDASVT
     MTYTQLDKES DILAQWLAKQ SLAPETLVSV LAGRSCQTIV AFLAILKAGL AYLPFDVRVP
     AKRMSTILGS LSGPKFVLLG EDVQPPYVDI SDIRFIRITE ALDEQTHEGS ASRDIVKPTA
     NSLAYVMFTS GSTGQPKGAM IEHRGIVRLV RDNNFVQHLP ASPVMAHMTN LAFDVSTWEI
     YASLLQGGTL VCIDRLTVLD PEAVLRTFRQ EHVSTAFMTP SLFRTYVQQL PALFAGLDML
     CVGGEALHSN DILSMTTLRT GKIINGYGPT ENTTFNTTFV LSREGQYPNG VPIGRALSNS
     GAYVMDLKQQ LVPLGVVGEL VVTGDGLARG YTDLERNIYR FITVQIGGEV VKAYRTGDSV
     RYRPADGQLE YFGRMDGQVK IRGHRIELGE IEHVLRSHGS VREAVAVVQQ QQNADEAARL
     AAFVTVYEGD ELVEEKPSGI DESEHVDVWE DQFDSKVYTP ISKVLPEAIG RDFIGWTSMY
     DGSAIDKVEM NEWLDDTIDT MLNGHPPGKV LEVGTGTGMV LFNLGDGLES YVGLDPSSRA
     VEFVKDTVRS VPTLADKVRV YKATATEIDR LEPIDASLIV INSVIQYFPS LEYLFKTTQQ
     LLGLESVSTI FFGDVRSYAL HREFLATRAM FMAGDSADRA EVSRMITDME LVEKELLVDP
     AFFTALPERL PDQVEHVEIL PKKMKATNEL SCYRYAAVIH VKPRDGRKQE QRIRHVGHDE
     WIDFREHKLD RQSLLAQLQS NPRPSTMAVS NIPYSKTIVS RCLIESIDNA VAELSDPQDW
     YSSVCQRAQC SSSMSATDLY ELAKEANCRV EVSWSRQHSQ CGGIDAIFHR YPPRGGENRV
     MFQFPTDHAE RPLHTLSSMP LRQQTLQRIQ GQLQEMLDAQ LPAYMVPQTV TFLETMPTNQ
     NGKIDRNALT QRTEIQVAKG QEFQRELTRA ESKIQQLIAR VLRIDSDRIG LDDSFFQLGG
     DSIAAMKLVA LARDEDIRLT VAKIFQYPKL IQLAAVAQEH VYVPNDNIVP FSLLDDEVDA
     TQTHHEVAVK CAIDRGIIED IYPCSPLQEG LMSLTVKRPG DYIMQTVLEL REEVDETAFK
     IAWEKTVQSF QILRTRIVIH ETLGLLQAVI AEKIKWADAD DLATYLARDK LSSMQLGKPL
     ARYGLVRDTR REKKWFVWTI HHAIYDGWAL NHISVLCKQH TMAGKPGKQV GFNSFIKYLR
     QMDEDALAEY RRTTLSDCDA NVFPPLVSGV QQPVADATAE YCCPPLPKRT SNTTISTLVR
     AAWAIVASGY TSSDDVVFGA TVTGRNAPVA GIESLVGPVI ATVPVRIRLQ RDSTILEFLE
     TVQKQATEMI PFEQTGLQRI AKLGPDTEHA CNFQTLLIVQ PAEDAFQSDD MFGTWEFGSG
     LQDFTTYGLM VQCKLAKEGV KITASFDARL VEQWQVERML GQLSFVMQQL ARGDSRTRVM
     DIGMLTQDDE QQLWMWNQRL PPAIDRCVHD LYSDQAKSRP EADAICAWDG VMTYKELDER
     SSRLATYLVD IGVKPETIVP LCFEKSMWMV VAMLAVLKAG GAFAPLDPSH PVSRHRDIFT
     QTKANMMLTS SQYANLWSEY IPTVVEITGH FIDQLTTNPY STETAVQPGN TAYVIFTSGS
     TGVPKGVQME HKAVSTSCSC QGPALGITED TRVLQFAAYT FDACILEIIT TLLHGACICI
     PSETQRRDHL VNTINTMKVT WALLTPAVAR ILDPQKIVSL KTLVLGGEKV NGSDCDTWSG
     RVRLINAYGP TECCVSCVAS PDMKGLDPEP IGKPIASIGW VTNPNDHNRL APLGAVGELL
     VEGPNLARGY LDDAKKTETA FVHDPLWLLR GCEGYSGRRG RLYKTGDLVY HTSDGDLVYV
     GRKDGQVKVR GQRIELAEIE ICLYQHISDI KEIAVELISP TGGKPMIAAF LKANPELLND
     KLSDGDSGVY VVYPARVDNE LSQRLPRNMV PEVYFALTEF PISTSGKINR RRLREIGGSF
     STDQLARLRT QKNESSDRKP ETKHEMALQK LWAQVLNIEA TSIGLNDSFF QLGGDSISAM
     KLVSEARNVD LVFSVQDVFQ VQRLGRLANR LVDPPTSSHS AITKIDHQRP VLQSFAQGRL
     WFLEQLHPGL DWYLMHLAVR IKGPVQLPAL QAALQAIEHR HETLRTTFST NNGESLQEVH
     PFCGGRELNV IDVGSNDDKI LLEALERDQK TPFNLRYEPG WRISIYRIND VSHVLSIVMH
     HIVSDGWSVD VLKKELSALY ASAIRNEDPI FCLPPLPIQY RDFSVWQRLP EQAQEHRRQL
     DYWINQLDGS RPAEFLYDKP RPTTLSGKAG TQRLNISHKL YNRLQIFARQ RGMTPFVVLL
     AVFRATHYRL TNQDDATIAV PNANRSRPEL GDLIGFFVNI QCMRMKIQDE TFEELLQHAY
     KTVVDSLANQ DVPFESIVSA LQGDRDSSRN PLAQVAFAVH SQQDIGKLDF EGVGTEAIEG
     LATSRFDLEF HFFQEKNGFQ GYIYFSEELF VPETIYSLAS VFTSILDNCL DKPETQIAVV
     PLMTVEAHTQ LDQMGLLRMH QTAYPRNSSI VDVFRQQAAM QPSRVAVKDT STDLTYAQLD
     SQSEKLAKFL ATKSFAPETA VGVLAHRCCQ AIVAFIGILK AGLAYLPFDH KAPEKRMESI
     FSTIEGNKLV LIGPNISLPG TGPKDVEFAY IPDILDADED FEFTRSELDP TLRPTASSLA
     YILFTSGSTG QPKGVMVEHR GIVRLAQHDQ MEHFKSSGAM AHMANLAFDG SSWEIYTCLL
     NGGTLVCIDA TTVLDQDALL RAFTESQIRI AFITPALLNY ILAESPDTIG NLDTLLVAGD
     RADVDDVFRA RDLVRNKVVA NAYGPTENSV MSTLYILSED ENCVNGVPIG RPISNSAAYV
     MDPEQNLVPL GVFGELVVTG DGVARGYTDP RRNVDRFVTV TIGHQTMRAY RTGDYVRQRP
     RDGEMEFFGR IDGQVKIRGN RVELGEIETV LRGHGLVRDA VVVAEQRKDK NQRLFGYITL
     KEDFEMLSAQ NSDDDQIQHV NAWEHRFNTE TYAQIVGIQS ETVGQDFIGW TSMYDGTDID
     KTEMKEWLEE TIGSIHDKVG GQLGNVLEIG SGSGMILFNL GDSLKHYTGF EPSRKAVEFV
     TGTARSIPSL ANKVEMYKAT AADISKVDQP LQADLVVLNS VVQYFPSQGY LFNVVRDLLK
     VDGVKTLFFG DIRSYALRRE FYAARALFMA GERASQKDLR RLVEDMEQIE QELLVDPGFF
     TSLTHRLPDL VQHVEIQPKR MRATNELSSY RYTAVVYSRS REPPCGGLRT IPDNEWIDFQ
     EQGLNNDSLQ QRIKDVSSTH PLAVSNISHT KTLFGNCLLG ALGDGKARKP VHTDWTAHIN
     RQAKGIPSLS AVDLDEMAKA AGCQVRISWN RQYSQHGGLD AIFYPRQING GSDKAGVMFS
     FPTDHAERRR QTLSNKPMRQ QLVKEVQQQL DELVKVQLPS YMVPQSIQVL NQLPINQNGK
     VDRKALIQRT RTQTEVSQGG LQRELSTAEL KVQRILSRVL GIEASRMGLE DSFFQLGGDS
     IAAMKIVAAA REEEIHLTIA NIFQHPKLVN LATVAQFSQH EGEQKSIQPF SLLSTTQRDY
     LLHAIPENTS NVNGNDIIDI LPTTWMQNLF ISRGVNIQPL AFNYFFLNLG TRVDASRLRS
     SIPTLVQQFS ILRTKFVYVD GVLWQTVLRK PHVPFTEFHL DMSLEEAADT VCLEDSRTTD
     PLELATAFML IRGTSNEHLL AIRITHAQYD GVCFPSFVKA LFAIYSGKSV EPAHNHSTYL
     AYTRERKSVS ALHWRDVLHG SRMTKATPLL SPSIRHGMIP VEVQTESIIG MPHVPTGLTL
     ASLVSAAWAK VLSQITGEED VVYGYMVAGR NANIPAITKI VGPCLNIIPV RARLHAKTTS
     TELIRSIQEQ YIALGEADSM GFDEIVRTST DWPADTEYDS VFQHQNLNEH PEFDFEGTSS
     RLHWFQNPDS VPCILTVVSY PLEDGLRIVV RGNEHIITPE SAERINKLLC ETIGALSSSL
     Q