ID A0A2V2Q1P0_9ACTN Unreviewed; 2153 AA.
AC A0A2V2Q1P0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:PWS42997.1};
DE Flags: Fragment;
GN ORFNames=DKT74_19155 {ECO:0000313|EMBL:PWS42997.1};
OS Streptomyces sp. ZEA17I.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2202516 {ECO:0000313|EMBL:PWS42997.1, ECO:0000313|Proteomes:UP000245984};
RN [1] {ECO:0000313|EMBL:PWS42997.1, ECO:0000313|Proteomes:UP000245984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZEA17I {ECO:0000313|EMBL:PWS42997.1,
RC ECO:0000313|Proteomes:UP000245984};
RA Chen X., Qin K., Li H., Cortesi P., Saracchi M., Sang W., Yang M.;
RT "Genome sequencing and identification of chitinase family genes of
RT Streptomyces sp. ZEA17I, a biocontrol agent against plant pathogens.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:PWS42997.1}.
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DR EMBL; QGMS01001189; PWS42997.1; -; Genomic_DNA.
DR Proteomes; UP000245984; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd17646; A_NRPS_AB3403-like; 1.
DR CDD; cd12117; A_NRPS_Srf_like; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
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; 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; IPR001031; Thioesterase.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 3.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 752..826
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1797..1872
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 730..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PWS42997.1"
SQ SEQUENCE 2153 AA; 231285 MW; DBC6BDD694AC6B65 CRC64;
VRDERGAVAP FTVPAEVAGR LSRLARERGA TPFMAALAAF QVLLGRYAGS TDIAVGTPVS
GRDRTETQDM LGLFLNTLVL RTDLSGAPGF GEVLNRVREG SLDDYGHQEV PFERLVDALA
PERDPSRTPL FGAMFLWDGA DGPSSEAHAG GADSLVVERL AVGESTAKFD LTLGVAEQPD
GSLSGGLNYA TALFDAATAA RMADHFVRLL TAAVAEPDVP VAELELMSPA ELEQVVHRWN
ETDVPFPTGT LHGLFEAQAA ATPDAVAVAD EDGTLGYAEL DRRAEAVADA LRAMGAGPGT
VTGVCLERSR GLLVALLGVL KAGSAYLPLE PDLPAERRRY MLSDSGARVV LTDTGAGPDG
VPEDVAVVPL ARGGMLPDGA PALPGGSSGP DDAAYLIYTS GSTGRPKGVL VEHRAIVNRL
HWMQREFGLD ATDRVLQKTP MGFDVSVWEF FWPVITGATL VMARPGGHRD PAYLARTIAE
RSITTLHFVP SMLRAFLAGP VPALPSVRRV VCSGEALPGD LVTAAVERLG IAPHNLYGPT
EAAVDVTHAP CVPGERVTIG RPIANTRTYI VDAALRPVPV GVPGELLLGG VQLARGYPGR
PALTADRFVP DPFGGEPGGR LYRTGDLARY LPDGTIDYLG RMDHQVKIRG QRIELGEIEA
VLHEHPSVSA AAVTVHDGRL VAHLVGHPSP EAGAPDTDAV RTWLRERLPD AMVPGDWTVL
DALPLTASGK TDRKALPAPD RSRESRAGEY TAPRTPVERT IAEELAAALD LDRVGVHDRF
FDLGGDSIRA IRAVGALTAR GLALSVQHLF THPTAARLAT VATETTGTGQ GPELVAPFAQ
LAPADLERLP DGLADAYPLG EVQAGMVYEL LADPDANTYQ NVSSFHFTDD GPFDLPALRE
AVRRLVDRHE ILRTSFRLSG FSGPLQLVHE KAGAEVGFTD LRELDPAGQR AAIAEFRAAE
QRLPFDLERA PLLRYHVHRT GERTWTLTHT ECHAILDGWS HHSVIQEIRA DYGRIREDAD
CAVTPPPRAR YADFIALEQR ALDSSEDRAF WQSRIDGFPR LELPAPTAPA EADGPAHEVR
VSWAGLDPEL RALAARTGTS LKTVLYTAHL TLLGLISGQR RFFAGAVCNG RPELPDGDEV
RGMYLNTVPF AVDLRAPSWE ELLRAVFAEE AAVWPHRRYP LPAMQREWGA GVPLVDVIFG
YLDFHVLDQS GSAPEAVTDS SPNEFTFDVW TFPGELRMTC RPGWADRARL ETMAAAFVEV
LRTMAERPES SPASFRATGL TGDAAGAVPR RLPPEVTLPE LIGRGADPEA VALVDRGSAV
TYGQLEERAN RFARLLRARG VRAEDPVAVC LERGAETVVA LLGVVKAGGC YVPVDPEYPE
ERIGYLLSDS GARLLVTRSD LAGRLPGNVP TVLLDTARDE LEAQSPTAPE TGVSPDNTAY
VIYTSGSTGR PKGVQITHRN VVRLVHDENH AAIGPRDTVL VVSPLAFDAS AFELWGTLAN
GGRLAFAPPG TPTTAGIAEV LREHGVTVAF LTTSLFHLMV ESCPDALTGL RTLLTGGDVL
SAGRVRAALG HGLRVSNMYG PTECTTFATG QHAITLEQTD RPIPIGPPIA HTTALVTDED
LVPVPYGVAG ELLLGGPGVA RGYLGRPELT ADRFVPDPTG TWPGGRLYRT GDLVRQDPDG
VLHFLGRRDH QVKVRGHRIE LGEVEAGLSG LPGVHEAAAA VRPGPDGDKQ LVGYIVPEEH
SGFDPALLRA ALRAKVPGFL VPSAWVRLEE LPLNANGKLD RAALPAPDGG TAGEMVAPRT
AAERALAEVW AEVLNLEQVG VHDDFFLLGG HSLLILRAIA LLRERHGLEL TVRAFVEHHT
LDAIAAAAER GDYGDTSRTA LMWLRAEGDR APLFCVHPGG GSAHWYQRLI PHLAPDLPVA
ALEWPGLQSG PGLPVPTASE MAQRYVAEIR AARPHGPYRL LGWCGGSGIT AEMADRLRAD
GEEVTFVLLD PGLDSHERQG LWEEFRLIES CTAKLEELAA AGPEEDTGAL REEILKLLDH
LVDDADPETG IVLPEHNGAD VWLPSARIWR EVMEMTLTYR HHHVPGTLHL VISDELARGE
HEVALGQSYE EYLSRWRELN SGVEVHRVPG DHFGVMRLPH VTSLASTLAS VLD
//
