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Database: UniProt
Entry: A0A1Q4VSG3_9ACTN
LinkDB: A0A1Q4VSG3_9ACTN
Original site: A0A1Q4VSG3_9ACTN 
ID   A0A1Q4VSG3_9ACTN        Unreviewed;      1551 AA.
AC   A0A1Q4VSG3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:OKI00761.1};
GN   ORFNames=A6A06_17645 {ECO:0000313|EMBL:OKI00761.1};
OS   Streptomyces sp. CB02923.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI00761.1, ECO:0000313|Proteomes:UP000185893};
RN   [1] {ECO:0000313|EMBL:OKI00761.1, ECO:0000313|Proteomes:UP000185893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02923 {ECO:0000313|EMBL:OKI00761.1,
RC   ECO:0000313|Proteomes:UP000185893};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKI00761.1}.
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DR   EMBL; LWKZ01000024; OKI00761.1; -; Genomic_DNA.
DR   RefSeq; WP_073763507.1; NZ_LWKZ01000024.1.
DR   STRING; 1718985.A6A06_17645; -.
DR   Proteomes; UP000185893; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; 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:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   CDD; cd12117; A_NRPS_Srf_like; 1.
DR   CDD; cd19543; DCL_NRPS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR010060; NRPS_synth.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01720; NRPS-para261; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 2.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185893}.
FT   DOMAIN          978..1052
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1551 AA;  161744 MW;  421C36421804CC6C CRC64;
     MKTSTPATGP ASGKGSALAE VWPLSPLQEG MLFHAGFGDQ GPDVYVIQRT LTIDGPLDAA
     RWRASWQALL ARHAALRASF HRRKSGEAVQ LITREAALPW READLSGLPE ADALAEVARL
     AARECAERFD LGVAPLLRLL LVRLGDGRHC MVLTAHHILL DGWSMPILFD EATTAYAAGG
     DATVLRRTAS YRDYLAWLGR QDKDAAREAW RAELSGDGEP TLVAPADPAR TPVLPDQAGA
     DLPAGLTRAL TDLARRHGLT VNTVVQGAWA LLLARLSGRD DVVYGTTVAG RPPELPGVES
     MVGLFINTVP VRVRLDAGQP VAEMLKNVQA RQSALLPHQH LGLADIQKHA GPGAGFDTLV
     VYENYPRSAA GPGGPGTLTF TTLGLRQATH YPLTLGILPG DRLEVEVSYR PDLVTAGLAR
     ALTGRLVRVL EQLVADPSVP VGRIGVLDAD ERHRAVEGWN VTAAATAGAT VPELFAARVA
     SAPDAVAVAD GRQSVQYGRL DADSDRLAAY VSGSGVRRGD RVAVVMERSA GLIAALLGVW
     KAGAAYVPVD AGYPAERIAF LLADSQPAAV LCTEATRAAV PADVSGQVIV LDDPKVRAAM
     AEAPAVAPRP SVTAGDLAYV MYTSGSTGVP KGVGVPHGSV AALAGERGWE LGPDDAVLMH
     APHAFDASLF EIWVPLVSGA RVAVAAAGAV DAQRVREAVA AGVTALHLTA GSFRVAAQED
     PECFAGLREV LTGGDVVPAA SVARVREACP QVSVRHLYGP TEATLSATWH RLRPGGPVPD
     VLPVGRPLAN RRAYVLDAFL HPVPPDVTGE LYLAGAGLAR GYLDRPGATA ERFTASPFVA
     GERMYRTGDL ARRTPDGDLV FAGRADAQVK VRGYRIEPGE IEAVLAAAPG VAEAAVVARE
     DRPGERRLVG YVVADGRDAD GPEPDGQALR EHVARTLPDY MVPAAVLVLD ALPVTANGKV
     DRTALPAPGF AGKAAGRAPR TAAEDILCGL FAELLGLARV GAEDSFFRLG GDSIMSMQLA
     TRARREGVVF SAQDVFEQET PGALAAVARL ADEVRAAPDA GLGEVAWTPG MTELGAYALS
     SGFAQWMVVT TPAGLRPDVL TGGLAAVLDT HDMLRARVEH ADRGPRLVVP GRGTVDAAAL
     LTRIDAADAP ATALDDLAER AAREATERLD TASGVLVQAV WLDAGPAEPG RLALVVHHLV
     VDGVSWRILL PDLRAACEAL ADGRAPEPEP VVTSFREWAG ALAAQATEER RVAELPDWTA
     VFEGVAPPLG GRALDPAEDT LAGMSRRTWT LPGATAATLV GKAPGVFHCG VHEVLLATLA
     GAVARELPHG ALVVDIEGHG REPAAGADLS RTVGWFTSVH PVRLDVSGIA LDDASRGGPA
     AGELLKRVKE QARAVPGDGL GHGLLRHLNP HTGPELDTLP GAHIGFNYLG RFAGAGRAAA
     TGDAWQPAGT SVVGSSADPR TPAPHALEAG AYVQDGPDGP ELALVLGGPA GLWPDTAVER
     LGRRWLDLLD GLAAHTADPA AGGHTASDFP LLDLGQDEVE EFEAGFTDGA P
//
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