ID   L7UC15_MYXSD            Unreviewed;      1508 AA.
AC   L7UC15;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:AGC45618.1};
GN   OrderedLocusNames=MYSTI_04320 {ECO:0000313|EMBL:AGC45618.1};
OS   Myxococcus stipitatus (strain DSM 14675 / JCM 12634 / Mx s8).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=1278073 {ECO:0000313|EMBL:AGC45618.1, ECO:0000313|Proteomes:UP000011131};
RN   [1] {ECO:0000313|EMBL:AGC45618.1, ECO:0000313|Proteomes:UP000011131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14675 / JCM 12634 / Mx s8
RC   {ECO:0000313|Proteomes:UP000011131};
RX   PubMed=23516218; DOI=10.1128/genomeA.00100-13;
RA   Huntley S., Kneip S., Treuner-Lange A., Sogaard-Andersen L.;
RT   "Complete genome sequence of Myxococcus stipitatus strain DSM 14675, a
RT   fruiting myxobacterium.";
RL   Genome Announc. 1:E0010013-E0010013(2013).
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DR   EMBL; CP004025; AGC45618.1; -; Genomic_DNA.
DR   RefSeq; WP_015349878.1; NC_020126.1.
DR   STRING; 1278073.MYSTI_04320; -.
DR   KEGG; msd:MYSTI_04320; -.
DR   PATRIC; fig|1278073.3.peg.4387; -.
DR   eggNOG; COG1020; Bacteria.
DR   HOGENOM; CLU_000022_2_4_7; -.
DR   OrthoDB; 9757540at2; -.
DR   Proteomes; UP000011131; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd12115; A_NRPS_Sfm_like; 1.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   CDD; cd05235; SDR_e1; 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; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.10.10.1830; Non-ribosomal peptide synthase, adenylation domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
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; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   InterPro; IPR041464; TubC_N.
DR   InterPro; IPR044894; TubC_N_sf.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01746; Thioester-redct; 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; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF18563; TubC_N; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
FT   DOMAIN          1033..1108
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1508 AA;  163915 MW;  445027B11B2CF9B7 CRC64;
     MNIREFLVTL TQKGVGLRAD GDKLVVQAGK AVLSPELRAE LVARKGEILA FLQKHTGQGS
     DAPQAPTRPE VLPLATGQER LWFLDRLLPD TAQYNVHLGL RVRGALDVPV LRRSLDEVVR
     RHEVLRTRFP EVDGTPRQVI APAESGAELT VIERLGLSEQ AREAELIRCS EELSRKPFDL
     SSGPLLRVTL VAVGPDDFGL FFTQHHIITD GWSLGVLIRE FSALYGAHAR GQPSPLPPVS
     MQFAEAALRE QSWLRGDAAA RERAYWKEKL TGLPQLQLPV DRAVALQTYR GAVLPFHLTE
     ALGADLKELA RREGCSLFMV LFSALAALFH RYSGQADFGL GTVVANRGAV PPGLIGFVAN
     TLALRCDLSG DPTFAQWLAR ARTVVLEGMD HQELPFSEVV QAAGAPRDGG FNPLVRACFT
     LENIPAPTLD LPGTKWSFLR GAPDGSVEGT AKFDLALIMA TAERGLAGML EYSTELFDAR
     TAERMVGHFQ VMLEAIVAHP EARLSKLPLL TQEERNQVLV EWNDTAFPVP STSIHGLVEA
     QVERTPEAVA LVSGPRRITY EELNRRSNQL AHHLRRLGVG PEVRVGICVE RTEDVVIGLL
     GILKAGGAYV PLDPAYPKER LALILEDARV PVLLTQRRLL TDLPEHSAHV LCLDSDRPVL
     DAERTERPAG GAGPENLAYL IYTSGSTGRP KGVMIEHRGA VAFLVWATRV FSGAQLAGTL
     ASTSMCFDLS VFEMFAPLCV GGTVIVAKNA LELPELPSAR EVTLINTVPS AMNALLLAGA
     VPPSVSTVNL AGEALGAALV ERIYQLSHVQ GVFNLYGPSE TTTYSTWTRV ARGEHVLIGR
     PVGNTQVYVL DANLEPVPPG VPGEVFIAGL GVARGYLDRP ELTAERFVRS PFGTEDGARM
     YRTGDLARWL PDGRLDYLGR MDHQVKLRGF RIELGEIGAV LVKHPGVRDA VVVVREDPGA
     EKQLVAYVVA RGEQPLDPAD LRNHLKTRLP EYMVPGIFVR MESLPLTPNG KVDRKALPAP
     DGARAGTTKA YVAPRTPDEE ALATVWREVL RVDKVGIHDS FFDLGGSSLS LYQVLTRVRA
     ACSVELTLRE LLQAATLEDL AKMVEAVRSG VRVVRETQAD MAADAVLEAD IDPRGLPAPR
     TLPPRTLLLT GATGFLGAFL LEELCRKTDA NIWCLVRCSD ARDGMRRIRK NLEGYSLWSD
     ALAARIVPLR GDIGKPMLGL SEAEFERLSS EVDVILHNGA LVNFLYPYEG LKAANVLGTR
     EILRLATRTR VKPLHYVSTI SVLASGRSEA IREDEPLGPP GSVAGGYSQS KWVAESLVRE
     ASRRGLPVSI YRPGRITGHS QTGAWGAEDL LCRTLQACVR MGAAPQVDAM IELTPVDYAS
     RAIVGLAAHP ESLGQTFHIV NPRTVRATTL WSGMQAFGYP LRILGFDAWL TELAAAQASD
     AVLMELHSIL QQVPPEDRTA SGPRMAVCDS QNAVKALESL GTSCPQVNDT LLSTYLASLV
     RRGFISAP
//