ID A0A1A0QSH8_9MYCO Unreviewed; 1810 AA.
AC A0A1A0QSH8; A0A1X0CXX6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:ORA64928.1};
GN ORFNames=BST23_15430 {ECO:0000313|EMBL:ORA64928.1};
OS Mycolicibacterium elephantis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=81858 {ECO:0000313|EMBL:ORA64928.1, ECO:0000313|Proteomes:UP000192772};
RN [1] {ECO:0000313|EMBL:ORA64928.1, ECO:0000313|Proteomes:UP000192772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FI-09383 {ECO:0000313|EMBL:ORA64928.1,
RC ECO:0000313|Proteomes:UP000192772};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:ORA64928.1}.
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; MVHP01000017; ORA64928.1; -; Genomic_DNA.
DR STRING; 81858.BST23_15430; -.
DR Proteomes; UP000192772; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
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 InterPro; IPR029058; AB_hydrolase.
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; 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; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; NF040607; mycolic_Pks13; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
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; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
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; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..113
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 134..559
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..613
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1810 AA; 194583 MW; 9F1EF920D11ECA69 CRC64;
MNMADTQDDS QQPEMPSGDD IQLAPEKPLT PPKTDMTVND MREWLRNWIA NATGQSPDAI
NDSTPMVELG LSSRDAVAMA SDIEDLTGVT LTATVAFRHP TIESLATVII EGEPEPAEGS
DDDENWTRDV DEDVANIAIV GIATRFPGDM NTPDQTWQAL LEGRDAITDL PEGRWEEFLG
EPRIAERVAK ARTRGGYLSD IKGFDAEFFA LSKMEADNID PQQRMALELT WEALEHARIP
ASSLRGANVG VYIGSSLNDY SFLAMSDPSV AHPYAITGTA SSIIANRVSY FYDFRGPSVA
VDTACSSSLV AAHQGVQALR SGEADVAIVG GVNALITPLV TVGFDEVGGV LAPDGRIKSF
SADADGYARS EGGGMLVLKR LGDARRDGDD IIAVIAGSAV NHDGRSNGLL APNPDAQAEV
LRKAYKDAGI NPRDVDYIEA HGTGTILGDP IEADALGRVV GRGRTADKPA LLGAVKSNVG
HLESAAGAAS LAKMALALRN NKIPPSINYA GPNPYIDFDG VHLKVADTVT DWPRYSGRAV
TGVSGFGFGG ANAHLVLREV LPSDLVEPEP KPEPEPEKPK PSEANAVYVG GVRMDEYGEF
IDDDDDDDAL DRPAQVTDDE PELPGLTDEA LRLLEIAREE LESAEQPTPV VPLAVSGFLT
SRKKATAAEL ADWIDSPEGR ASSLESIGRA LSRRNHGRSR AVVLARDHDE AVKGLRAVAE
GKQNPNVYSA DGPVTNGPVW VLAGFGAQHR KMAKNLYLRN DVFAEWINKV DAYVQDERGY
SIVELILDDS QDYGIETTQI TIFAIQIALG ELLKHHGAKP AAVVGQSLGE AAAAYFAGGL
SLEDATRTIC SRSHLMGEGE AMLFGEWIRL MALVEYSAEE IETVFADFSD LEVCVYAAPT
QTVIGGPPEQ VDAIIARAES EGKFARKFQT KGASHTSQMD PLLGELAAEL VGIQPHPIQI
GYFSTVHEGK YFRPGEVLHD VDYWKKGLRH SVYFTHGIRN AVDNGHTTFL ELAPNPVALM
QVGLTTAAAG LHDAQLIATL ARKQDEVDSM VAAMAQLYVH GHDLDIWTLF PRGEYANIPP
TRFRRKPHWL EARFTGDSST IMPGNHVAMP DGRHVWEFSP KGEADLAALV KAAAAQVLPD
AKLVASEQRA VPGEGARLVT TLTRHPGGAS VQVHARIDES FTLVYDAVVS RDGAVGALPV
AVATGAAVAQ QVSAAPADEP EEEAAEILQD NLTAGAGLAA GFAKWSPDSG ETIHDRLGAI
VGGAMGYEPE DLPWEVPLIE LGLDSLMAVR IKNRVEYDFD LPPIQLTAVR DANLYAVEKL
IHYAIEHRDE VDQLAEHQKT RTAEEIAAEQ AELMGGATTV AELEQVLAEK TGVASEVTSA
GTATESDIPA PPTDPSGPNI PPPPTDPSGP AVPPPPTDPS GPQGDGPSQS AVAAATKVLT
QEAVTEALGA DVPPRDAAER VTFATWAIVT GKSPGGIFNE LPAIDDATAT KIAERLTERV
DEGTVTVDDV RAAKTVEELA TTVREYLEGG KVDGFVRTLR APKEGSDRIP VFVFHAAGGS
TVVYEPLLKR LPPDTPMYGI ERVEGSIEER AREYVPKLLE LNGDKPFILA GWSLGGVLAY
ACAIGLKEAG ADVRFVGLID AVRPGEEIPQ TKEETRARWD RYARFAERTF NVEIPEIPYE
ELEKLDDEGQ VRFVLEAVKQ SGVQIPGGII EHQRTSYLDQ RAIDTAEIRP YDGKVTLYMA
DRYHDDAIYF EPRYATRASD GGWGEFVSEL EVVPIGGEHI QAIDEPYIAK VGAHMSEAIS
RIESEEKQAK
//