ID A0A069K7W4_9ACTN Unreviewed; 1102 AA.
AC A0A069K7W4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KDQ69997.1};
GN ORFNames=DT87_23240 {ECO:0000313|EMBL:KDQ69997.1};
OS Streptomyces sp. NTK 937.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ69997.1, ECO:0000313|Proteomes:UP000027475};
RN [1] {ECO:0000313|EMBL:KDQ69997.1, ECO:0000313|Proteomes:UP000027475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ69997.1,
RC ECO:0000313|Proteomes:UP000027475};
RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT producer of the benzoxazol antibiotic caboxamycin.";
RL Submitted (APR-2014) 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:KDQ69997.1}.
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DR EMBL; JJOB01000001; KDQ69997.1; -; Genomic_DNA.
DR RefSeq; WP_051673824.1; NZ_JJOB01000001.1.
DR AlphaFoldDB; A0A069K7W4; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000027475; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
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; IPR018201; Ketoacyl_synth_AS.
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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
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; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..457
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 964..1038
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 924..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 114999 MW; A6610DB6671216D9 CRC64;
MTENGGSAEA LSAALTAVRG LRARVEELGR GRREPIAVTG IGVRLPGGIG SPADLHEALA
AGRDTVRELG TVRWDHDALH DPDPEALGRT HMRHAALVDD VDRFDARFFG ISPREAARID
PQQRLLLEVA WEAFEDAGLP AERLAGSGTG VYVGANSSDY LAMQLARPET VDLYSVVGGT
NCIIANRLSY QFDLRGPSMA VDTACSSSLV AVHLAVQSLR SGECDAAVAA GVNLLLSPAS
SVAHSKGLPL SPDGRCKTFD AAADGYVRGE GVVAVVLKRL TDAVNDGDRV YAVIHGTAVN
QDGRTNGLTA PSGRAQRECI TAALRAARVE PGQISLVEAH GTGTSLGDPI EVEALAEVYG
AVDGPTCRLG SLKTNMGHLE AAAGLAGLVK AALATYHRKV YPTLHLRTVN PRLEIAGTRL
AFAGDEVRPW DEDDEHRMAA VSAFGAGGTN AHAVLGPPPV SVQTSQAGAS EATAPAVDGP
FTLRLSAATT EGLEGLADRY ADLLADANAA RVRAVAAATD HRRALLPQRL SVSGATPQEM
VAALRTAAEG EPGPAGVTGS AKGTGGIVFV FPGQGPHWLG MASGLRTASP RFDAALDEVD
RAMRPFLGRS VQELIDHGDE GKLPTRFVQP ALFAIAVGLA AMWREAGVEP DAVVGHSMGE
VAAAHVAGAL SLTDAARIIC ERSRLLSRID GQGRMLVVGL GRDAARELCS VYDDICVAVI
NSPHSTVLSG GADSLERVAT QLAERNVFAK FVHVDVASHS PQTDALQPAL RTALAGIRPL
APKVPLVSTV SGAPLTEGPD AEYWCDNLRA PVRFTDAVAA LLAQGCDTFV ELAPHPTLID
ALEGLCAGTG AAATWTLHRD LPDAVARERA SGFLYAHRRR GPWPHRAGEH RAPAPMVALP
TYPFQRERHW FTEDQWAHPW PEPGIPGQRT AEPFTGARKP GNSGASGTPR PVDPSGAPGG
WTVAQVVEAV DQAIAETLGL TAGTLDVDAG FFSLGMDSML AARARSRLSR AFGLTLPTRL
LFEHPTAAEL AACIAQLLNA RQGHVTAARA IPQARSGATA ATSAPAAGAA PVGTGTALTD
EDVIRALESQ LRRSHPTHGG HA
//
