ID V6KLT9_STRRC Unreviewed; 1303 AA.
AC V6KLT9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EST33057.1};
GN ORFNames=M878_13795 {ECO:0000313|EMBL:EST33057.1};
OS Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST33057.1, ECO:0000313|Proteomes:UP000017984};
RN [1] {ECO:0000313|EMBL:EST33057.1, ECO:0000313|Proteomes:UP000017984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS 12.976 {ECO:0000313|EMBL:EST33057.1,
RC ECO:0000313|Proteomes:UP000017984};
RX PubMed=24407645;
RA Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT 12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL Genome Announc. 2:e01147-e01113(2014).
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:EST33057.1}.
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DR EMBL; AWQX01000117; EST33057.1; -; Genomic_DNA.
DR RefSeq; WP_023546758.1; NZ_CM002285.1.
DR STRING; 1352936.M878_13795; -.
DR PATRIC; fig|1352936.5.peg.2907; -.
DR HOGENOM; CLU_000022_16_6_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000017984; Chromosome.
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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0033068; P:macrolide 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; 3.40.50.1820; alpha/beta hydrolase; 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; 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; IPR020802; PKS_thioesterase.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08990; Docking; 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 Pfam; PF00975; Thioesterase; 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 SMART; SM00824; PKS_TE; 1.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000017984};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..458
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 944..1018
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 460..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1303 AA; 138137 MW; 2C9D063EE32CD0C5 CRC64;
MTGTEEKLVD YLKKVTAELR ETRRQLHSAT SASREPIAIV GMACRYPGGV RSPEDLWRLV
LEERDAISGF PTNRGWDIEG IYHPDPDRPG TCNAREGGFL HDAALFDADF FGISPREAQA
MDPQQRLLLE TAWEAFERAG IDPTSLRGSD TGVFAGVVHH DYATAQVPDT LEPYLVTGLS
GGVASGRIAY TFGFEGPAVT VDTACSSSLV ALHQAAHALR SGECGLALAG GVTIMATPRA
FLSFSRQRGL SPDGRCRAFG AGADGTGWAE GVGMLLVERL SDARRNGHPV LAVLRGSAVN
QDGASNGLSA PNGPSQQRVI RKALAHGGLA ARDIDVVEGH GTGTKLGDPI EAQALLATYG
QERDADRPLY LGSMKSNVGH TQAAAGVGGV IKMIEAMRHG ILPKTLHADE ATPHVDWSAG
AVELLTSRRA WPETGRPRRA AVSSFGISGT NAHVILEAPP EAPEPDTAAG PTAAGTVGDG
SRDAVPSLVP WPLSGRDAGA LRDQITRLRE SVEETSADPV DVSHTLARRA AFRHRAVLLR
GGATIREIRG VARPGGTALL FSGQGSQRLG MGRELYETHP VFAESFDAVA EHTGLPLKEV
VFGAAQDGLL DQTRYAQVAL FAVEVSLYRL IRSLGVDVHA VVGHSVGEVA AAHVAGVMSL
EDACRLVEAR GRLMQALPAG GAMAAVEVSE AEASAALAGL EDRVALAAVN GPVSVVLSGE
EAEVRKLVDA WREQGVRTHQ LTVSHAFHSP LMDPMLAEFR EVVAGLELHE PVLAGLPAEV
VDPEYWVRHV RRPVRFADAV ARVCEAGAVR WLEVGPGGVL TALAQKIVPD AQDQVFAAAL
RADRPETESL VTALAQVHVD GGTVDWSRLI DGRGTLVDLP TYPFQYRPYW IEDQPFPTTT
PASPFANLSS GHRVDEAAGN GAGTPDGGKA GGLLAGLTGA ERLSAVTELV RAEASETLCH
TGTTITADRT RQELGFDSLT AIELRNRLSR ALGLPLPTTL VFEHDDLASI AAFIDARLED
VSSGRCVDDG RFGADGSGLL TELFREAAAA GRIEDAIPLT EAAARMRKTF TDPADPAVRR
VPVWLGRGAA LPTVVCLPSF SAIAGVHVYA RFADGFSDAW KVAALAHPGF FPGEPLPDSV
EVLAELHART ILEMTEGSPL LLVGRSAGGW VAHEVAAALE RMDKAPTGVA LLDTPASGDD
PRGHGVMVGG MLERDSRLVT VDDYRLTAMG AYARLFSDWK PEPNAAPTLL VHAATPYGAD
ETRIASWHLP HDIAEVTGDH FTMLEEHSTT TAEAVERWTR SLL
//
