ID A0A0L0KGF5_9ACTN Unreviewed; 1730 AA.
AC A0A0L0KGF5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KND37222.1};
GN ORFNames=IQ63_09850 {ECO:0000313|EMBL:KND37222.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND37222.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-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:KND37222.1}.
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DR EMBL; JPPY01000068; KND37222.1; -; Genomic_DNA.
DR RefSeq; WP_050370296.1; NZ_KQ257813.1.
DR PATRIC; fig|42234.21.peg.2030; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000037151; 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; cd08955; KR_2_FAS_SDR_x; 1.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
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; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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.
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:UP000037151};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..435
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1652..1728
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1016..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1730 AA; 181178 MW; 98441F05B6CD84A8 CRC64;
MTGTSQEQGD GEPIAVVGLS CRFPGDADSP EAFWDLLVQG RDGIGDGAER WAPYAGTGPE
HAAVVRETPT RGGFLADIAG FDAEFFGIAP REAELMDPQQ RLLLELAWEA LEHAGLPPLG
LGGTDCGVFV GVGSDDYGRR LLEDLARIEP WTGIGAALCA TANRISHSLD LRGPSLAVDT
ACSASLVGVH LACRSLLAGE SDVALAAGVN LMVAPGLSVT LARAGATSPD GHSKPFDASA
DGYGRGEGAG VLALKRLSDA ERAGDRVLAV IRGSGVSQDG RTAGIMAPNG EAQADLLRRT
YAQCGIAPQS VDYVEAHGTG TVAGDPLEAG ALAAVFGAGR PADSPCLIGS VKGNIGHLEA
GSGIAGMIKT ILALVHEEIP PSVHFSAPNP RIPWAEARLR VTRERTPWRR GERPRRAGVS
SFGYGGTIAH VVLEEAPTAS HREEAPAASQ GALPRLFPLS GRSEAAVRED AARLADWLDG
PGSDIALASV AQHLGTRRSH LERRVAVVAA DRAELAGGLR RFAAGDAAPG LVEGAVTDEG
LDDVVWVFSG TGAQWPGMGR ELLATDAVFA EVIERIGPVF AEEFGTTARK LIEDGDVSRV
DVAQTMIYAV QMGLVAVWRS LGVRPAAVIG HSMGEIAAAA TAGVLSLEDG ARLVCRRSVL
LRRVAGAGGM LMIGLPADEA EARLGGTDGV VPAVLASPTT TVVAGAVAEI EALARDLASD
RSLLVRRVDS DVAFHSPQME PLLKELAEAA ADLTVHAPRI PVYSTALADP RDTALRDGAY
WAANLRSPVR LSGAVSAAAE DGFRTFLEVS AHPVVRHSVQ ETLDTVGADR HCLAASLRRD
TGERQHLLLN AGLLYCHGVP LDWPSAPDAR PLSLPVRSWR RQRFWRDLPV HRADRGRHDP
ASRTLLGPRT TLAGTTPLDL WRTRVDLESR PYPGSHTIHG AEIVPAAVVL QTFLDAAGVS
GLSDVSFDLP LALSTAQDVD VIAQDGVLRL LSRTAGPKEP DPDGDEGPAL THAVASVSDD
ASPPLRPTTA EPGTALPHDQ ITTHLASVGV PSMAFPWRVE RLERVPDGLR ADIVASDEPA
SWAPLFDAAL SMAAVAFPGP AALRVVAGVG RVWTTAEPPP RARLEAYVDG GDTVNVRIAA
DGDRTVAVLS GVRYAGGETQ ARSTPPGELL FRTDWKPLPL DAPRPHRPLV LVGADGELTA
ALRATADGLG VPCLAAESPD GLDGLRGQVP GPVDVLLLPL PDRPAGETEV AERAVREAWQ
LASAARLLGA WPPGTARLWS LTCGVREADR LEAVAQAARW GLGRVVGGEH PELWGGTVDL
GPRPTGDDLA AVLRVVAANP GEDVVAVREG GAWANRLVRS VNAEGAPLRC RQDGTYLVTG
GLGSLGGEIA RWLVERGARR LVLAGRSALP PRSEWDAVTD EVQARRVATV RRLEALGATV
RVVSLDLSDA EAAAAALTPD ALGMPPIRGV VHAAGVLQDQ LVDGLDADAL AAVMRPKAGG
ALTLHRLFPP GSLDFLVHFS SCGQYLGLTG QAAYASANAF LDAMAGYDHT LGAVGSMSLA
WTSWRGMGMA ANAAVDAELQ AHGVGDITAP EAFAAWDLAG RTGAASLAVL RTVPLPGGVR
RTGLLRDLSE EAPAREAAAG ALPSEELSEE ELRALLHEQT VSVIVSEMKL DRAQLDPDRS
LLKSGLDSVM AIVIRRRLER LLERKLPANL VWHQQTVTAI VNYLVTSARS
//
