ID A0A2S6GTP0_9PSEU Unreviewed; 3919 AA.
AC A0A2S6GTP0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:PPK68491.1};
GN ORFNames=CLV40_105220 {ECO:0000313|EMBL:PPK68491.1};
OS Actinokineospora auranticolor.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=155976 {ECO:0000313|EMBL:PPK68491.1, ECO:0000313|Proteomes:UP000239203};
RN [1] {ECO:0000313|EMBL:PPK68491.1, ECO:0000313|Proteomes:UP000239203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YU 961-1 {ECO:0000313|EMBL:PPK68491.1,
RC ECO:0000313|Proteomes:UP000239203};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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:PPK68491.1}.
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DR EMBL; PTIX01000005; PPK68491.1; -; Genomic_DNA.
DR Proteomes; UP000239203; 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR CDD; cd08956; KR_3_FAS_SDR_x; 2.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 3.
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; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
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:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 2.
DR Pfam; PF08990; Docking; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF21089; PKS_DH_N; 2.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 2.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00826; PKS_DH; 2.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000239203};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PPK68491.1}.
FT DOMAIN 33..451
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1883..1958
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2224..2633
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3768..3843
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 489..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1962..2004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2053..2126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2140..2223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..31
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 498..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2169..2185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3919 AA; 405183 MW; 35795953E6C33C1C CRC64;
MSVEQKLRDY LKRATTDLRE ANRRVRELED RREEPVAIVG MACRYPGAAD PEALWELLLA
ETDAVGPVPA DRGWDLAELA AAGAVPVGGF LDDVAGFDAG LFGISPREAL AMDPQQRLLL
ECAWAALESA GLDPTGLAGS DTGVFVGTSG QDYPALLAAS GDVAEVAGHI ATGTLASVLS
GRVAYVLGLE GPALSVDTAC SSSLVALHQA VQSLRRGECS AALVGGVTVM STPGAFLEFG
RQGTLAADGR CKPFAEGADG IAWAEGVGVL VVQRLSDARR AGRPVLATVL GSAVNSDGAS
NGLTAPNGPS QQRVITRALA DAGLSSSDVD FVEAHGTGTA LGDPIEAQAL LATYGQDRDR
SLWLGSVKSN IGHSQAAAGL AGVIKTVFAL REAQLPATLH ATQPTTRVDW SSGAVELVRE
RRAWPEVDRP RRAAVSSFGV SGTNAHVILE QGDAAEVVES EEVEVVPLVL SAASEEALRE
YAARLRGMPP APDIDATGQH RQNPNKTIKP VDNSTPEDRG ATATASGARE MAGGNAGGGV
VSGVSGADHG SRTVASWVGR AGQEDHDVEP GATAMALGAR EAVAGNVGGG AVSGVSGADL
GSPTSARRAG GISVADLGFS LATTRARLGY RAVVVGLGAA GLDVVAAGTL RDGVVEGVAD
LDGRVVFVFP GQGAQWIGMA RELLDTSPVF AARIRDCEAA LAPHVDFSLT AALRGGPDAP
SLERVDVVQP ALFAVMVALA ALWAAHGVHP DAVIGHSQGE IAAAHVAGAL SLADAAKVVA
VRSRELTVLH GTGGMASVRL PLADVEADLA DVPGVSVAAI NGASSIVVAG DPAGLDELQA
RWDARDIRNR RIPVDYASHS PQVEAIQDRL RAELADITPG RATTPFHSTV TGTTLDGPEL
DGAYWYRNLR QVVRFEPVVE SLLDAGHDTF VELSPQPVLT MAVQETIDAK DARAVTTGTL
RRDDGGYRRF LTSAAEIHVR GATVDWTPAF PKATAIPLPT YPFRHRRFWP TPATARQDAT
ALGLTPLTDH AILGAAVPLA GGGHVLSGRV SLATHPWLAD HTVGGTVVYP GTGFVDLALR
AGDILARDAI ADLTLVAPLL LPETGATRLQ VTLDGDTITI HSHPEDADPH TPWTLHATGT
LAESTLAALP TQPADASQPE TLSAMSTLDS SSGTASVAAT GAIGTLAEST AESKLAAAHP
VEPADTSRLK ASTLDYPPRE VSIDAPDRRA GSAPDSSSRG QEVAERSVGS AVPFAPRPPE
DARALDTTAS RPRGASPGAP DHHAGATSDL SPRDPEVVEH SAGTPAPFAS GPPENVPPPD
AAGRRAGSDS SSRGRGAVQH PLASAPWPPA NACPLDTTDF YAGLAAAGLA YGPLFRGLTA
AWTHDDSLYL DVTLPDAAAR AHHVLHPALL DAALQGIALA ADGPARVPFS FDGVTLHATG
ASRLRVRLTP TTPDAVELTA VDDTGAPVLT IAAVSLRPVD PAAFTATAEP LLEPRWTPVE
LPVAEHASDA RVLTVTGGDP RVQLHKTLAA IHDTLSGDGR LVVRTTTRDI ASAAVLGLVR
SAATENPGRI VAVDSDAESS HLLPAALASG LPEVALRGGT AHVRRLVRLA GAPGKRPIKD
GTVLITGGTG HLGGLLAQHL RTRHGVRDVL LLSRTGRAPN TEPGVRALAC DVTDRGALAA
AIADAGPIAA VFHAAGVLDD AVVTGLTPDR VDHVLSAKLD AAQWLHELTL PHDPSHFVLF
SSVAGLLGSA GQGNHAAANA ALDAFAEYRH SLGLPATSLA WGPWEGGKVG ALTTTDTARM
ARSGLRLLTA TSGMALLDTA LDSDRPILAP VLVGGPATIP DQVPPLLRGL IGTPRRQART
ADTPKPNDLA ATLAALPEDE RHTTLTDIVR RQVAAVLGHD SIREIGHRRT FKDLGFDSLT
AVDLRNRLAT TTGLRLRASL VFDYPDVTTL TAHLLKNLTR SAADPTRATR GRTAEPAHAA
GSAGATRSVD AAHATDSVGS GRIGDAARAA GSAGATRSVD AAHAAGSAGA THSADAARVA
GSAGATHSAD AADAASSAGS GHSVDAAHAT DSVGSGRIGD AARAAGSAGS GHSAGPVRTV
DPSGLGSPAA PTEPGRAAEF AGTTQSAEPS LVANPAWHGR TAQPARVADS AEPTRTADPA
PNPAQPNEPA EAKLTQATRP HTSSPAADFG QPPAEQPGEP PVFHSTAQDR RNGQVSEPPV
DNSPGAIAIV GMACRFPGGV DSPAALWELV EAEVDAIGPF PSDRGWAATD GLGGFVHTAA
EFDAEFFGIS PREATAMDPQ QRWLLECTWE ALERAGVDPH GLRDSDAGVF AGLSHSVYQS
AGGGLGEASG FAVTGTSPSV ASGRIAYVLG TQGPTMSVDT ACSSSLVALH LAVRALRAGE
CGLAIVGGVA VMATDGLFAE FEMQGGLAAD GRCKAFADAA DGTSWGEGAG VLVVERLEDA
HRAGHEVLAV IRGSAVNSDG TSNGLTAPNG PSQERVITRA LADADLAPSE VDAVEAHGTG
TRLGDPIEAQ AILATYGQDR DRPLWLGSVK SNIGHTQAAA GMAGLIKLVE SLRHGTLPRT
LHVDRPSTHV DWTEGAVEIL TETRPWPATG RPRRAAISAF GIGGTNAHVI LEHTPTQPPT
PADHAEPVPL VLSARTPAAL SDQARALKET LAKQQNWNRT AVAHRITTTR ARFDHRAVVL
ANDNESVLDG LAAIAAGAPE IHGTARPGAR PVFVFPGQGS QWPAMAVELM ARPVFRAAIE
DCATEIDRFT DWSLLDTLTR AEPLDRVDVV QPALFAVMVA LARLWRAHGV TPGAVIGHSQ
GEIAAAHVAG ALSLRDAAKV VTRRSQALRA LSGQGGMVSV TLSAARVEEL LTAGLSVAAT
NGPQSTVVSG DAEAITAFLA ECEKRDVRAK RVPVDYASHS AHVERIHSEL LTTLDDIRPR
TGDIPFYSTV RGRRIDTAEL TTAYWYDNLR LPVRFDEVVR ALLDRDHNVF LEMSPHPVLT
FGVEGTIDDV DAPAAALGTL RRDHGGPDEF RAALARAHAH GVEPDWATLF PANPTGPVPD
LPTYRFQRKH FWPRGSAAAP TAPDPSGHPF VRDVVDLPGT DGLVLRGRVS TATHPWLADH
AVSGTVLFPG TAFVELATTA AARAGHPHLD ELTLAAPLVL PPGATVDLQV SVGAPDDGRR
PVELFSRPAD APDGTPWTRH AAGHATRQAG PAADFPWPPT GATEIDVPAL YAAVAQAGLH
YGPSFAGLRQ AWRRGRELFA EVALPEQDEH TARGFRLHPA LFDAALHALG APGDTPDPDA
RVALPFSWTG AHLADTGRAT ARVRLARADD GAVTITLADD LGQVIAHVDA LVLRPVDPAR
LTAGSRAAGG LLGVEWTPVD LPPAPGPVPL RIVTLESGSP ADSAVRALEL VREPHAEHLA
IVTGNAVAGA RPDPALAAAW GLVRSAQTEQ PDRFLLVDTD GPTPHDTLAR AIAAGETQLA
LRAGRPHVPR LTPLPPAEPR PFTPAGTVLI TGGTGGLGAR VARHLVTAHG VRSLVLLSRR
GPDAPGAAEL VAELPAISIV ACDVTDRDRL AAVLAEHRPT TVIHTAGALD DGVIGSLDRD
RVERVFAAKV QGALNLHDLA TDVDRFILFS SAAGVLGGAG QGNYAAANAA IEALAQRRRA
DGLPATAIAW GPWASATELT GGLGEAGLAR LARAGTIPLT DDDGLALFDR ALAADAPVVV
ATRLDLSALR ARGPAPIWHR LVPPTTAAAQ PKSVADDLRA MPAAKRAEAL AALLRSHVAD
VLGFTAADEI DEQRPFRDLG FDSLTAVELR NRLTAATALR LPPTLVFDHP TPKALVAHLL
AELAPDQDSS VLDDLDRLET ALSGLDRDDL LRTTALARLT ELIGRWGTPT PTGTAEPVDV
PDADLFEVLG QRYGAADAD
//
