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Database: UniProt
Entry: A0A364K3A0_9BACL
LinkDB: A0A364K3A0_9BACL
Original site: A0A364K3A0_9BACL 
ID   A0A364K3A0_9BACL        Unreviewed;      1057 AA.
AC   A0A364K3A0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RAL23310.1};
GN   ORFNames=DL897_11475 {ECO:0000313|EMBL:RAL23310.1};
OS   Thermoflavimicrobium daqui.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Thermoflavimicrobium.
OX   NCBI_TaxID=2137476 {ECO:0000313|EMBL:RAL23310.1, ECO:0000313|Proteomes:UP000251213};
RN   [1] {ECO:0000313|EMBL:RAL23310.1, ECO:0000313|Proteomes:UP000251213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL23310.1,
RC   ECO:0000313|Proteomes:UP000251213};
RA   Wang X., Zhou H.;
RT   "Thermoflavimicrobium daqus sp. nov., a thermophilic microbe isolated from
RT   Moutai-flavour Daqu.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RAL23310.1, ECO:0000313|Proteomes:UP000251213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL23310.1,
RC   ECO:0000313|Proteomes:UP000251213};
RA   Zhirakovskaya E.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004789}.
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:RAL23310.1}.
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DR   EMBL; QJKK01000006; RAL23310.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A364K3A0; -.
DR   OrthoDB; 9765680at2; -.
DR   Proteomes; UP000251213; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 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   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   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000251213};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          33..448
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          946..1021
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1020..1057
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1057 AA;  115927 MW;  D1801E4F94814A03 CRC64;
     MTQRADARSP AALALESLQK AKKRIIELET QRSEPIAIVG MACRFPGNAN TPDEYFHLLN
     EGHDCVCEMP SSRRLAISQT SIKAGWLEKI DEFDADLFGI TADEANYLDP QQRLLLHVAW
     EAFEDGGFAI DRLFGSKTGV FIGISTQDYL YELLRTPNVA NQAAVVTGNG HCFAAGRLSY
     VFGFEGPSLA VDTACSSSLS AVHLACQSLR LRESDLAVAA GVNLLVSDQT TQMIDATKAL
     AADGRCKAFD EQADGFVRGE GCGVVLLKRL SDARRDGDRI LALIRGSAMN QDGRSMGITA
     PNVLAQTQLI RTALNNARVS PAEVSYVETH GTGTAIGDPI EVDALRNVFD QDVSSKVPCI
     LGAVKTNVGH LEAAAGIAGL IKTVLALQHE VIPKNLHFHR LNPLIDLDHS RFAIPTESIP
     WTKGETPRIA GVSSFGMSGT NVHLVLEEAP ERVNSPQVER IRPCHLLTLS GHSKTTLLKK
     AAELAEFLKE SPAVHIKDVA HTTNTGRVHL SYRSAVVGSS HKEIIPLLES MAKGDDRADE
     LMSQVHQQDH RPKVAFLYSG QGSQFPAMGK ELYQTHPVFK KMVDRCAKIL DPLLGSSIVS
     LLLSEELGSQ IHEIGNAAPA QFVLQVALTE LWKSWGITPD VVAGHSVGEY AAAWAAGVFS
     LEDALRLVAA RCSLMQGLPK EGAMVSIAAS REQVAEVMKP YSDQVSIAVV NTYDQIVISG
     KNEAVLQIVE QFEKEGIQTK KLEISHASHS PLMSPILEDF RKVAESVTYH TPAVPYVSNM
     TGDLESDLIM NVDYWVEHLI RPVVFVEGMN KLKQLEVECF VEIGPHRTLL SFARDVHVDA
     IGIPSMERDQ PVWPTIANAL AQLYRMGAHI DWTEFDQPYG CQKIRIPTYP FESRKYWASE
     LSYPTARNIS QTKPEAVASL DLPVSQDTSE IVASDDSTTS QEEQKIFLSP VESSIARHFT
     ELLGRKFIDP QTNFFAIGGD SLLATRLTSR LRDEFKVHLE LGSVLKAQTV QKIAKKIKQL
     QEDGKNSDNM SLGPIKRVNR NRAKNHQTSN HDRSSKI
//
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