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Database: UniProt
Entry: G5JUF8_9STRE
LinkDB: G5JUF8_9STRE
Original site: G5JUF8_9STRE 
ID   G5JUF8_9STRE            Unreviewed;       986 AA.
AC   G5JUF8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Beta-ketoacyl synthase, N-terminal domain protein {ECO:0000313|EMBL:EHJ51803.1};
GN   ORFNames=STRMA_0781 {ECO:0000313|EMBL:EHJ51803.1};
OS   Streptococcus macacae NCTC 11558.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=764298 {ECO:0000313|EMBL:EHJ51803.1, ECO:0000313|Proteomes:UP000003573};
RN   [1] {ECO:0000313|EMBL:EHJ51803.1, ECO:0000313|Proteomes:UP000003573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 11558 {ECO:0000313|EMBL:EHJ51803.1,
RC   ECO:0000313|Proteomes:UP000003573};
RX   PubMed=24625962; DOI=10.1093/gbe/evu048;
RA   Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA   Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT   "Phylogenomics and the dynamic genome evolution of the genus
RT   Streptococcus.";
RL   Genome Biol. Evol. 6:741-753(2014).
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:EHJ51803.1}.
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DR   EMBL; AEUW02000001; EHJ51803.1; -; Genomic_DNA.
DR   RefSeq; WP_003079052.1; NZ_UHFV01000002.1.
DR   AlphaFoldDB; G5JUF8; -.
DR   STRING; 764298.STRMA_0781; -.
DR   eggNOG; COG3321; Bacteria.
DR   OrthoDB; 9765680at2; -.
DR   Proteomes; UP000003573; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; 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; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 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; 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; 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; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..428
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          907..982
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   986 AA;  109951 MW;  DB24F46B7DEC7668 CRC64;
     MEDENLIAVV GMSGRFPQAD SIDKLWENLL MGKECLQHFT REELLDEGIA QEDIDSDNYV
     KVKGIIDSPN AFDTEFFEYT VKESMLMDPQ ARVFMEEVWK AIEDSGHAVS QYKGKIGVYA
     GSGMNTYLLR AMQRGLLDQY EDFDIMLGSD KDLLSTRVSY KLNLTGPSVS IQSTCSTSLV
     SVHFACQGLL SGDCDIAVAG GVSISYPIKQ GYKYRDGMIF SKTGSCQPFE AKSDGTVFSD
     GVGVVVLKRL EEAIADGDDI YGVIKGTAIN NDGNDKVGFT APSVSGQSEV IKDCLDIADV
     AAESIQYIET HGTATEIGDL LEIKALSQVY DEETSRKNFC AIGSIKSNLG HLNTASGIAG
     FIKCLLILKH GIIPPMANFD KENEKLNLKD SHFFINHHPI ELDKNELARI AISSFGIGGT
     NAHVILEEAP LLKKNVDHQI SKQIFPFSAK TPKSLTKNME KLADWLSTNT ETNLMDVAKT
     LQTGRESFGL RQAIVSESIK ELESKINQSL EERKPVKVKK RPIYFLVTGQ GSQFINMARD
     LYENVTVFKN IVDKGMRILQ EKYHENFLAI LYPDKSINES QETINNTKYA QPLLFIISYA
     LGRYLMSLGV QPSKIIGHSL GEYVGACLAG VMTFEEGLDI IYWRGHYLQN AEHGKMISVR
     ASVENLKELH LENVYVSAVN GPRSTVLGGD YDSIAKAEKI LTAHQILYQS LQTSHAFHTP
     IMKNAAKEFR SYLEKYELKD PIIDLISNTT AQSVQKGQLS DSSYWEKHII NPVLFSSSVQ
     HLLAEEEAIF IEIGSGRTLI ELTKQQDLAK KHLFIDMLPG RYSKENQYTF FIERLAALWE
     LGLEIDFEKF QNKEARKVHL PTYHFDQQEF SLLSLGNNVP KKEKADNNIV NYSTNISRNG
     ISADYAEPEN EIEELLLKLL KENVGIENIG VLDNFFELGL SSLLASQYAV SIKESIDLDI
     EIQSIIEAGC VSSLSETVMD KLIEEG
//
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