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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//