ID S9U724_PAEAL Unreviewed; 1578 AA.
AC S9U724;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=JamP {ECO:0000313|EMBL:EPY06300.1};
GN ORFNames=PAALTS15_16331 {ECO:0000313|EMBL:EPY06300.1};
OS Paenibacillus alvei TS-15.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1117108 {ECO:0000313|EMBL:EPY06300.1, ECO:0000313|Proteomes:UP000015344};
RN [1] {ECO:0000313|EMBL:EPY06300.1, ECO:0000313|Proteomes:UP000015344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TS-15 {ECO:0000313|EMBL:EPY06300.1,
RC ECO:0000313|Proteomes:UP000015344};
RA Strain E.A., Brown E., Allard M.W., Luo Y.L.;
RL Submitted (MAY-2013) 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:EPY06300.1}.
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DR EMBL; ATMT01000056; EPY06300.1; -; Genomic_DNA.
DR RefSeq; WP_021260577.1; NZ_ATMT01000056.1.
DR PATRIC; fig|1117108.3.peg.3371; -.
DR eggNOG; COG3321; Bacteria.
DR Proteomes; UP000015344; 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 CDD; cd08953; KR_2_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; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR049490; C883_1060-like_KR_N.
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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
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; PF21394; Beta-ketacyl_N; 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; 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.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..423
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1471..1546
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1578 AA; 173495 MW; 5EC365451C98BF3D CRC64;
MDVGKKIETM NGIAIIGMAG RFPGARNVEQ LWDNLINGIE SVTAFKEPEE GRIHTACLLE
NAAAFDAAFF GMTPREAELT DPQHRLFLEC AYEAMEASGY APTRCPERVG VYAGSGQSDY
VRHVQSHSDI MQTVGTFQVA IGNGPDFLTT RVSHKLKLNG PSIAVQTACS SSLVAVHMAC
QALFTYECDM ALAGGVSVKA DQMLGFDYQE GGILAPDGHC RAFDAASQGT VVGNGVGVVA
LKRLDDAIAD GDEIVAIIRG TAVNNDGADK VGYTAPSVAR QAEVVKEALT IAGVDPATIT
YIEAHGTGTA LGDPIEIAAL TDAYRTFTRK KQYCAVGSVK TNIGHLDSAA GVSGLIKAVL
CIKHRMLPPS LHYKEPNPHI NFADSPFYVN GNLKDWLSDG EPLRAGVSSF GIGGTNAHVI
LEEAPPRTTD EKDVDAEPDW HLLALSARTP GSLRQRAEDL IDYLQRHQEV DMASIAYTLA
VGKESFARRM AIVAHKSAES AMEELRKMTA SMPSNMDEAN EATPSVFFMF TGQGAQYVHM
ASDLYRCAPA FRKHIQQCAK LSASVLDADL LRLLYPLPGE EKEAANQLHQ TKYAQPALFC
VEYALAKQME AWGIKQEAMI GHSIGEYVAA CLAGVMSLND AIKVIAVRAS LMQQMERGAM
TVVSLSEADT IEALGESGAE LSIAVVNSPR SCVVAGTYAA TERFEAFLSG KGVISKRLAT
SHAYHSEMME PILPRFAEAM RTIRLHPPNI SYISNVTGRW ITPEEATDPQ YWVDHLRKCV
RFADGIKLLL DAREHSIFVE IGPGHTLSAM VRQQIGGDYE KKSAIFMLPA EANEQSAYAS
VLRAIGELWC SGVNVDPASV APLHARRRVC LPTYPFERHI YYLPLKEHET RASYQEAGAE
SNPDSGEWFY APMWKQTALP FQTTALEMSK AETEHSGSMV GSAGLEEAEM HEQPEKKEMQ
EKPLYLLLSD NCGVSETLKE ELERFGNTVI LAHSGDLNDS MNDSRLVYNP AQSDSYERLI
GNIAAYHRRL PNKVIHLGNL DADLSNNHSD RYQSYENIQQ QGLFSVVSLA QAIGLQHVFQ
DVELIVLTGN LLQIAHERVA NPERATLVGA LRVIPQEYAR IGTRLIDVDV ADFSEAVTFS
RRYVRQLAIE ISSSSLEFLV AYRGFHRYVQ TIEGVRLPLS EQQTISIRDG GVYFITGADG
GIGLLMAEAI AKAVKAKLIL IGESPLPDIS EWDRYLSSDD TTETTKHIRS IRALEQNGSE
VWYASASLAD EVELKQIIVE AEERFGSIHG MLIASEPYDS GLIQLKDIQE TTQRIVPYLV
GLSVLASSLN NPDAFLVLFS RTVAITGGAG QMDLCAYNWY ADTFAKHRTA TGYPTLSVNW
SMWQEDVWLD RQKEIPPQMR EQLRHVQKQY GIAATEGIHA LERMLASGLP QIIVSKQNFQ
TASQDWQSIH TSPVIINSGA GETHEEVSHS VPRNETEEKI AAIWQTLFGI SDIGVHRSFF
DLGGNSLHAI QLVARLRHQF HGDIPMDIIF HHPTVAELAE AVSRSQTKQK QWDEVERLLN
EIEFMSEDEL LHALSRDG
//
