ID A0A1V4HHH7_9BACL Unreviewed; 1966 AA.
AC A0A1V4HHH7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OPH56174.1};
GN ORFNames=BC351_28815 {ECO:0000313|EMBL:OPH56174.1};
OS Paenibacillus ferrarius.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1469647 {ECO:0000313|EMBL:OPH56174.1, ECO:0000313|Proteomes:UP000190626};
RN [1] {ECO:0000313|Proteomes:UP000190626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CY1 {ECO:0000313|Proteomes:UP000190626};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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:OPH56174.1}.
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DR EMBL; MBTG01000017; OPH56174.1; -; Genomic_DNA.
DR STRING; 1469647.BC351_28815; -.
DR OrthoDB; 9765680at2; -.
DR Proteomes; UP000190626; 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; cd08953; KR_2_SDR_x; 1.
DR CDD; cd19531; LCL_NRPS-like; 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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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 Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
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; 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; PF21394; Beta-ketacyl_N; 1.
DR Pfam; PF00668; Condensation; 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 SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Reference proteome {ECO:0000313|Proteomes:UP000190626};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..431
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1436..1511
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1966 AA; 219592 MW; 273EE253C3E39A5E CRC64;
MSDERTGLEI AVIGMSGRFP KAKNIQEFWE NLRGGVDALS KFTDEELLEF GVDPELLSHP
DYVKKKGSLD AIEDFDASFF GYTPKEASYM DPQFRLFHEV SYEALEDAGY ANVTYKGRIG
LYAGNTQNLL WMGHLLTHMQ SPNDQFEIVS LNDSNTFSTR VAYKLNLRGP ALTVQTACST
SLVAIHLASQ ALIAGECKMA LAGGASVVVP RKNGYLYEEG MLLSRSGACR AFDEEADGLV
FGDGAGCVVL KMLDDAIRDG DHIYAVIKGT AINNDGNLKA GYTAPSPKGQ MIAVRSAHHV
AEVDPETITY VETHGAGSTL GDPIEFEGLK LAFNSDQKGF CALGSAKTNT GHLNQAAGVT
GFIKTVLSMH HKELVPALHF KKANPKINFE NSPFYVNTEL KRWERTGNTP LRAGVSAFGI
GGTNAHVVLE EAPPRQPSGQ GRDAHLLTLS AQSEVSLQNM TAELADFLES KAEVNLADVA
YTLQTGRNLF DHRRHLVVTN VQEAVEALRA ETSGTRKVHT HFSREKNRPV VFLFPGQGSQ
YVNMGRDLYE KEAVFRNELD RCFAIFDHLG CSHLRNVLYP TGDVAVAEEE MRKMQNAQPL
IFAFEYAVAK LLLNLGIQPD AMIGYSFGEY VAACLADVFT LEDALKLIVA RGNLMQRVPE
GAMLSIPLSE SKVLPYLTTN VSLAVDNGTS CIVAGTVDAI EALESRMKEA RVLCMRVKTA
LAGHSLLMDG ILEPFEQLVR SVGLRKPQRP YISDLTGRWI TDQEATDPMY WVRHMRETVR
FAAGVEELAK TSNLVFLEVG PGRDLSSLIG RFVDAKKGQN IVDLIRNAQR QVSDSEQLLA
KLGWLWAYGV AVDWNAFYKG AVRHRLKLPT YAFDRKRYWI DGSAAESAKA LRSQIVTSIG
KRKDTTNWGY IPRWKRTADP QEEENHDLVG WLILTSHTSM GQALAERFAQ RGEWVVTVEP
GTQFAVHDDQ RIVLNPANAQ DYDALLKHLN QSEKRLYKIV HAWILTEETR TLSPEVAQDA
QTLGFYSLLY LAQAMDRVRT EHDYEITVIT DGIHVVNGDE VVQAEKATLL GGVTVIPQEN
PAIRCRSVDI DHVKSTAWQQ KKLLDQLVKE LTAPVRDLLV AYRRGARLVQ SLEPVTLHRP
QDNALQLRED GVYLITGGLG AIGLLFAEYL ITRWHAKVVL TGRTSFPSAQ EWDAYLATHP
AEEATSQKIR RLQMMLQNGG DVLVLKADVA DEERMRIVVQ EAEERFGTLN GVIHAAGIVG
KKSFISIKET TPSHVEEQFQ AKLYGILTLK NVLRGKELDF CMLMSSLTSV LGGLGHIVYS
AANLFVDHYV HRHNAEGDGR WIGVNWDFWM FEEDEANQGA YFGKSATEFA MTPEEGLTVL
EALLNGCEDS QVLISTADLQ ERLDQWIRVE SSIADVAHVQ QSVGHARPAL SNPYVAARDE
LEQQIASIWE SVLGFQQIGI EDDFLELGGD SVKVVSVVSA IHKKLNADIP LHEFFERSTI
EKLVDFIRQN RKAERYEEIQ PIAKQEVYPL SSAQRRLFIL NQFDSTSTNY NTPLAIRLEG
NLDRARMEAA FAKLIQRHEA LRTSFEILEG QPVQRVYDDV DFEIVTTTAD ETEIDDIIAA
FIRPFDLVVA PQLRAQLVQT GVDVHFLLID LHHLCSDGVT IEIVKREIAE LYQGLELPPL
RLQYRDFAAW QTAQLQSDEV KKQEQYWLKR FAGDVPMLNL PTDFLRPPVQ FYAGERLKFE
LDASTVLGLK EGAQRQGATL YMALLGIYNI LLAKYSMQDD VIIGSPIEGR TRPDLQGIAG
IFVNMLAMRN RPTADKTFAG LLGEVKKHAL DAYENQEYQF EDLVARLQLE RVTNRNPLFE
TVLVMQNMEE GKVELEGLRL TPCDIAMKTS IFDLYLQAVE SGETVTLWLD FKTALFKRQT
VEKMIQRFVE IAAQVAETPN RRIGDISFAL DLVEAKSAVP SIEFDF
//
