ID Q6YK41_BACIU Unreviewed; 3980 AA.
AC Q6YK41;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Bacillomycin D synthetase A {ECO:0000313|EMBL:AAN07012.1};
GN Name=bamA {ECO:0000313|EMBL:AAN07012.1};
OS Bacillus subtilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423 {ECO:0000313|EMBL:AAN07012.1};
RN [1] {ECO:0000313|EMBL:AAN07012.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATTCAU195 {ECO:0000313|EMBL:AAN07012.1};
RX PubMed=15109718; DOI=10.1016/j.femsle.2004.03.011;
RA Moyne A.-L., Cleveland T.E., Tuzun S.;
RT "Molecular characterization and analysis of the operon encoding the
RT antifungal lipopeptide bacillomycin D.";
RL FEMS Microbiol. Lett. 234:43-49(2004).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; AY137375; AAN07012.1; -; Genomic_DNA.
DR SMR; Q6YK41; -.
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:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05908; A_NRPS_MycA_like; 1.
DR CDD; cd19531; LCL_NRPS-like; 3.
DR CDD; cd00610; OAT_like; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 4.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 3.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 3.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 3.
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; 4.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 4.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 4.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 6.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 4.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 577..652
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 668..1091
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1289..1364
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2416..2491
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3451..3526
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1369..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1929..1955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3980 AA; 448211 MW; 50899CDDA7206B76 CRC64;
MYTSQFQTLV DVIRERSNIS DRGIRFIESD KNETVVSYRQ LFAEAQGYLG YLQHLGIKPK
QEIVFQIQEN KSFVVAFWAC ILGGMIPVPV SIGEDDDHKL KVWRIWNILN HPFLIASEKV
LDKIKKYAAE HDLQDFHHQL NEKSDIIQDQ TYDYPASFYK PDADELAFIQ FSSGSTGDPK
GVMLTHHNLI HNTCAIGNAL AVHSKDSFLS WMPLTHDMGL IACHLVPFIT GINQNLMPTE
LFIRRPILWM KKAHEHKASI LSSPNFGYNY FLKFLKNEPD WDLSHIKVIA NGAEPILPEL
CDEFLKRCAP FNLKRSAILN VYGLAEASVG AAFSKLGEEF VPVYLHRDHL NLGERAVKVS
KEDQNCASFV EVGQPIDYCQ LRISDETNER VEDGIIGHIH IKGDNVTQGY YNNPESTEKA
LTSDGWVKTG DLGFISESGN LVVTGREKDI IFVNGKNIYP HDIERVAIEM EEVDLGRVAA
CGVYDQKTQS GEIVLFVVYK KSPEKFAPLV KEIKKHLYKR GGWSIKEVLP IRKLPKTTSG
KVKRYELARQ YEAGNFSTES AAINECLESS PETSGQTPIH EIETELLSIF SEVLDGKKVH
LADSYFDMGA NSLQLSQIAE RIEQKFGREL AVSDLFTYPS ITDLAAYLSE SRAEIKQDAA
AKPSHVTPKD IAIIGMSLNV PGASTKSDFW NLLEKGEHSI REYPESRLKD AADYLKSIQS
EFNESQFVKG GYLDEIDRFD YSFFGLAPKA AQFMDPNQRL FLQSAWHAIE DAGYAGGSMN
GSRVGVYAGY SKVGYDYERL LSANYPEELH QYIVGNLPSV LASRIAYFLN LKGPAVTVDT
ACSSSLAAVH MACKSLMSGD CEMALAGGIR TSLLPICIGL DMESSDGYTK TFSKDSDGTG
TGEGAAAVLL KPLQDAVRDG DHIYGVIKGS ALNQDGTTAG ITAPNPAAQT EVIETAWKDA
GIAPETLSFI EAHGTGTKLG DPVEFNGLCK AFEKYTAKKQ FCAIGSVKSN IGHLFEAAGI
VGLIKSVLML NHKKNPPLAH FNEPNPLIHF HSSPFYVNQE VSEFTSGDEP LRGGVSSFGF
SGTNAHVVLE EYISQSEYAP EDEHEPHLFV LSAHTEKSLY ELAQQYRQYV SDDSQASLKS
ICYTASTGRA HLDHGIAMIV SGKQELSDKL TRLIQGDRNL PGVYIGYKNM KEMLPAHKEE
LNQQAAALIK QRLRTQDERI TWLNRAAELF VQGAVIDWRA LYSGETVQKT PLPLYPFERS
RCWAEADQLR LNEGEKRGEA ALNINQSKAH IESFLKTVIS NASGIRGEEL DLNAHFIGLG
MDSIMLSQVK KAIADEFGVD IPMDRFFDTL TNLQSVIDYL ADTVPSSFAS APPQENVPAQ
EKQVISEAQL ESDRRDGHQE HTLEKIIASQ NQLIQDALQA QLNSFNLLRN SGHHSDEKEY
AKAQEKSIPS VKQGPPTVNA EQKAAQEAKP YVPFQPQNLN DQGHYTARQK QYLEDFIKKY
AGKTKGSKQY TDNTRFAHAN NRNLSSFRSY WKEIVYPIIA ERSDGSKMWD IDGNEYIDIT
MGFGVNLFGH HPSFITQVID DSTRSSLPPL GPMSDVAGEV ADRIRTCTGV ERVAFYNSGT
EAVMVALRLA RAATGRKKVV AFSGSYHGTF DGVLGVAGTK GGAASANPLA PGILQSFMDD
LIILHYNNPD SLDVIRSLGD ELAAVLVEPV QSRRPDLQPQ AFLKELRAIT QQSGTALIMD
EIITGFRIGL GGAQEWFGIQ ADLVTYGKII GGGQPLGVVA GKAEFMNAID GGTWQYGDDS
YPQDEAKRTF VAGTFNTHPL TMRMSLAVLR HLQTEGEHLY EQLNQKTAYL VDELNHCFEQ
AQVPIRMVRF GSLFRFVSSL DNDLFFYHLN YKGVYVWEGR NCFLSVAHTA DDIENIIQAV
KDTVEDLRRG GFIPEGPDSP DGGGRKKSGT RELSPEQKQL VMASHYGNEA SAALNQSIML
KVKGELQYTS LKQAVRHIVD RHEALRTVIH PDDEVQQVQE RMNIEIPVID FTGLPHEHRE
PEIQKWLTED AKRPFHFHEQ KPLFRIHVLT SAHNEHLIVL TFHHIIADGW SIAVFVQELE
SNYAAIVQGK SISPKEADVS FRQYLDWQQA QIDSGQYEEG VRYWRRHFSE PIQQPILPSA
DSVRYPNGYE GDRCTVRLGR PLSEALRSLS IQMKNSVFVT MLGAFHLFLH RLTKQSGLVI
GIPAAGQSHM KQHDLIGNCV NMIPVKNTSS SESTLSGYLG SMKESVNLAM RHQAVPMTLV
ARELPHDQVP DMRIIFNLDR PFRKLHFGKA EAEPVAYPVK CTLYDLFLNI TDAHQEYVLD
FDFNTNVISP EIMKKWGAGF TKLLQKMVEG DSIPLDAMMM FSDEEQQDLQ ALYGEHQKRV
SSIASNTANF TEAYEAPVNE TERQLARIWE ELFGLERVGR SDRFLALGGN SLQATLMLSK
VQKTFHQKVS IGQFFNHQTV KELARFIQNE TKVVHLPMKT AEKKAYYPTS PAQQRVYFLH
QLEPDQLAQN MFGHISITGK YDEQALISSL QQVMQRHEAF RTYFDIIDGD IVQKLENEVD
FNVHVRTMSR DEFDAYSDRF VKPFRLDQAP LVRAELIKIE NEQAELLMHH IISDGYSVNI
LTNELLALYH QKPLPDIEFE YKDFAEWQNQ RLNDDAMKRQ ATYWLEQFQD EIPILDLPTD
GSKAAERSSE GQRVTCSLQP DVIRSLQDLA QKAETTLYTV LLAAYNVLLH KYTGQEDIVV
GTPASGRNHP DIERIIGIFI QTIGIRTKPH ANRTFTDYLE EVKRQTLDAF ENQDYPFDRL
VEKLNVQRET TGKSLFNTMF VFQNIEFHEI RHNECTFKVK ERNPGVSLYD LMLTIEDAGQ
QIEMHFDYKP GRFTKDTIEQ ITRHYTAILN SLAEQPEMTL SSVPMLSETE RHQLLTECNG
TKTPYPHKET VYRWFEMQAE QSPDHEAVIF GNERYTYRQL NERANRLART LRTKGVQADQ
FIAIISPHRI ELIVGILAVL KAGGAYVPID PEYPEDRIQY MLRDSRAEVV LTQRSLLDQL
PYDGDIVLLD EENSYHEDHS NLESDSDAHD LAYMIYTSGS TGNPKGVLIE HQGLANYIWW
AKEVYVRGEK TNFPLYSSIS FDLTVTSIFT PLVTGNTIIV FDGEDKSAVL SEIMRDSRID
MIKLTPAHLH VIKEMNIAGG TAIRKMIVGG ENLSTRLAKS VSEQFKGRLD IFNEYGPTEA
VVGCMIYHFD AERDKREFVP IGTPAANTDI YVADASRNLV PFGVIGEIYI SGPGVARGYW
NRPDLTAEKF VENPYVPGAK MYKSGDLAKR LKDGNLLYIG RVDEQVKIRG HRIELGEIEA
AMHNAEAVQK AAVTVKEEED GLKQLCAYYV SDKPIAAAQL REQLSSGLPD YMVPTYFVHL
EHMPLTSNGK INRKALPAPE ASLQQTAEYV PPGNETESKL TDLWKEVLGI SHAGIKHNFF
DLGGNSIRAA ALAARIHKEL DVNLSLKDIF KFPTIEQLAD KALHMDKNRY VPIPAAKEMP
YYPVSSAQRR MYLLSHTEGG ELTYNMTGAM NVEGTIDPER LNAAFRKLIA RHEALRTSFD
LYEGEPAQRI HQNVDFTIER IQASEEEAED RVLDFIKAFD LAKPPLMRAG LIEIEPARHV
LVVDMHHIIS DGVSVNILMK DLSRIYEGNE PDPLSIQYKD FAVWQQSDIQ KRIIKSQEAY
WLDQFHGDIP VLDMPADYER PAIRDYEGES FEFLIPEHLK QRLSQMEEDT GATLYMILLA
AYTILLSKYS GQEDIIVGTP SAGRTHLDVE PVVGMFVNTL VIRNHPAGRK TFDAYLNEVK
ENMLNAYKNQ DYPLEELIQH LHLPKDSSRN PLFDTMFVLQ NPDHAELTFD SLQIKPYPFH
HPVAKFDLTL SIQADRDNYH GLFEYTKKLF KKSRIEILSN DYLHILSAIL EQPSILIEHI
GLSGSNEEEE NALDSIQLNF
//
