ID MYCB_BACIU Reviewed; 5369 AA.
AC Q9R9J0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-NOV-2024, entry version 95.
DE RecName: Full=Mycosubtilin synthase subunit B;
DE EC=2.3.1.-;
DE Includes:
DE RecName: Full=ATP-dependent tyrosine adenylase;
DE Short=TyrA;
DE AltName: Full=Tyrosine activase;
DE Includes:
DE RecName: Full=ATP-dependent asparagine adenylase 2;
DE Short=AsnA 2;
DE AltName: Full=Asparagine activase 2;
DE Includes:
DE RecName: Full=ATP-dependent glutamine adenylase;
DE Short=GlnA;
DE AltName: Full=Glutamine activase;
DE Includes:
DE RecName: Full=ATP-dependent proline adenylase;
DE Short=ProA;
DE AltName: Full=Proline activase;
GN Name=mycB;
OS Bacillus subtilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX PubMed=10557314; DOI=10.1073/pnas.96.23.13294;
RA Duitman E.H., Hamoen L.W., Rembold M., Venema G., Seitz H., Saenger W.,
RA Bernhard F., Reinhardt R., Schmidt M., Ullrich C., Stein T., Leenders F.,
RA Vater J.;
RT "The mycosubtilin synthetase of Bacillus subtilis ATCC6633: a
RT multifunctional hybrid between a peptide synthetase, an amino transferase,
RT and a fatty acid synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13294-13299(1999).
CC -!- FUNCTION: This protein is a multifunctional enzyme, able to activate
CC and polymerize the amino acids Tyr, Asn, Gln and Pro as part of the
CC synthesis of mycosubtilin. The Asn and Gln residues are further
CC epimerized to the D-isomer form. The activation sites for these amino
CC acids consist of individual domains.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC Note=Binds 4 phosphopantetheines covalently. {ECO:0000305};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF184956; AAF08796.1; -; Genomic_DNA.
DR PIR; T44807; T44807.
DR SMR; Q9R9J0; -.
DR STRING; 483913.AN935_09465; -.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:TreeGrafter.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd17655; A_NRPS_Bac; 1.
DR CDD; cd17656; A_NRPS_ProA; 1.
DR CDD; cd19543; DCL_NRPS; 2.
DR CDD; cd19534; E_NRPS; 2.
DR CDD; cd19531; LCL_NRPS-like; 2.
DR FunFam; 3.30.300.30:FF:000010; Enterobactin synthetase component F; 4.
DR FunFam; 3.40.50.12780:FF:000012; Non-ribosomal peptide synthetase; 3.
DR FunFam; 3.40.50.980:FF:000001; Non-ribosomal peptide synthetase; 4.
DR FunFam; 2.30.38.10:FF:000001; Non-ribosomal peptide synthetase PvdI; 4.
DR FunFam; 1.10.1200.10:FF:000005; Nonribosomal peptide synthetase 1; 4.
DR Gene3D; 3.30.300.30; -; 4.
DR Gene3D; 3.40.50.980; -; 8.
DR Gene3D; 1.10.1200.10; ACP-like; 4.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 6.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 7.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR010060; NRPS_synth.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 4.
DR NCBIfam; TIGR01720; NRPS-para261; 2.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 4.
DR Pfam; PF13193; AMP-binding_C; 3.
DR Pfam; PF00668; Condensation; 7.
DR Pfam; PF00550; PP-binding; 4.
DR SMART; SM00823; PKS_PP; 4.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 4.
DR SUPFAM; SSF47336; ACP-like; 4.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 13.
DR PROSITE; PS00455; AMP_BINDING; 3.
DR PROSITE; PS50075; CARRIER; 4.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 4.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Repeat; Transferase.
FT CHAIN 1..5369
FT /note="Mycosubtilin synthase subunit B"
FT /id="PRO_0000360849"
FT DOMAIN 764..838
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2275..2349
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3801..3876
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 4840..4915
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 260..1620
FT /note="Domain 1 (D-tyrosine-activating)"
FT REGION 290..686
FT /note="Adenylation 1"
FT REGION 846..1305
FT /note="Epimerization 1"
FT REGION 1315..1615
FT /note="Condensation 1"
FT REGION 1770..3132
FT /note="Domain 2 (D-asparagine-activating)"
FT REGION 1800..2197
FT /note="Adenylation 2"
FT REGION 2357..2816
FT /note="Epimerization 2"
FT REGION 2826..3127
FT /note="Condensation 2"
FT REGION 3281..4182
FT /note="Domain 3 (glutamine-activating)"
FT REGION 3311..3723
FT /note="Adenylation 3"
FT REGION 3888..4177
FT /note="Condensation 3"
FT REGION 4334..5221
FT /note="Domain 4 (proline-activating)"
FT REGION 4364..4762
FT /note="Adenylation 4"
FT REGION 4927..5216
FT /note="Condensation 4"
FT MOD_RES 799
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2310
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3836
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4875
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 5369 AA; 612337 MW; E99AD8C33B45EBE2 CRC64;
MSVFKNQVTY WANLFDEEDS LSVIPYFKTA ENASLTRVGY QEKSIYRSLS PEVSQRILTM
ANHSEMATYL ILLAGIECLL YKYTDRASTI LGIPTVSKQK SSSSTVNTIV LLKNTLSCQS
TFKTVFEQLK KAVNDSLKNQ NLPFRKIVQH VNVQYDNENI PLIHTVVSLN EIHSLQFKED
IATDTLFHFD LENSEIHLKL IYNGNLYDED YMDQMVSHLN QLLSVILFQP QAAIHTAEGI
PEAVKQQILF DFNDTAADYS GNKTVSQLFE EQAERTPDHV AVKFVNNHMT YRELNEKSNR
LARTLRNYGV QADTLVAIMA ERSLEMIVSI MAIWKAGGAY VPLDPEYPEE RLQYVLNDAN
ADVLVVQRHF KNSLVFDGPM IDLNDETSYH ADCSLLSPIA EHSHLAYVIY TSGTTGKPKG
VMVEHGGIVN SLQWKKAFFK HSAEDRVLVL YPYVFDAFIL NFFGPLISGA ALYLLPNEDN
KDLFAIQNVL KLERITHFST SPRLLQAMTE QMNAEDFYHV QHVVVGGEKL EPDTVERLFS
LQPQIRINNE YGPTENSVVS TFQPVYSADE QITIGKPVAN HQAYILGAHR QIQPIGVPGE
LYVGGSGVAR GYLNQPDLTE EKFVDHLLIP RRKMYKTGDL ARWLPDGRIE YLGRIDHQVK
IRGYRIELGE VEAALSNLEE VRETTVESRE GIDGTKQLYA YYVGEPSLSA GQFREILSRE
LPDYMIPSYF IHLERIPLTS NGKIDLKALP VADEKTRMEN EYIAPQNSIE ELLASIWQEV
LGTERIGILD NFFDFGGDSI KSIQVSSRLY QSGYKIDMKH LFTYPTIAEL SPFVEPVGRM
ADQGEVKGRT SLTPIQHWFF EQNMPHANHY NQAVMLYSAQ GFKETPLRRA IESIAVHHDA
LRMVFEETPN GYTARIAGTE ESKLYQLEVM NCKEDADPAH AVANKANQIQ SSMELSQGPL
MKLGLFKCAD GDHLLIAIHH LVIDGVSWRI LLEDFASSYE QAERGQMVRL PQKTDSFPFW
AEQLSKYAQE TDREQELAYW NELARLELEP LPKDNAVEDS LLKDSGDVTI QWTREETQQL
LKQANRAYNT EINDLLLTSL GLAVHRWTGM EEVVVNLEGH GREPVIPDVD ITRTVGWFTS
QYPVVLKMEA GKELSQRIKT VKEGLRRVPN KGMNYSVIQY LSGRAEADSL QLHPEIRFNY
LGQFDQDLQQ HALQISPYST GVSLNENQPR TAVLDLNGMV AEGKLSLSLS YSHKQYERST
MEQFARSLKE SLQEIIVHCV NQQQTSLTPS DVLLKDIKID ELEELLDQTR ELGEVENIYP
LTPMQKGMLF HSLFDSHSGA YFQQTMFELH GDLDIDSFSK SLDDLSKRYE IFRTNFLKGK
DQPLQIIFKT KKIGFQFIDL REMDQARQDD RICAYAKEDK LRGFDLAKDV LMRVIVLRTD
DTTYRFIWSF HHILMDGWCL PLITKEIFDH YFALLQQKQP EQAAITPYSQ YIEWLDRQDA
EEAKRYWDQY LEGYEEQTVL LKDSHQAEDE HYFPEKVSCA IDTDLTLKMK QTASKHHVTL
NTLLQTAWGI LLQKYNRSRD VVFGSVVSGR PSAIPNVETM IGLFINTIPV RIQCEAGTTF
AELMKRTQER AVASQTYETY PLYDIQALTT QKQNLITHLM IFENYPVDQY MESIGQHNES
PIDISNVKME EQTNYHLNVT VIPGDVININ FEYNAKVYDR ESMERVRGHL LQILHQVVAD
ADIRVEQLEM LTEGEKRQLL QNLNDTAAPY PQSTVGQWFE AQSQQIPDQA AVIDGDKQIT
YRQLNERANR LARTLRARGV QADQPVATIS RNSIELVTGI LAILKAGGAY VPIDPEYPQD
RIQYILEDSK AGIILMPRDV RQQITYEGVV ILLDEESSYH EEAFNLEPLS NANHLAYVIY
TSGSTGKPKG VLIEHRGLSN YIWWAKEVYV KNEKTNFPLY SSISFDLTVT SIFTPLVTGN
TIIVYDGEDK TALLSSIVQD QRVDIIKLTP AHLHVLKAMN IANKIAIRKM IVGGENLSTQ
LAQSIHEQFD GQIEICNEYG PTETVVGCML YRYDAVKDRR ESVPIGTAAA NTSIYVLDED
MKPVPIGVPG EMYISGAGVA RGYLNRPELT AEKFVENPFV TGERMYKTGD LAKWLPDGNI
EYLGRMDEQV KIRGFRIELG EIETAMLQAE EIKEAVVTAR EDVHGLKQLC GYYVSSQPIT
VSQIREQLSQ SLPGYMIPAY FIKLEKMPLT PNGKINQKEL PTPDLQLQDR VAYKPPRTQV
EQLLVSTWES VLGAEKIGIL DNFFDLGGDS IKSIQVSSRL NQLGYKMEIK HLFQYATIAE
LSPHIEQNVR IPDQDEVKGK VSLTPIQHWF FEQTTTDPHY YNQAVMLYAP QGFSGIAASP
NATKAWRAPR CVRMTFQATE HGYEAWNAEI TQSELYHLDV INLKTEADPG PAIEAKANQI
QSSMQLSNGP LMKAGLFQCA DGDHLLIAIH HLIVDGISWR ILMEDIVSGY KQAENGQDIQ
LPYKTDSFRL WAEKLSAYAQ SDAIKQEQEY WARIEQTDVK PLPKDFQESH AFSIDSETVT
VEWTKEETEQ LLKQANRAYN TEINDLLLSS LGLSISHWSG LEQIALHLEG HGREQVIPNM
DISRTVGWFT SLFPVVLHIE PGKEISHYIK TAKEELRQIP HKGIGYGVLR YLSGSTTPLP
AKMTPEISFN YLGQFDQDIQ NQAVQLSSYS CGSDSSGNQI RPYVLNINGM IVNDRLMVTI
SYSTKQYAKE TIDQLSAIIQ NNLRTVIEHC VHKEQTELTP SDILLKGMAI DELDQLLIQL
PDAGEIENVY PLTPMQKGML FHSLLDEDSN SYFEQASFDL QGELKIDRFE ASLDHLFAKY
AVLRTRFYSG WNDIPLQIVY KTQRMKVHFT DLRDIDENQR KDEIASYQSE DKAKGFDLAR
DPLMRIAIFR IEERKYHLIW SFHHIVMDGW CLPLITKEAF EHYIGLQEGR ETDLAYTDPY
SKYIEWLDQQ DQNAAKRYWR EYLEGYKGET RILHKRPQHE RKAYAYANEI CRFNQKQTRQ
LQRIANQHHV TLNTLIQTLW GILLQKYSGT GDVVFGSVVS GRPAEISGVE QMIGLFINTI
PVRICCDEGS SFVETMKMVQ DNALASQSYD TYPLYEIQAQ TEQKQNLIDH ILIFENYPIG
QQVEEGHNAA ELNIMNFHME EHSHYDFNMV VIPGEQLNVH FGYNQNVYEQ SEVERISGHF
EQLMHQVLEH PNIKVEELEL LTQQEKEQLL SRFQAREMQY SREQTIHERF SKQAFRTPDR
TAVVFEGESL TYGELNKRAN QLAQALRVEG VQAGQLVGIM AERSLEMIIG IFGILKAGGA
YLPIDPDSPV ERIHYIARDS GINILLTHGE LPENLNFSGT CINMKEEQAY HETDINLAVP
CQFDQLAYCI YTSGTTGTPK GTPKGTLIEH RQVIHLIEGL RNAVYSAYDG VLHVAMLAPY
YFDASVQQIY ASLLLGHTLF IVPKEAVSDG EALCQYYRQH RIDVTDGTPA HLKLLVAADD
GEGVPLRHLL IGGEALPKTT VTKFIHLFGA DRAAPAITNV YGPTETCVDA SLFNIEVSAD
AWTRSQVHIP IGKPLGNNRM YILDSQQKLQ PVGVQGELYI AGDGVGRGYL NLPELTNKKF
VNDPFVPSGR MYRTGDLARL LPDGNIEFIE RVDHQVKIHG FRIELGEIES IMLNIPEIQE
AVASVLEDAD GEHYICGYYV ANKPFPTSQL RDRLTRHLPG YMIPAYFVQM DQMPLTPNGK
LNRNLLPEPD GKRYGDTEYV PPRNSTEMKL TKIWQDVLGL EQVGIRDNFF DIGGHSLRAT
TLIAKIQKQL HVQIPLRNIF QFPTIEQLAQ AIMTMEETEY ASIPLIEKRP YYPVSSAQKR
LYILNHLEGG ELSYNMLGLM TVKGELDRDK LQQAFDKLIH RHESLRTGFK MVDGEPVQYV
LDHVEFAVES YYAKEDEIDH CISQFVRAFQ LEEPPLLRVG LIELQPNHAI LMFDMHHIIS
DGTSMNVLIK EFVRAYQGAE LPPLRIQYKD YSVWQTGEAR LEQIQKQEDY WLELYSGDIP
VLHLPTDYIR PSTRDFTGAT LHFTIDEKKS EGLKQLALKT ESTLYMVLLA SYTLLLSKYS
GQEDIVVGSP IAGRPHADLD SIIGMFVNTL AMRNYPAKEK TFSQYLAEVK ENALKAYEHQ
DYPFEALVDQ LNIARDLSRN PLFDTMFVLQ NTEQEQLGMD GLTFKPYPSK HTMAKFDLTL
TAVEEETHIH CTMEYLTTLF KPETVERMMR HFVQLIDAII EHPEARLASL EMMRSREKNE
IWNLFNDTAV IDERMPTTIH QQFEQQAEDT PDRVAILFEN QTWTYRQLNE RSNQLARVLR
NQGVGADRVA AILTERSANM MIGILAILKA GGAFLPIDPE LPDERRAYLM EDSGADVLVT
CVEHTVPPSF EGSVVLLDDP LVYQGDASNL NLSYAENHLL YVIYTSGTTG KPKGVQLEHK
TMLNLLAYER EYTQLRFDRV LQFAAMSFDV CYQEIFSTIL SGGTLYIIDN EAKREIRELN
EFVKTHRIQT AFLPTAFLKL LASEKQYFEP FAECVDHIIT AGEQLIMTNT LREMMMRHQV
SLHNHYGPSE THVVTMCTVD PEIHQEMPPI GKPISNTEIL ILNEAGTLQP IGIVGELCIA
GISLARGYHN RESLTHEKFV PHPYDANKRM YKTGDLARYL PDGNIEYAGR MDHQVKIRGY
RIELNEVEAA LLNIEHVQEA VVLARENTEG QSDLYAYFVA EQALPISQFK EKLAQQIPGY
MIPSYLMQLE QMPLTSNGKV NRSALPLPAA GMQTGIDHVA PRTRLEEQLV LIWKEVLKLE
QVGVKDNFFD LGGHSLRGMT LVGKIHKQFN KTISLREVFQ GPTIEEMAKV IANSETCGPD
YIPAVEVKDV YPVSSVQKMV YLSTQIEGGE LSYNMPGILT LEGRIDMDRL QTAFHRLIQR
HESLRTGFEM IRGEPMQMVK PEVEFTIERY KATAEEVEEL FRTFVRPFDL SQAPLLRVGL
IELEQEKHIF MFDMHHIVTD GASMNIFIEE LIQLYDGKEL APLRIQYKDF TAWQQQAEQK
ERIKKQEDYW LDVFHEALPS FELPKDFARP QVRSFEGKRY NFVLNESVVQ GVKQLEELTG
STTYMILFAA YTILLAKYSG QEDIVVGTPV AGRVHDDLQH IIGMFVNTLA IRTAPAGEKT
FKDYVTETKE TMLKAYENQE YPFEELVEKL GVQRDLSRNP LFDTMFVLQN TEQTDIEIDS
LAVRPYEETH AVAKFDLQLT FEMHQHEIQG SFDYCTKLFK KRTIATLAQD YVMILSAVIQ
NSSIPLKEIQ LSEKVNKKEH FASVIELDF
//
