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   03-AUG-2022, entry version 86.
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; Firmicutes; 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   PRIDE; Q9R9J0; -.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1200.10; -; 4.
DR   Gene3D; 3.30.300.30; -; 4.
DR   Gene3D; 3.30.559.10; -; 6.
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.
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   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; SSF47336; SSF47336; 4.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 4.
DR   TIGRFAMs; TIGR01720; NRPS-para261; 2.
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