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Database: UniProt
Entry: O30408
LinkDB: O30408
Original site: O30408 
ID   TYCB_BREPA              Reviewed;        3587 AA.
AC   O30408;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   01-OCT-2014, entry version 83.
DE   RecName: Full=Tyrocidine synthase 2;
DE   AltName: Full=Tyrocidine synthase II;
DE   Includes:
DE     RecName: Full=ATP-dependent proline adenylase;
DE              Short=ProA;
DE     AltName: Full=Proline activase;
DE   Includes:
DE     RecName: Full=ATP-dependent phenylalanine adenylase;
DE              Short=PheA;
DE     AltName: Full=Phenylalanine activase;
DE   Includes:
DE     RecName: Full=ATP-dependent D-phenylalanine adenylase;
DE              Short=D-PheA;
DE     AltName: Full=D-phenylalanine activase;
DE   Includes:
DE     RecName: Full=Phenylalanine racemase [ATP-hydrolyzing];
DE              EC=5.1.1.11;
GN   Name=tycB;
OS   Brevibacillus parabrevis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Brevibacillus.
OX   NCBI_TaxID=54914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8185 / DSM 362 / JCM 20017 / NBRC 3331 / NCDO 717 / NCIMB
RC   8598 / IAM 1031;
RX   PubMed=9352938;
RA   Mootz H.D., Marahiel M.A.;
RT   "The tyrocidine biosynthesis operon of Bacillus brevis: complete
RT   nucleotide sequence and biochemical characterization of functional
RT   internal adenylation domains.";
RL   J. Bacteriol. 179:6843-6850(1997).
CC   -!- FUNCTION: Activates the second to fourth amino acids in tyrocidine
CC       (in tyrocidine A, Pro, Phe, and D-Phe) and epimerizes the last
CC       one.
CC   -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + H(2)O = AMP +
CC       diphosphate + D-phenylalanine.
CC   -!- COFACTOR: Binds 3 phosphopantetheines covalently. {ECO:0000250}.
CC   -!- PATHWAY: Antibiotic biosynthesis; tyrocidine biosynthesis.
CC   -!- SUBUNIT: Large multienzyme complex of TycA, TycB and TycC.
CC   -!- DOMAIN: Consists of three modules, including a C-terminal
CC       epimerization domain. Each module incorporates one amino acid into
CC       the peptide product and can be further subdivided into domains
CC       responsible for substrate adenylation, thiolation, condensation
CC       (not for the initiation module), and epimerization (optional), and
CC       N methylation (optional).
CC   -!- MISCELLANEOUS: Tyrocidine is a mixture of four cyclic
CC       decapeptides, tyrocidine A (D-Phe-Pro-Phe-D-Phe-Asn-Gln-Tyr-Val-
CC       Orn-Leu), B, C, and D, in which Phe, at positions 3, 4, and Tyr
CC       residues are gradually replaced by Trp, depending on the relative
CC       concentrations of these amino acids in the growth medium.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 3 acyl carrier domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00258}.
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DR   EMBL; AF004835; AAC45929.1; -; Genomic_DNA.
DR   ProteinModelPortal; O30408; -.
DR   SMR; O30408; 967-1484, 2001-2521, 2524-3029.
DR   UniPathway; UPA00180; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0047462; F:phenylalanine racemase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 3.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR010060; NRPS_synth.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 3.
DR   Pfam; PF13193; AMP-binding_C; 3.
DR   Pfam; PF00668; Condensation; 4.
DR   Pfam; PF00550; PP-binding; 3.
DR   SMART; SM00823; PKS_PP; 3.
DR   SUPFAM; SSF47336; SSF47336; 3.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 3.
DR   TIGRFAMs; TIGR01720; NRPS-para261; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 3.
DR   PROSITE; PS00455; AMP_BINDING; 3.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; ATP-binding; Isomerase; Ligase;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphopantetheine;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   3587       Tyrocidine synthase 2.
FT                                /FTId=PRO_0000193094.
FT   DOMAIN      977   1044       Acyl carrier 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   DOMAIN     2012   2079       Acyl carrier 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   DOMAIN     3045   3111       Acyl carrier 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   REGION      466   1045       Domain 1 (Proline-activating).
FT   REGION     1522   2081       Domain 2 (Phenylalanine-activating).
FT   REGION     2540   3122       Domain 3 (D-phenylalanine-activating).
FT   MOD_RES    1007   1007       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
FT   MOD_RES    2042   2042       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
FT   MOD_RES    3075   3075       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
SQ   SEQUENCE   3587 AA;  404817 MW;  322B8471BBB28B47 CRC64;
     MSVFSKEQVQ DMYALTPMQE GMLFHALLDQ EHNSHLVQMS ISLQGDLDVG LFTDSLHVLV
     ERYDVFRTLF LYEKLKQPLQ VVLKQRPIPI EFYDLSACDE SEKQLRYTQY KRADQERTFH
     LAKDPLMRVA LFQMSQHDYQ VIWSFHHILM DGWCFSIIFD DLLAIYLSLQ NKTALSLEPV
     QPYSRFINWL EKQNKQAALN YWSDYLEAYE QKTTLPKKEA AFAKAFQPTQ YRFSLNRTLT
     KQLGTIASQN QVTLSTVIQT IWGVLLQKYN AAHDVLFGSV VSGRPTDIVG IDKMVGLFIN
     TIPFRVQAKA GQTFSELLQA VHKRTLQSQP YEHVPLYDIQ TQSVLKQELI DHLLVIENYP
     LVEALQKKAL NQQIGFTITA VEMFEPTNYD LTVMVMPKEE LAFRFDYNAA LFDEQVVQKL
     AGHLQQIADC VANNSGVELC QIPLLTEAET SQLLAKRTET AADYPAATMH ELFSRQAEKT
     PEQVAVVFAD QHLTYRELDE KSNQLARFLR KKGIGTGSLV GTLLDRSLDM IVGILGVLKA
     GGAFVPIDPE LPAERIAYML THSRVPLVVT QNHLRAKVTT PTETIDINTA VIGEESRAPI
     ESLNQPHDLF YIIYTSGTTG QPKGVMLEHR NMANLMHFTF DQTNIAFHEK VLQYTTCSFD
     VCYQEIFSTL LSGGQLYLIT NELRRHVEKL FAFIQEKQIS ILSLPVSFLK FIFNEQDYAQ
     SFPRCVKHII TAGEQLVVTH ELQKYLRQHR VFLHNHYGPS ETHVVTTCTM DPGQAIPELP
     PIGKPISNTG IYILDEGLQL KPEGIVGELY ISGANVGRGY LHQPELTAEK FLDNPYQPGE
     RMYRTGDLAL WLPDGQLEFL GRIDHQVKIR GHRIELGEIE SRLLNHPAIK EAVVIDRADE
     TGGKFLCAYV VLQKALSDEE MRAYLAQALP EYMIPSFFVT LERIPVTPNG KTDRRALPKP
     EGSAKTKADY VAPTTELEQK LVAIWEQILG VSPIGIQDHF FTLGGHSLKA IQLISRIQKE
     CQADVPLRVL FEQPTIQALA AYVEGGEESA YLAIPQAEPQ AYYPVSSAQK RMLILNQLDP
     HSTVYNLPVA MILEGTLDKA RLEHAISNLV ARHESLRTSF HTINGEPVSR IHEQGHLPIV
     YLETAEEQVN EVILGFMQPF DLVTAPLCRV GLVKLAENRH VLIIDMHHII SDGVSSQLIL
     NDFSRLYQNK ALPEQRIHYK DFAVWEKAWT QTTDYQKQEK YWLDRFAGEI PVLNLPMDYP
     RPAVQSFEGE RYLFRTEKQL LESLQDVAQK TGTTLYMVLL AAYHVLLSKY SGQDDVMIGT
     VTAGRVHPDT ESMTGMFVNT LAMRNQSAPT KTFRQFLLEV KDNTLAAFEH GQYPFEELVE
     KLAIQRNRSR NPLFDTLFIL QNMDADLIEL DGLTVTPYVP EGEVAKFDLS LEASENQAGL
     SFCFEFCTKL FARETIERMS LHYLQILQAV SANTEQELAQ IEMLTAHEKQ ELLVHFNDTA
     ALYPAESTLS QLFEDQAQKT PEQTAVVFGD KRLTYRELNE RANQLAHTLR AKGVQAEQSV
     GIMAQRSLEM AIGIIAILKA GGAYVPIDPD YPNERIAYML EDCRRLVLTQ QQLAEKMTAN
     VECLYLDEEG SYSPQTENIE PIHTAADLAY IIYTSGTTGR PKGVMVEHRG IVNSVTWNRD
     EFALSVRDSG TLSLSFAFDA FALTFFTLIV SGSTVVLMPD HEAKDPIALR NLIAAWECSY
     VVFVPSMFQA ILECSTPADI RSIQAVMLGG EKLSPKLVQL CKAMHPQMSV MNAYGPTESS
     VMATYLRDTQ PDQPITIGRP IANTAIYIVD QHHQLLPVGV VGEICIGGHG LARGYWKKPE
     LTAEKFVANP AVPGERMYKT GDLGRWLHDG TIDFIGRVDD QIKVRGYRIE VGEIEAVLLA
     YDQTNEAIVV AYQDDRGDSY LAAYVTGKTA IEESELRAHL LRELPAYMVP TYLIQLDAFP
     LTPNGKVDRK ALPKPEGKPA TGAAYVAPAT EVEAKLVAIW ENALGISGVG VLDHFFELGG
     HSLKAMTVVA QVHREFQIDL LLKQFFAAPT IRDLARLIEH SEQAAGAAIQ PAEPQAYYPV
     SSAQQRMYLL HQLEGAGISY NTPGIIMLEG KLDREQLANA LQALVDRHDI LRTSFEMVGD
     ELVQKIHDRV AVNMEYVTAE EQQIDDLFHA FVRPFDLSVP PLLRMSLVKL ADERHLLLYD
     MHHIAADAAS ITILFDELAE LYQGRELPEM RIQYKDFAVW QKALHESDAF KQQEAYWLST
     FAGNITAVDV PTDFPRPAVK SFAGGQVTLS MDQELLSALH ELAAHTNTTL FMVLLAAYNV
     LLAKYAGQDD IIVGTPISGR SRAELAPVVG MFVHTLAIRN KPTAEKTFKQ FLQEVKQNAL
     DAFDHQDYPF ESLVEKLGIP RDPGRNPLFD TMFILQNDEL HAKTLDQLVY RPYESDSALD
     VAKFDLSFHL TERETDLFLR LEYCTKLFKQ QTVERMAHHF LQILRAVTAN PENELQEIEM
     LTAAEKQMLL VAFNDTHREY RADQTIQQLF EELAEKMPEH TALVFEEKRM SFRELNERAN
     QLAAVLREKG VGPAQIVALL VERSAEMVIA TLATLKAGGA FLPVDPDYPE ERIRYMLEDS
     QAKLVVTHAH LLHKVSSQSE VVDVDDPGSY ATQTDNLPCA NTPSDLAYII YTSGTTGKPK
     GVMLEHKGVA NLQAVFAHHL GVTPQDRAGH FASISFDASV WDMFGPLLSG ATLYVLSRDV
     INDFQRFAEY VRDNAITFLT LPPTYAIYLE PEQVPSLRTL ITAGSASSVA LVDKWKEKVT
     YVNGYGPTES TVCATLWKAK PDEPVETITI GKPIQNTKLY IVDDQLQLKA PGQMGELCIS
     GLSLARGYWN RPELTAEKFV DNPFVPGTKM YRTGDLARWL PDGTIEYLGR IDHQVKIRGH
     RVELGEVESV LLRYDTVKEA AAITHEDDRG QAYLCAYYVA EGEATPAQLR AYMENELPNY
     MVPAFFIQLE KMPLTPNDKI DRKALPKPNQ EENRTEQYAA PQTELEQLLA GIWADVLGIK
     QVGTQDNFFE LGGDSIKAIQ VSTRLNASGW TLAMKELFQY PTIEEAALRV IPNSRESEQG
     VVEGEIALTP IQKWFFANNF TDRHHWNQAV MLFREDGFDE GLVRQAFQQI VEHHDALRMV
     YKQEDGAIKQ INRGLTDERF RFYSYDLKNH ANSEARILEL SDQIQSSIDL EHGPLVHVAL
     FATKDGDHLL VAIHHLVVDG VSWRILFEDF SSAYSQALHQ QEIVLPKKTD SFKDWAAQLQ
     KYADSDELLR EVAYWHNLET TTTTAALPTD FVTADRKQKH TRTLSFALTV PQTENLLRHV
     HHAYHTEMND LLLTALGLAV KDWAHTNGVV INLEGHGRED IQNEMNVTRT IGWFTSQYPV
     VLDMEKAEDL PYQIKQTKEN LRRIPKKGIG YEILRTLTTS QLQPPLAFTL RPEISFNYLG
     QFESDGKTGG FTFSPLGTGQ LFSPESERVF LLDISAMIED GELRISVGYS RLQYEEKTIA
     SLADSYRKHL LGIIEHCMAK EEGEYTPSDL GDEELSMEEL ENILEWI
//
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