TYCB_BREPA
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 03-AUG-2022, entry version 110.
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; 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 8598
RC / IAM 1031;
RX PubMed=9352938; DOI=10.1128/jb.179.21.6843-6850.1997;
RA Mootz H.D., Marahiel M.A.;
RT "The tyrocidine biosynthesis operon of Bacillus brevis: complete nucleotide
RT sequence and biochemical characterization of functional internal
RT adenylation domains.";
RL J. Bacteriol. 179:6843-6850(1997).
CC -!- FUNCTION: Activates the second to fourth amino acids in tyrocidine (in
CC tyrocidine A, Pro, Phe, and D-Phe) and epimerizes the last one.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-phenylalanine = AMP + D-phenylalanine +
CC diphosphate + H(+); Xref=Rhea:RHEA:20201, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57981, ChEBI:CHEBI:58095, ChEBI:CHEBI:456215;
CC EC=5.1.1.11;
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250};
CC Note=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 epimerization
CC domain. Each module incorporates one amino acid into the peptide
CC product and can be further subdivided into domains responsible for
CC substrate adenylation, thiolation, condensation (not for the initiation
CC module), and epimerization (optional), and N methylation (optional).
CC -!- MISCELLANEOUS: Tyrocidine is a mixture of four cyclic decapeptides,
CC tyrocidine A (D-Phe-Pro-Phe-D-Phe-Asn-Gln-Tyr-Val-Orn-Leu), B, C, and
CC D, in which Phe, at positions 3, 4, and Tyr residues are gradually
CC replaced by Trp, depending on the relative concentrations of these
CC amino acids in the growth medium.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF004835; AAC45929.1; -; Genomic_DNA.
DR PDB; 6TA8; X-ray; 2.40 A; A/B=3113-3587.
DR PDBsum; 6TA8; -.
DR SMR; O30408; -.
DR STRING; 54914.AV540_22695; -.
DR KEGG; ag:AAC45929; -.
DR SABIO-RK; O30408; -.
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 GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 3.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 3.30.559.10; -; 4.
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; 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; PS00455; AMP_BINDING; 3.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; ATP-binding; Isomerase; Ligase;
KW Multifunctional enzyme; Nucleotide-binding; Phosphopantetheine;
KW Phosphoprotein; Repeat.
FT CHAIN 1..3587
FT /note="Tyrocidine synthase 2"
FT /id="PRO_0000193094"
FT DOMAIN 972..1047
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2007..2082
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3040..3114
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 466..1045
FT /note="Domain 1 (Proline-activating)"
FT REGION 1522..2081
FT /note="Domain 2 (Phenylalanine-activating)"
FT REGION 2540..3122
FT /note="Domain 3 (D-phenylalanine-activating)"
FT REGION 3017..3040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1007
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2042
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3075
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT STRAND 3124..3126
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3130..3137
FT /evidence="ECO:0007829|PDB:6TA8"
FT TURN 3141..3144
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3146..3154
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3160..3173
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3175..3178
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3179..3182
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3184..3186
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3189..3192
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3195..3197
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3201..3206
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3213..3225
FT /evidence="ECO:0007829|PDB:6TA8"
FT TURN 3230..3232
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3236..3243
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3246..3254
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3255..3257
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3260..3278
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3292..3303
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3304..3306
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3308..3311
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3312..3320
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3338..3340
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3341..3347
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3350..3358
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3361..3364
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3368..3384
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3387..3395
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3416..3423
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3430..3442
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3445..3448
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3450..3456
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3473..3481
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3486..3488
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3491..3493
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3511..3519
FT /evidence="ECO:0007829|PDB:6TA8"
FT STRAND 3522..3530
FT /evidence="ECO:0007829|PDB:6TA8"
FT TURN 3531..3533
FT /evidence="ECO:0007829|PDB:6TA8"
FT HELIX 3536..3557
FT /evidence="ECO:0007829|PDB:6TA8"
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
