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Protein

Tyrocidine synthase 2

Gene

tycB

Organism
Brevibacillus parabrevis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Activates the second to fourth amino acids in tyrocidine (in tyrocidine A, Pro, Phe, and D-Phe) and epimerizes the last one.

Catalytic activityi

ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine.

Cofactori

pantetheine 4'-phosphateBy similarityNote: Binds 3 phosphopantetheines covalently.By similarity

Pathwayi: tyrocidine biosynthesis

This protein is involved in the pathway tyrocidine biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway tyrocidine biosynthesis and in Antibiotic biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Ligase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKO30408.
UniPathwayiUPA00180.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrocidine synthase 2
Alternative name(s):
Tyrocidine synthase II
Including the following 4 domains:
ATP-dependent proline adenylase
Short name:
ProA
Alternative name(s):
Proline activase
ATP-dependent phenylalanine adenylase
Short name:
PheA
Alternative name(s):
Phenylalanine activase
ATP-dependent D-phenylalanine adenylase
Short name:
D-PheA
Alternative name(s):
D-phenylalanine activase
Phenylalanine racemase [ATP-hydrolyzing] (EC:5.1.1.11)
Gene namesi
Name:tycB
OrganismiBrevibacillus parabrevis
Taxonomic identifieri54914 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaeBrevibacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 35873587Tyrocidine synthase 2PRO_0000193094Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1007 – 10071O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei2042 – 20421O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei3075 – 30751O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

Large multienzyme complex of TycA, TycB and TycC.

Structurei

3D structure databases

ProteinModelPortaliO30408.
SMRiO30408. Positions 967-1484, 2001-2521, 2524-3029.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini977 – 104468Acyl carrier 1PROSITE-ProRule annotationAdd
BLAST
Domaini2012 – 207968Acyl carrier 2PROSITE-ProRule annotationAdd
BLAST
Domaini3045 – 311167Acyl carrier 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni466 – 1045580Domain 1 (Proline-activating)Add
BLAST
Regioni1522 – 2081560Domain 2 (Phenylalanine-activating)Add
BLAST
Regioni2540 – 3122583Domain 3 (D-phenylalanine-activating)Add
BLAST

Domaini

Consists of three modules, including a C-terminal epimerization domain. Each module incorporates one amino acid into the peptide product and can be further subdivided into domains responsible for substrate adenylation, thiolation, condensation (not for the initiation module), and epimerization (optional), and N methylation (optional).

Sequence similaritiesi

Contains 3 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di1.10.1200.10. 3 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR010060. NRPS_synth.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00501. AMP-binding. 3 hits.
PF13193. AMP-binding_C. 3 hits.
PF00668. Condensation. 4 hits.
PF00550. PP-binding. 3 hits.
[Graphical view]
SMARTiSM00823. PKS_PP. 3 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 3 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 3 hits.
TIGR01720. NRPS-para261. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00455. AMP_BINDING. 3 hits.
PS00012. PHOSPHOPANTETHEINE. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O30408-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVFSKEQVQ DMYALTPMQE GMLFHALLDQ EHNSHLVQMS ISLQGDLDVG
60 70 80 90 100
LFTDSLHVLV ERYDVFRTLF LYEKLKQPLQ VVLKQRPIPI EFYDLSACDE
110 120 130 140 150
SEKQLRYTQY KRADQERTFH LAKDPLMRVA LFQMSQHDYQ VIWSFHHILM
160 170 180 190 200
DGWCFSIIFD DLLAIYLSLQ NKTALSLEPV QPYSRFINWL EKQNKQAALN
210 220 230 240 250
YWSDYLEAYE QKTTLPKKEA AFAKAFQPTQ YRFSLNRTLT KQLGTIASQN
260 270 280 290 300
QVTLSTVIQT IWGVLLQKYN AAHDVLFGSV VSGRPTDIVG IDKMVGLFIN
310 320 330 340 350
TIPFRVQAKA GQTFSELLQA VHKRTLQSQP YEHVPLYDIQ TQSVLKQELI
360 370 380 390 400
DHLLVIENYP LVEALQKKAL NQQIGFTITA VEMFEPTNYD LTVMVMPKEE
410 420 430 440 450
LAFRFDYNAA LFDEQVVQKL AGHLQQIADC VANNSGVELC QIPLLTEAET
460 470 480 490 500
SQLLAKRTET AADYPAATMH ELFSRQAEKT PEQVAVVFAD QHLTYRELDE
510 520 530 540 550
KSNQLARFLR KKGIGTGSLV GTLLDRSLDM IVGILGVLKA GGAFVPIDPE
560 570 580 590 600
LPAERIAYML THSRVPLVVT QNHLRAKVTT PTETIDINTA VIGEESRAPI
610 620 630 640 650
ESLNQPHDLF YIIYTSGTTG QPKGVMLEHR NMANLMHFTF DQTNIAFHEK
660 670 680 690 700
VLQYTTCSFD VCYQEIFSTL LSGGQLYLIT NELRRHVEKL FAFIQEKQIS
710 720 730 740 750
ILSLPVSFLK FIFNEQDYAQ SFPRCVKHII TAGEQLVVTH ELQKYLRQHR
760 770 780 790 800
VFLHNHYGPS ETHVVTTCTM DPGQAIPELP PIGKPISNTG IYILDEGLQL
810 820 830 840 850
KPEGIVGELY ISGANVGRGY LHQPELTAEK FLDNPYQPGE RMYRTGDLAL
860 870 880 890 900
WLPDGQLEFL GRIDHQVKIR GHRIELGEIE SRLLNHPAIK EAVVIDRADE
910 920 930 940 950
TGGKFLCAYV VLQKALSDEE MRAYLAQALP EYMIPSFFVT LERIPVTPNG
960 970 980 990 1000
KTDRRALPKP EGSAKTKADY VAPTTELEQK LVAIWEQILG VSPIGIQDHF
1010 1020 1030 1040 1050
FTLGGHSLKA IQLISRIQKE CQADVPLRVL FEQPTIQALA AYVEGGEESA
1060 1070 1080 1090 1100
YLAIPQAEPQ AYYPVSSAQK RMLILNQLDP HSTVYNLPVA MILEGTLDKA
1110 1120 1130 1140 1150
RLEHAISNLV ARHESLRTSF HTINGEPVSR IHEQGHLPIV YLETAEEQVN
1160 1170 1180 1190 1200
EVILGFMQPF DLVTAPLCRV GLVKLAENRH VLIIDMHHII SDGVSSQLIL
1210 1220 1230 1240 1250
NDFSRLYQNK ALPEQRIHYK DFAVWEKAWT QTTDYQKQEK YWLDRFAGEI
1260 1270 1280 1290 1300
PVLNLPMDYP RPAVQSFEGE RYLFRTEKQL LESLQDVAQK TGTTLYMVLL
1310 1320 1330 1340 1350
AAYHVLLSKY SGQDDVMIGT VTAGRVHPDT ESMTGMFVNT LAMRNQSAPT
1360 1370 1380 1390 1400
KTFRQFLLEV KDNTLAAFEH GQYPFEELVE KLAIQRNRSR NPLFDTLFIL
1410 1420 1430 1440 1450
QNMDADLIEL DGLTVTPYVP EGEVAKFDLS LEASENQAGL SFCFEFCTKL
1460 1470 1480 1490 1500
FARETIERMS LHYLQILQAV SANTEQELAQ IEMLTAHEKQ ELLVHFNDTA
1510 1520 1530 1540 1550
ALYPAESTLS QLFEDQAQKT PEQTAVVFGD KRLTYRELNE RANQLAHTLR
1560 1570 1580 1590 1600
AKGVQAEQSV GIMAQRSLEM AIGIIAILKA GGAYVPIDPD YPNERIAYML
1610 1620 1630 1640 1650
EDCRRLVLTQ QQLAEKMTAN VECLYLDEEG SYSPQTENIE PIHTAADLAY
1660 1670 1680 1690 1700
IIYTSGTTGR PKGVMVEHRG IVNSVTWNRD EFALSVRDSG TLSLSFAFDA
1710 1720 1730 1740 1750
FALTFFTLIV SGSTVVLMPD HEAKDPIALR NLIAAWECSY VVFVPSMFQA
1760 1770 1780 1790 1800
ILECSTPADI RSIQAVMLGG EKLSPKLVQL CKAMHPQMSV MNAYGPTESS
1810 1820 1830 1840 1850
VMATYLRDTQ PDQPITIGRP IANTAIYIVD QHHQLLPVGV VGEICIGGHG
1860 1870 1880 1890 1900
LARGYWKKPE LTAEKFVANP AVPGERMYKT GDLGRWLHDG TIDFIGRVDD
1910 1920 1930 1940 1950
QIKVRGYRIE VGEIEAVLLA YDQTNEAIVV AYQDDRGDSY LAAYVTGKTA
1960 1970 1980 1990 2000
IEESELRAHL LRELPAYMVP TYLIQLDAFP LTPNGKVDRK ALPKPEGKPA
2010 2020 2030 2040 2050
TGAAYVAPAT EVEAKLVAIW ENALGISGVG VLDHFFELGG HSLKAMTVVA
2060 2070 2080 2090 2100
QVHREFQIDL LLKQFFAAPT IRDLARLIEH SEQAAGAAIQ PAEPQAYYPV
2110 2120 2130 2140 2150
SSAQQRMYLL HQLEGAGISY NTPGIIMLEG KLDREQLANA LQALVDRHDI
2160 2170 2180 2190 2200
LRTSFEMVGD ELVQKIHDRV AVNMEYVTAE EQQIDDLFHA FVRPFDLSVP
2210 2220 2230 2240 2250
PLLRMSLVKL ADERHLLLYD MHHIAADAAS ITILFDELAE LYQGRELPEM
2260 2270 2280 2290 2300
RIQYKDFAVW QKALHESDAF KQQEAYWLST FAGNITAVDV PTDFPRPAVK
2310 2320 2330 2340 2350
SFAGGQVTLS MDQELLSALH ELAAHTNTTL FMVLLAAYNV LLAKYAGQDD
2360 2370 2380 2390 2400
IIVGTPISGR SRAELAPVVG MFVHTLAIRN KPTAEKTFKQ FLQEVKQNAL
2410 2420 2430 2440 2450
DAFDHQDYPF ESLVEKLGIP RDPGRNPLFD TMFILQNDEL HAKTLDQLVY
2460 2470 2480 2490 2500
RPYESDSALD VAKFDLSFHL TERETDLFLR LEYCTKLFKQ QTVERMAHHF
2510 2520 2530 2540 2550
LQILRAVTAN PENELQEIEM LTAAEKQMLL VAFNDTHREY RADQTIQQLF
2560 2570 2580 2590 2600
EELAEKMPEH TALVFEEKRM SFRELNERAN QLAAVLREKG VGPAQIVALL
2610 2620 2630 2640 2650
VERSAEMVIA TLATLKAGGA FLPVDPDYPE ERIRYMLEDS QAKLVVTHAH
2660 2670 2680 2690 2700
LLHKVSSQSE VVDVDDPGSY ATQTDNLPCA NTPSDLAYII YTSGTTGKPK
2710 2720 2730 2740 2750
GVMLEHKGVA NLQAVFAHHL GVTPQDRAGH FASISFDASV WDMFGPLLSG
2760 2770 2780 2790 2800
ATLYVLSRDV INDFQRFAEY VRDNAITFLT LPPTYAIYLE PEQVPSLRTL
2810 2820 2830 2840 2850
ITAGSASSVA LVDKWKEKVT YVNGYGPTES TVCATLWKAK PDEPVETITI
2860 2870 2880 2890 2900
GKPIQNTKLY IVDDQLQLKA PGQMGELCIS GLSLARGYWN RPELTAEKFV
2910 2920 2930 2940 2950
DNPFVPGTKM YRTGDLARWL PDGTIEYLGR IDHQVKIRGH RVELGEVESV
2960 2970 2980 2990 3000
LLRYDTVKEA AAITHEDDRG QAYLCAYYVA EGEATPAQLR AYMENELPNY
3010 3020 3030 3040 3050
MVPAFFIQLE KMPLTPNDKI DRKALPKPNQ EENRTEQYAA PQTELEQLLA
3060 3070 3080 3090 3100
GIWADVLGIK QVGTQDNFFE LGGDSIKAIQ VSTRLNASGW TLAMKELFQY
3110 3120 3130 3140 3150
PTIEEAALRV IPNSRESEQG VVEGEIALTP IQKWFFANNF TDRHHWNQAV
3160 3170 3180 3190 3200
MLFREDGFDE GLVRQAFQQI VEHHDALRMV YKQEDGAIKQ INRGLTDERF
3210 3220 3230 3240 3250
RFYSYDLKNH ANSEARILEL SDQIQSSIDL EHGPLVHVAL FATKDGDHLL
3260 3270 3280 3290 3300
VAIHHLVVDG VSWRILFEDF SSAYSQALHQ QEIVLPKKTD SFKDWAAQLQ
3310 3320 3330 3340 3350
KYADSDELLR EVAYWHNLET TTTTAALPTD FVTADRKQKH TRTLSFALTV
3360 3370 3380 3390 3400
PQTENLLRHV HHAYHTEMND LLLTALGLAV KDWAHTNGVV INLEGHGRED
3410 3420 3430 3440 3450
IQNEMNVTRT IGWFTSQYPV VLDMEKAEDL PYQIKQTKEN LRRIPKKGIG
3460 3470 3480 3490 3500
YEILRTLTTS QLQPPLAFTL RPEISFNYLG QFESDGKTGG FTFSPLGTGQ
3510 3520 3530 3540 3550
LFSPESERVF LLDISAMIED GELRISVGYS RLQYEEKTIA SLADSYRKHL
3560 3570 3580
LGIIEHCMAK EEGEYTPSDL GDEELSMEEL ENILEWI
Length:3,587
Mass (Da):404,817
Last modified:January 1, 1998 - v1
Checksum:i322B8471BBB28B47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004835 Genomic DNA. Translation: AAC45929.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004835 Genomic DNA. Translation: AAC45929.1.

3D structure databases

ProteinModelPortaliO30408.
SMRiO30408. Positions 967-1484, 2001-2521, 2524-3029.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00180.
SABIO-RKO30408.

Family and domain databases

Gene3Di1.10.1200.10. 3 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR010060. NRPS_synth.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00501. AMP-binding. 3 hits.
PF13193. AMP-binding_C. 3 hits.
PF00668. Condensation. 4 hits.
PF00550. PP-binding. 3 hits.
[Graphical view]
SMARTiSM00823. PKS_PP. 3 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 3 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 3 hits.
TIGR01720. NRPS-para261. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00455. AMP_BINDING. 3 hits.
PS00012. PHOSPHOPANTETHEINE. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The tyrocidine biosynthesis operon of Bacillus brevis: complete nucleotide sequence and biochemical characterization of functional internal adenylation domains."
    Mootz H.D., Marahiel M.A.
    J. Bacteriol. 179:6843-6850(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 8185 / DSM 362 / JCM 20017 / NBRC 3331 / NCDO 717 / NCIMB 8598 / IAM 1031.

Entry informationi

Entry nameiTYCB_BREPA
AccessioniPrimary (citable) accession number: O30408
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Tyrocidine is a mixture of four cyclic decapeptides, tyrocidine A (D-Phe-Pro-Phe-D-Phe-Asn-Gln-Tyr-Val-Orn-Leu), B, C, and D, in which Phe, at positions 3, 4, and Tyr residues are gradually replaced by Trp, depending on the relative concentrations of these amino acids in the growth medium.

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.