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Database: UniProt
Entry: P09095
LinkDB: P09095
Original site: P09095 
ID   TYCA_BREPA              Reviewed;        1088 AA.
AC   P09095; O30407;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   26-NOV-2014, entry version 103.
DE   RecName: Full=Tyrocidine synthase 1;
DE   AltName: Full=Tyrocidine synthase I;
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=tycA;
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=3267240; DOI=10.1093/nar/16.24.11841;
RA   Weckermann R., Fuerbass R., Marahiel M.A.;
RT   "Complete nucleotide sequence of the tycA gene coding the tyrocidine
RT   synthetase 1 from Bacillus brevis.";
RL   Nucleic Acids Res. 16:11841-11841(1988).
RN   [2]
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-62.
RX   PubMed=3032912;
RA   Marahiel M.A., Zuber P., Czekay G., Losick R.;
RT   "Identification of the promoter for a peptide antibiotic biosynthesis
RT   gene from Bacillus brevis and its regulation in Bacillus subtilis.";
RL   J. Bacteriol. 169:2215-2222(1987).
RN   [4]
RP   PROTEIN SEQUENCE OF 374-385; 406-417 AND 484-496.
RX   PubMed=8193142; DOI=10.1021/bi00186a030;
RA   Pavela-Vrancic M., Pfeifer E., van Liempt H., Schafer H.J.,
RA   von Dohren H., Kleinkauf H.;
RT   "ATP binding in peptide synthetases: determination of contact sites of
RT   the adenine moiety by photoaffinity labeling of tyrocidine synthetase
RT   1 with 2-azidoadenosine triphosphate.";
RL   Biochemistry 33:6276-6283(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1018-1088.
RC   STRAIN=ATCC 8185 / DSM 362 / JCM 20017 / NBRC 3331 / NCDO 717 / NCIMB
RC   8598 / IAM 1031;
RX   PubMed=2768192;
RA   Mittenhuber G., Weckermann R., Marahiel M.A.;
RT   "Gene cluster containing the genes for tyrocidine synthetases 1 and 2
RT   from Bacillus brevis: evidence for an operon.";
RL   J. Bacteriol. 171:4881-4887(1989).
CC   -!- FUNCTION: In the first step of peptide synthesis this enzyme
CC       activates phenylalanine and racemizes it to the D-isomer.
CC   -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + H(2)O = AMP +
CC       diphosphate + D-phenylalanine.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000305};
CC       Note=Binds 1 phosphopantetheine covalently. {ECO:0000305};
CC   -!- PATHWAY: Antibiotic biosynthesis; tyrocidine biosynthesis.
CC   -!- SUBUNIT: Large multienzyme complex of TycA, TycB and TycC.
CC   -!- DOMAIN: One-module-bearing peptide synthase with 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 1 acyl carrier domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00258}.
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DR   EMBL; X13237; CAA31623.1; -; Genomic_DNA.
DR   EMBL; AF004835; AAC45928.1; -; Genomic_DNA.
DR   EMBL; M16442; AAA22876.1; ALT_FRAME; mRNA.
DR   PIR; A26878; A26878.
DR   PIR; T31074; YGBSTB.
DR   ProteinModelPortal; P09095; -.
DR   SMR; P09095; 23-518.
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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020459; AMP-binding.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR010060; NRPS_synth.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PRINTS; PR00154; AMPBINDING.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   TIGRFAMs; TIGR01720; NRPS-para261; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; ATP-binding; Direct protein sequencing;
KW   Isomerase; Ligase; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphopantetheine; Phosphoprotein.
FT   CHAIN         1   1088       Tyrocidine synthase 1.
FT                                /FTId=PRO_0000193093.
FT   DOMAIN      533    599       Acyl carrier. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   MOD_RES     563    563       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
FT   CONFLICT    197    242       NLQSFFQNSFGVTEQDRIGLFASMSFDASVWEMFMALLSGA
FT                                SLYIL -> ICNPFSKIRLASPSKTGSGFLPACRSTHPFGK
FT                                CSWLCCLAPRVHP (in Ref. 1; CAA31623).
FT                                {ECO:0000305}.
FT   CONFLICT    359    360       GS -> AD (in Ref. 1; CAA31623).
FT                                {ECO:0000305}.
FT   CONFLICT    496    496       L -> I (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    665    665       L -> V (in Ref. 1; CAA31623).
FT                                {ECO:0000305}.
FT   CONFLICT    737    737       L -> F (in Ref. 1; CAA31623).
FT                                {ECO:0000305}.
FT   CONFLICT    756    790       EDLATGYAQALAGQAISLPEKTDSFQSWSQWLQEY -> KI
FT                                WQPDTRRHLQGKRSVCPKKRILFKAGHNGCKNN (in
FT                                Ref. 1; CAA31623). {ECO:0000305}.
FT   CONFLICT    876    894       QIVIHLEGHGREDIIEQAN -> KSSFIWRGTGARTSSNRQ
FT                                T (in Ref. 1; CAA31623). {ECO:0000305}.
SQ   SEQUENCE   1088 AA;  122672 MW;  6AC4804199572027 CRC64;
     MLANQANLID NKRELEQHAL VPYAQGKSIH QLFEEQAEAF PDRVAIVFEN RRLSYQELNR
     KANQLARALL EKGVQTDSIV GVMMEKSIEN VIAILAVLKA GGAYVPIDIE YPRDRIQYIL
     QDSQTKIVLT QKSVSQLVHD VGYSGEVVVL DEEQLDARET ANLHQPSKPT DLAYVIYTSG
     TTGKPKGTML EHKGIANLQS FFQNSFGVTE QDRIGLFASM SFDASVWEMF MALLSGASLY
     ILSKQTIHDF AAFEHYLSEN ELTIITLPPT YLTHLTPERI TSLRIMITAG SASSAPLVNK
     WKDKLRYINA YGPTETSICA TIWEAPSNQL SVQSVPIGKP IQNTHIYIVN EDLQLLPTGS
     EGELCIGGVG LARGYWNRPD LTAEKFVDNP FVPGEKMYRT GDLAKWLTDG TIEFLGRIDH
     QVKIRGHRIE LGEIESVLLA HEHITEAVVI AREDQHAGQY LCAYYISQQE ATPAQLRDYA
     AQKLPAYMLP SYFVKLDKMP LTPNDKIDRK ALPEPDLTAN QSQAAYHPPR TETESILVSI
     WQNVLGIEKI GIRDNFYSLG GDSIQAIQVV ARLHSYQLKL ETKDLLNYPT IEQVALFVKS
     TTRKSDQGII AGNVPLTPIQ KWFFGKNFTN TGHWNQSSVL YRPEGFDPKV IQSVMDKIIE
     HHDALRMVYQ HENGNVVQHN RGLGGQLYDF FSYNLTAQPD VQQAIEAETQ RLHSSMNLQE
     GPLVKVALFQ TLHGDHLFLA IHHLVVDGIS WRILFEDLAT GYAQALAGQA ISLPEKTDSF
     QSWSQWLQEY ANEADLLSEI PYWESLESQA KNVSLPKDYE VTDCKQKSVR NMRIRLHPEE
     TEQLLKHANQ AYQTEINDLL LAALGLAFAE WSKLAQIVIH LEGHGREDII EQANVARTVG
     WFTSQYPVLL DLKQTAPLSD YIKLTKENMR KIPRKGIGYD ILKHVTLPEN RGSLSFRVQP
     EVTFNYLGQF DADMRTELFT RSPYSGGNTL GADGKNNLSP ESEVYTALNI TGLIEGGELV
     LTFSYSSEQY REESIQQLSQ SYQKHLLAII AHCTEKKEVE RTPSDFSVKG LQMEEMDDIF
     ELLANTLR
//
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