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 03-APR-2013, entry version 98.
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: Binds 1 phosphopantetheine covalently (Potential).
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.
CC -!- SIMILARITY: Contains 1 acyl carrier domain.
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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: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; 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; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PRINTS; PR00154; AMPBINDING.
DR SUPFAM; SSF47336; ACP_like; 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.
FT CHAIN 1 1088 Tyrocidine synthase 1.
FT /FTId=PRO_0000193093.
FT DOMAIN 533 599 Acyl carrier.
FT MOD_RES 563 563 O-(pantetheine 4'-phosphoryl)serine (By
FT similarity).
FT CONFLICT 197 242 NLQSFFQNSFGVTEQDRIGLFASMSFDASVWEMFMALLSGA
FT SLYIL -> ICNPFSKIRLASPSKTGSGFLPACRSTHPFGK
FT CSWLCCLAPRVHP (in Ref. 1; CAA31623).
FT CONFLICT 359 360 GS -> AD (in Ref. 1; CAA31623).
FT CONFLICT 496 496 L -> I (in Ref. 4; AA sequence).
FT CONFLICT 665 665 L -> V (in Ref. 1; CAA31623).
FT CONFLICT 737 737 L -> F (in Ref. 1; CAA31623).
FT CONFLICT 756 790 EDLATGYAQALAGQAISLPEKTDSFQSWSQWLQEY -> KI
FT WQPDTRRHLQGKRSVCPKKRILFKAGHNGCKNN (in
FT Ref. 1; CAA31623).
FT CONFLICT 876 894 QIVIHLEGHGREDIIEQAN -> KSSFIWRGTGARTSSNRQ
FT T (in Ref. 1; CAA31623).
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
//
