TYCA_BREPA
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-AUG-2022, entry version 126.
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; 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=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 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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-62.
RX PubMed=3032912; DOI=10.1128/jb.169.5.2215-2222.1987;
RA Marahiel M.A., Zuber P., Czekay G., Losick R.;
RT "Identification of the promoter for a peptide antibiotic biosynthesis gene
RT 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., von Dohren H.,
RA Kleinkauf H.;
RT "ATP binding in peptide synthetases: determination of contact sites of the
RT adenine moiety by photoaffinity labeling of tyrocidine synthetase 1 with 2-
RT 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 8598
RC / IAM 1031;
RX PubMed=2768192; DOI=10.1128/jb.171.9.4881-4887.1989;
RA Mittenhuber G., Weckermann R., Marahiel M.A.;
RT "Gene cluster containing the genes for tyrocidine synthetases 1 and 2 from
RT Bacillus brevis: evidence for an operon.";
RL J. Bacteriol. 171:4881-4887(1989).
CC -!- FUNCTION: In the first step of peptide synthesis this enzyme activates
CC phenylalanine and racemizes it to the D-isomer.
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: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 the
CC peptide product and can be further subdivided into domains responsible
CC for substrate adenylation, thiolation, condensation (not for the
CC initiation module), and epimerization (optional), and N methylation
CC (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; 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 PDB; 5N81; X-ray; 1.60 A; A/B=3-418.
DR PDB; 5N82; X-ray; 1.71 A; A=3-418.
DR PDBsum; 5N81; -.
DR PDBsum; 5N82; -.
DR AlphaFoldDB; P09095; -.
DR SMR; P09095; -.
DR STRING; 54914.AV540_22690; -.
DR PRIDE; P09095; -.
DR KEGG; ag:AAC45928; -.
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 GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
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; IPR020459; AMP-binding.
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; IPR009081; PP-bd_ACP.
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; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; ATP-binding;
KW Direct protein sequencing; Isomerase; Ligase; Multifunctional enzyme;
KW Nucleotide-binding; Phosphopantetheine; Phosphoprotein.
FT CHAIN 1..1088
FT /note="Tyrocidine synthase 1"
FT /id="PRO_0000193093"
FT DOMAIN 528..602
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 563
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 197..242
FT /note="NLQSFFQNSFGVTEQDRIGLFASMSFDASVWEMFMALLSGASLYIL -> IC
FT NPFSKIRLASPSKTGSGFLPACRSTHPFGKCSWLCCLAPRVHP (in Ref. 1;
FT CAA31623)"
FT /evidence="ECO:0000305"
FT CONFLICT 359..360
FT /note="GS -> AD (in Ref. 1; CAA31623)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="L -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="L -> V (in Ref. 1; CAA31623)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="L -> F (in Ref. 1; CAA31623)"
FT /evidence="ECO:0000305"
FT CONFLICT 756..790
FT /note="EDLATGYAQALAGQAISLPEKTDSFQSWSQWLQEY -> KIWQPDTRRHLQG
FT KRSVCPKKRILFKAGHNGCKNN (in Ref. 1; CAA31623)"
FT /evidence="ECO:0000305"
FT CONFLICT 876..894
FT /note="QIVIHLEGHGREDIIEQAN -> KSSFIWRGTGARTSSNRQT (in Ref.
FT 1; CAA31623)"
FT /evidence="ECO:0000305"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 55..72
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:5N81"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:5N81"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:5N81"
FT HELIX 379..385
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 395..406
FT /evidence="ECO:0007829|PDB:5N81"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:5N81"
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
