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TFXA_RHILT
ID   TFXA_RHILT              Reviewed;          42 AA.
AC   P42723;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Trifolitoxin;
DE            Short=TFX;
DE   Flags: Precursor;
GN   Name=tfxA;
OS   Rhizobium leguminosarum bv. trifolii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T24;
RX   PubMed=8509324; DOI=10.1128/jb.175.12.3693-3702.1993;
RA   Breil B.T., Ludden P.W., Triplett E.W.;
RT   "DNA sequence and mutational analysis of genes involved in the production
RT   and resistance of the antibiotic peptide trifolitoxin.";
RL   J. Bacteriol. 175:3693-3702(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 32-42.
RA   Lethbridge B.J.;
RL   Thesis (1989), University of Adelaide, Australia.
CC   -!- FUNCTION: Antibiotic whose production provides the bacterium a
CC       mechanism of host root nodule competitiveness with other invading
CC       inefficient strains.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Sensitive to extremes of pH.;
CC       Temperature dependence:
CC         Thermostable.;
CC   -!- PTM: Synthesized ribosomally as a prepeptide that is post-
CC       translationally modified to the active peptide. TfxB, TfxD and TfxF are
CC       all required for this processing.
CC   -!- PTM: The chromophore is probably a six-membered ring derived from the
CC       cyclization of Gln-38.
CC   -!- PTM: Maturation of thiazole and oxazole containing antibiotics involves
CC       the enzymatic condensation of a Cys, Ser or Thr with the alpha-carbonyl
CC       of the preceding amino acid to form a thioether or ether bond, then
CC       dehydration to form a double bond with the alpha-amino nitrogen.
CC       Thiazoline or oxazoline rings are dehydrogenated to form thiazole or
CC       oxazole rings.
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DR   EMBL; L06719; AAA26363.1; -; Genomic_DNA.
DR   PIR; A47116; A47116.
DR   AlphaFoldDB; P42723; -.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW   Thioether bond.
FT   PROPEP          1..31
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="PRO_0000002778"
FT   PEPTIDE         32..42
FT                   /note="Trifolitoxin"
FT                   /evidence="ECO:0000269|PubMed:8509324"
FT                   /id="PRO_0000002779"
FT   MOD_RES         38
FT                   /note="Glutamine derivative"
FT                   /evidence="ECO:0000269|PubMed:8509324"
FT   CROSSLNK        39..40
FT                   /note="Thiazole-4-carboxylic acid (Gly-Cys)"
FT                   /evidence="ECO:0000269|PubMed:8509324"
SQ   SEQUENCE   42 AA;  4406 MW;  BC1F91116818E3D7 CRC64;
     MDNKVAKNVE VKKGSIKATF KAAVLKSKTK VDIGGSRQGC VA
 
 
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