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MUTI_ENTMU
ID   MUTI_ENTMU              Reviewed;          43 AA.
AC   P80925;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Bacteriocin mundticin;
OS   Enterococcus mundtii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=53346;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   STRAIN=ATO6;
RX   PubMed=9733915; DOI=10.1016/s0005-2736(98)00086-8;
RA   Bennik M.H.J., Vanloo B., Brasseur R., Gorris L.G.M., Smid E.J.;
RT   "A novel bacteriocin with a YGNGV motif from vegetable-associated
RT   Enterococcus mundtii: full characterization and interaction with target
RT   organisms.";
RL   Biochim. Biophys. Acta 1373:47-58(1998).
CC   -!- FUNCTION: This bacteriocin inhibits the growth of several Gram-positive
CC       bacteria, especially pathogenic L.monocytogenes and C.botulinum but has
CC       no effect on the growth of a number of yeasts and Gram-negative
CC       bacteria.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Stable from pH 1 to 10.;
CC       Temperature dependence:
CC         Thermostable. Retains 100% of its maximal activity after heating at
CC         100 degrees Celsius for 15 min, but only 50% of activity after
CC         heating 1 hour at this same temperature.;
CC   -!- MASS SPECTROMETRY: Mass=4287.21; Mass_error=0.59; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9733915};
CC   -!- SIMILARITY: Belongs to the bacteriocin class IIA/YGNGV family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P80925; -.
DR   SMR; P80925; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.130; -; 1.
DR   InterPro; IPR002633; Bacteriocin_IIa.
DR   InterPro; IPR023384; Bacteriocin_IIa_CS.
DR   InterPro; IPR023388; Bacteriocin_IIa_dom_sf.
DR   Pfam; PF01721; Bacteriocin_II; 1.
DR   PROSITE; PS60030; BACTERIOCIN_IIA; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW   Disulfide bond.
FT   PEPTIDE         1..43
FT                   /note="Bacteriocin mundticin"
FT                   /id="PRO_0000110572"
FT   DISULFID        9..14
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   43 AA;  4290 MW;  9438645EE055097D CRC64;
     KYYGNGVSCN KKGCSVDWGK AIGIIGNNSA ANLATGGAAG WSK
 
 
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