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WSNA_WEIPA
ID   WSNA_WEIPA              Reviewed;          43 AA.
AC   B3A0N4;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Bacteriocin weissellin-A {ECO:0000303|PubMed:21511463};
DE   Flags: Fragment;
OS   Weissella paramesenteroides (Leuconostoc paramesenteroides).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Weissella.
OX   NCBI_TaxID=1249;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, AND MASS SPECTROMETRY.
RC   STRAIN=DX {ECO:0000269|PubMed:21511463};
RX   PubMed=21511463; DOI=10.1016/j.biortech.2011.03.106;
RA   Papagianni M., Papamichael E.M.;
RT   "Purification, amino acid sequence and characterization of the class IIa
RT   bacteriocin weissellin A, produced by Weissella paramesenteroides DX.";
RL   Bioresour. Technol. 102:6730-6734(2011).
CC   -!- FUNCTION: Highly active against Gram-positive bacteria M.flavus strain
CC       ATCC 400, M.luteus strain CECT241, C.soprogenes strain NCTC533,
CC       L.monocytogenes strain ATCC 19111, L.inocua strain ATCC BAA-680D and
CC       S.carnosus strain LMG13564. Less active against B.cereus strain
CC       LMG13569, C.thiaminolyticum strain ATCC 15579, E.faecalis strain
CC       NCTC8176, L.lactis strain LM0230, L.casei strain ATCC 344, L.lactis
CC       strain IL1403, L.jensenii strain ATCC 25258, L.plantarum strain
CC       CECT220, L.brevis strain ATCC 8287, L.bulgaricus strain LMG13551,
CC       P.acidilactici strain ATCC 25740, P.pentosaceus strain ATCC 33316 and
CC       P.pentosaceus strain LMG13560. Weakly active against L.mesenteroides
CC       strain ATCC 19254, L.lactis strain ATCC 1454, L.sakei strain CECT906T,
CC       L.lactis subsp. cremoris strain MC1363 and L.curvatus strain ATCC
CC       51436. Not active against Gram-negative bacterium S.enteritidis strain
CC       ATCC 13076. The mode of action appears to be non-lytic. Inactivated by
CC       proteinase K, but insensitive to trypsin, alpha-chymotrypsin, pepsin
CC       and papain. {ECO:0000269|PubMed:21511463}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Remains active between pH 2 and 10. {ECO:0000269|PubMed:21511463};
CC       Temperature dependence:
CC         Remains active after incubation at 121 degrees Celsius for 1 hour.
CC         {ECO:0000269|PubMed:21511463};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21511463}.
CC       Note=Partly adsorbed to cell wall. {ECO:0000269|PubMed:21511463}.
CC   -!- MASS SPECTROMETRY: Mass=4450; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:21511463};
CC   -!- SIMILARITY: Belongs to the bacteriocin class IIA/YGNGV family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; B3A0N4; -.
DR   SMR; B3A0N4; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
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; Secreted.
FT   CHAIN           1..>43
FT                   /note="Bacteriocin weissellin-A"
FT                   /id="PRO_0000414627"
FT   DISULFID        9..14
FT                   /evidence="ECO:0000250|UniProtKB:P29430"
FT   NON_TER         43
FT                   /evidence="ECO:0000303|PubMed:21511463"
SQ   SEQUENCE   43 AA;  4449 MW;  97A1D080B7A931D1 CRC64;
     KNYGNGVYCN KHKCSVDWAT FSANIANNSV AMAGLTGGNA GNK
 
 
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