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LANA_BLAHA
ID   LANA_BLAHA              Reviewed;          47 AA.
AC   P83675; P83679; P83680; Q8VLK0;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Ruminococcin-A;
DE   Flags: Precursor;
GN   Name=rumA1;
GN   and
GN   Name=rumA2;
GN   and
GN   Name=rumA3;
OS   Blautia hansenii (Ruminococcus hansenii).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=1322 {ECO:0000312|EMBL:AAL73934.1};
RN   [1] {ECO:0000312|EMBL:AAL73934.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (RUMA1; RUMA2 AND RUMA3).
RC   STRAIN=LEMV98 {ECO:0000312|EMBL:AAL73934.1};
RX   PubMed=12089024; DOI=10.1128/aem.68.7.3424-3431.2002;
RA   Marcille F., Gomez A., Joubert P., Ladire M., Veau G., Clara A., Gavini F.,
RA   Willems A., Fons M.;
RT   "Distribution of genes encoding the trypsin-dependent lantibiotic
RT   ruminococcin A among bacteria isolated from human fecal microbiota.";
RL   Appl. Environ. Microbiol. 68:3424-3431(2002).
CC   -!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic)
CC       active on Gram-positive bacteria. The bactericidal activity of
CC       lantibiotics is based on depolarization of energized bacterial
CC       cytoplasmic membranes, initiated by the formation of aqueous
CC       transmembrane pores. Ruminococcin A is a broad spectrum bacteriocin
CC       exhibiting activity against a wide range of pathogenic clostridia and
CC       B.longum (By similarity). {ECO:0000250|UniProtKB:P36499,
CC       ECO:0000250|UniProtKB:P83677}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83677}.
CC   -!- PTM: Maturation of lantibiotics involves the enzymatic conversion of
CC       Thr, and Ser into dehydrated AA and the formation of thioether bonds
CC       with cysteine. This is followed by membrane translocation and cleavage
CC       of the modified precursor. {ECO:0000303|PubMed:12089024}.
CC   -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000305}.
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DR   EMBL; AF439552; AAL73934.1; -; Genomic_DNA.
DR   EMBL; AF439552; AAL73935.1; -; Genomic_DNA.
DR   EMBL; AF439552; AAL73936.1; -; Genomic_DNA.
DR   AlphaFoldDB; P83675; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR   GO; GO:0006965; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-positive bacteria; ISS:UniProtKB.
DR   InterPro; IPR007682; Lantibiotic_typ-A_Lactobact.
DR   Pfam; PF04604; L_biotic_typeA; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Bacteriocin; Lantibiotic; Secreted; Signal;
KW   Thioether bond.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         24..47
FT                   /note="Ruminococcin-A"
FT                   /id="PRO_0000017126"
FT   MOD_RES         30
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000250|UniProtKB:P83674"
FT   MOD_RES         39
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000250|UniProtKB:P83674"
FT   CROSSLNK        30..35
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P83674"
FT   CROSSLNK        32..46
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P83674"
FT   CROSSLNK        45..47
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P83674"
SQ   SEQUENCE   47 AA;  5346 MW;  2A77213404D1FED9 CRC64;
     MRNDVLTLTN PMEENELEQI LGGGNGVLKT ISHECNMNTW QFLFTCC
 
 
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