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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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