LANLB_BACLD
ID LANLB_BACLD Reviewed; 69 AA.
AC P86720;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Lantibiotic lichenicidin A2 {ECO:0000303|PubMed:19561184, ECO:0000303|PubMed:19707558};
DE Short=LchA2 {ECO:0000250|UniProtKB:P86476};
DE AltName: Full=BliA2 {ECO:0000303|PubMed:19561184};
DE Flags: Precursor;
GN Name=lanA2 {ECO:0000303|PubMed:19561184};
GN Synonyms=licA2 {ECO:0000303|PubMed:19707558};
GN OrderedLocusNames=BLi04126.1, BL05375.1;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
RN [3] {ECO:0000305}
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX PubMed=19561184; DOI=10.1128/aem.00730-09;
RA Begley M., Cotter P.D., Hill C., Ross R.P.;
RT "Identification of a novel two-peptide lantibiotic, lichenicidin, following
RT rational genome mining for LanM proteins.";
RL Appl. Environ. Microbiol. 75:5451-5460(2009).
RN [4] {ECO:0000305}
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX PubMed=19707558; DOI=10.1371/journal.pone.0006788;
RA Dischinger J., Josten M., Szekat C., Sahl H.G., Bierbaum G.;
RT "Production of the novel two-peptide lantibiotic lichenicidin by Bacillus
RT licheniformis DSM 13.";
RL PLoS ONE 4:E6788-E6788(2009).
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. When present individually, LchA2 exhibits activity
CC towards L.lactis HP. When combined with LchA1, it displays activity
CC towards a broad spectrum of non-pathogenic and pathogenic Gram-positive
CC bacteria including strains of L.monocytogenes, methicillin-resistant
CC S.aureus, S.pneumoniae and strains of vancomycin-resistant enterococci,
CC but not towards E.faecium L4001 and BM4147-1. Combined LchA1 and LchA2
CC peptides also inhibit Bacillus sp. HIL-Y85/54728, L.lactis DPC3417 and
CC B.halodurans C-125, which produce lantibiotics themselves. Inactivated
CC by proteinase K and pronase E, but not by trypsin and chymotrypsin.
CC {ECO:0000269|PubMed:19561184, ECO:0000269|PubMed:19707558}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:19561184,
CC ECO:0000269|PubMed:19707558}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:O87237}.
CC -!- MASS SPECTROMETRY: Mass=3020.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19561184, ECO:0000269|PubMed:19707558};
CC -!- MASS SPECTROMETRY: Mass=3020.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19561184, ECO:0000269|PubMed:19707558};
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DR EMBL; AE017333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP000002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P86720; -.
DR SMR; P86720; -.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009275; C:Gram-positive-bacterium-type cell wall; IDA: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; IDA:UniProtKB.
DR InterPro; IPR027632; Lant_SP_1948.
DR Pfam; PF16934; Mersacidin; 1.
DR TIGRFAMs; TIGR03893; lant_SP_1948; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Bacteriocin; Cell wall; Lantibiotic;
KW Reference proteome; Secreted; Thioether bond.
FT PROPEP 1..37
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT /id="PRO_0000399040"
FT PEPTIDE 38..69
FT /note="Lantibiotic lichenicidin A2"
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT /id="PRO_0000399041"
FT MOD_RES 38
FT /note="2-oxobutanoic acid"
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT MOD_RES 39
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT MOD_RES 42
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT MOD_RES 43
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT MOD_RES 45
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT MOD_RES 50
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT MOD_RES 54
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT MOD_RES 63
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT CROSSLNK 44..48
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT CROSSLNK 56..60
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT CROSSLNK 62..65
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000250|UniProtKB:P86476"
FT CROSSLNK 66..69
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000250|UniProtKB:P86476"
SQ SEQUENCE 69 AA; 7088 MW; 72F41C9E5C7FD3B6 CRC64;
MKNSAAREAF KGANHPAGMV SEEELKALVG GNDVNPETTP ATTSSWTCIT AGVTVSASLC
PTTKCTSRC
