PZNA_BACVZ
ID PZNA_BACVZ Reviewed; 41 AA.
AC D3VML5;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Plantazolicin {ECO:0000303|PubMed:20971906};
DE Short=PZN {ECO:0000303|PubMed:20971906};
DE AltName: Full=Plantazolicin A {ECO:0000303|PubMed:21568297};
DE AltName: Full=Plantazolicin B {ECO:0000303|PubMed:21568297};
DE AltName: Full=cpd1335 {ECO:0000303|PubMed:20971906};
DE Flags: Precursor;
GN Name=pznA {ECO:0000303|PubMed:20971906};
GN Synonyms=ptnA {ECO:0000312|EMBL:CBJ61635.1}; OrderedLocusNames=RBAM_007445;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=326423;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=20971906; DOI=10.1128/jb.00784-10;
RA Scholz R., Molohon K.J., Nachtigall J., Vater J., Markley A.L.,
RA Sussmuth R.D., Mitchell D.A., Borriss R.;
RT "Plantazolicin, a novel microcin B17/streptolysin S-like natural product
RT from Bacillus amyloliquefaciens FZB42.";
RL J. Bacteriol. 193:215-224(2011).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant growth-
RT promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(2007).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 28-41, FUNCTION, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, METHYLATION AT ARG-28, AND STRUCTURE.
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=21950656; DOI=10.1021/cb200339d;
RA Molohon K.J., Melby J.O., Lee J., Evans B.S., Dunbar K.L., Bumpus S.B.,
RA Kelleher N.L., Mitchell D.A.;
RT "Structure determination and interception of biosynthetic intermediates for
RT the plantazolicin class of highly discriminating antibiotics.";
RL ACS Chem. Biol. 6:1307-1313(2011).
RN [4] {ECO:0000305}
RP STRUCTURE BY NMR, AND MASS SPECTROMETRY.
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=21568297; DOI=10.1021/ol200809m;
RA Kalyon B., Helaly S.E., Scholz R., Nachtigall J., Vater J., Borriss R.,
RA Sussmuth R.D.;
RT "Plantazolicin A and B: structure elucidation of ribosomally synthesized
RT thiazole/oxazole peptides from Bacillus amyloliquefaciens FZB42.";
RL Org. Lett. 13:2996-2999(2011).
CC -!- FUNCTION: Peptide antibiotic inhibiting growth of Gram-positive
CC bacteria in the dimethylated form plantazolicin A. The desmethyl form
CC plantazolicin B has no antibiotic activity. The mode of action appears
CC to be disruption of cell walls and lysis of cells. Inhibits B.subtilis
CC strain HB0042, B.megaterium strain 7A1 and B.anthracis (MIC=2-4 ug/ml).
CC Weakly inhibits Gram-positive bacteria B.brevis strain ATCC 8246,
CC B.subtilis strain 168, B.cereus strain ATCC 14579 and strain CU1065,
CC B.licheniformis strain ATCC 9789, M.luteus, B.sphaericus, P.granivorans
CC and S.pyogenes (MIC=128 ug/ml). Does not inhibit B.pumilus, P.polymyxa,
CC Arthrobacter sp., S.aureus, vancomycin-resistant E.faecalis,
CC L.monocytogenes, methicillin-resistant S.aureus or Gram-negative
CC bacteria E.coli strain K12, K.terrigena, Pseudomonas sp. and
CC E.carotovora. {ECO:0000269|PubMed:20971906,
CC ECO:0000269|PubMed:21950656}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:20971906,
CC ECO:0000269|PubMed:21950656}.
CC -!- PTM: Maturation of thiazole and oxazole containing antibiotics involves
CC the enzymatic condensation of a Cys, Ser or Thr with the alpha-carbonyl
CC of the preceding amino acid to form a thioether or ether bond, then
CC dehydration to form a double bond with the alpha-amino nitrogen.
CC Thiazoline or oxazoline ring are dehydrogenated to form thiazole or
CC oxazole rings. {ECO:0000305}.
CC -!- PTM: 2 forms exist: plantazolicin A and plantazolicin B. The structural
CC difference between them is a dimethylation at Arg-28 in plantazolicin
CC A. {ECO:0000269|PubMed:21568297}.
CC -!- MASS SPECTROMETRY: Mass=1336.6; Method=Electrospray; Note=Plantazolicin
CC A.; Evidence={ECO:0000269|PubMed:20971906,
CC ECO:0000269|PubMed:21568297};
CC -!- MASS SPECTROMETRY: Mass=1308.5; Method=Electrospray; Note=Plantazolicin
CC B.; Evidence={ECO:0000269|PubMed:20971906,
CC ECO:0000269|PubMed:21568297};
CC -!- MASS SPECTROMETRY: Mass=1336.4783; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21950656};
CC -!- MASS SPECTROMETRY: Mass=1336.48; Method=Electrospray;
CC Note=Plantazolicin A.; Evidence={ECO:0000269|PubMed:20971906,
CC ECO:0000269|PubMed:21568297};
CC -!- MASS SPECTROMETRY: Mass=1308.44; Method=Electrospray;
CC Note=Plantazolicin B.; Evidence={ECO:0000269|PubMed:20971906,
CC ECO:0000269|PubMed:21568297};
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; FN668567; CBJ61635.1; -; Genomic_DNA.
DR EMBL; CP000560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; D3VML5; -.
DR iPTMnet; D3VML5; -.
DR Proteomes; UP000001120; Chromosome.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0009275; C:Gram-positive-bacterium-type cell wall; IDA:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0001897; P:cytolysis by symbiont of host cells; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR InterPro; IPR026474; Plantazolicin.
DR TIGRFAMs; TIGR04218; TOMM_plantaz; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Bacteriocin; Cell wall;
KW Direct protein sequencing; Methylation; Secreted; Thioether bond.
FT PROPEP 1..27
FT /evidence="ECO:0000269|PubMed:20971906,
FT ECO:0000269|PubMed:21950656"
FT /id="PRO_0000415155"
FT PEPTIDE 28..41
FT /note="Plantazolicin"
FT /evidence="ECO:0000269|PubMed:21950656"
FT /id="PRO_0000415156"
FT MOD_RES 28
FT /note="N2,N2-dimethylarginine"
FT /evidence="ECO:0000269|PubMed:21568297,
FT ECO:0000269|PubMed:21950656"
FT CROSSLNK 28..29
FT /note="Thiazole-4-carboxylic acid (Arg-Cys)"
FT /evidence="ECO:0000269|PubMed:21568297,
FT ECO:0000269|PubMed:21950656"
FT CROSSLNK 29..30
FT /note="5-methyloxazole-4-carboxylic acid (Cys-Thr)"
FT /evidence="ECO:0000269|PubMed:21568297,
FT ECO:0000269|PubMed:21950656"
FT CROSSLNK 30..31
FT /note="Thiazole-4-carboxylic acid (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:21568297,
FT ECO:0000269|PubMed:21950656"
FT CROSSLNK 31..32
FT /note="5-methyloxazole-4-carboxylic acid (Cys-Thr)"
FT /evidence="ECO:0000269|PubMed:21568297,
FT ECO:0000269|PubMed:21950656"
FT CROSSLNK 32..33
FT /note="5-methyloxazole-4-carboxylic acid (Thr-Thr)"
FT /evidence="ECO:0000269|PubMed:21568297,
FT ECO:0000269|PubMed:21950656"
FT CROSSLNK 35..36
FT /note="Oxazole-4-carboxylic acid (Ile-Ser)"
FT /evidence="ECO:0000269|PubMed:21568297,
FT ECO:0000269|PubMed:21950656"
FT CROSSLNK 36..37
FT /note="Oxazole-4-carboxylic acid (Ser-Ser)"
FT /evidence="ECO:0000269|PubMed:21568297,
FT ECO:0000269|PubMed:21950656"
FT CROSSLNK 37..38
FT /note="Oxazole-4-carboxylic acid (Ser-Ser)"
FT /evidence="ECO:0000269|PubMed:21568297,
FT ECO:0000269|PubMed:21950656"
FT CROSSLNK 38..39
FT /note="Oxazole-4-carboxylic acid (Ser-Ser)"
FT /evidence="ECO:0000269|PubMed:21568297,
FT ECO:0000269|PubMed:21950656"
FT CROSSLNK 39..40
FT /note="5-methyloxazoline-4-carboxylic acid (Ser-Thr)"
FT /evidence="ECO:0000269|PubMed:21568297,
FT ECO:0000269|PubMed:21950656"
SQ SEQUENCE 41 AA; 4366 MW; 65EDC0E4EF44DF52 CRC64;
MTQIKVPTAL IASVHGEGQH LFEPMAARCT CTTIISSSST F
