KAWA_MICA8
ID KAWA_MICA8 Reviewed; 87 AA.
AC A0A139GI49;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Kawaguchipeptin peptide {ECO:0000303|PubMed:26846478};
DE AltName: Full=Cyclic cyanobactin {ECO:0000303|PubMed:26846478};
DE Contains:
DE RecName: Full=Kawaguchipeptin A {ECO:0000303|Ref.3};
DE AltName: Full=Non-posttranslationnaly modified kawaguchipeptin B {ECO:0000303|PubMed:26846478, ECO:0000303|PubMed:9249979};
DE Flags: Precursor;
GN Name=kgpE {ECO:0000303|PubMed:26846478, ECO:0000312|EMBL:KXS89845.1};
GN ORFNames=OA58_19045 {ECO:0000312|EMBL:KXS89845.1};
OS Microcystis aeruginosa (strain NIES-88 / KW-MA1-3).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=449441;
RN [1] {ECO:0000312|EMBL:KXS89845.1, ECO:0000312|Proteomes:UP000070196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], EXPRESSION IN E.COLI, AND
RP MASS SPECTROMETRY.
RC STRAIN=NIES-88 / KW-MA1-3;
RX PubMed=26846478; DOI=10.1002/anie.201509920;
RA Parajuli A., Kwak D.H., Dalponte L., Leikoski N., Galica T., Umeobika U.,
RA Trembleau L., Bent A., Sivonen K., Wahlsten M., Wang H., Rizzi E.,
RA De Bellis G., Naismith J., Jaspars M., Liu X., Houssen W., Fewer D.P.;
RT "A unique tryptophan C-prenyltransferase from the kawaguchipeptin
RT biosynthetic pathway.";
RL Angew. Chem. Int. Ed. Engl. 55:3596-3599(2016).
RN [2]
RP ERRATUM.
RX PubMed=28045232; DOI=10.1002/anie.201609949;
RA Parajuli A., Kwak D.H., Dalponte L., Leikoski N., Galica T., Umeobika U.,
RA Trembleau L., Bent A., Sivonen K., Wahlsten M., Wang H., Rizzi E.,
RA De Bellis G., Naismith J., Jaspars M., Liu X., Houssen W., Fewer D.P.;
RT "Corrigendum: a unique tryptophan C-prenyltransferase from the
RT kawaguchipeptin biosynthetic pathway.";
RL Angew. Chem. Int. Ed. 56:433-433(2017).
RN [3]
RP NMR SPECTROSCOPY OF 34-44; 52-62 AND 70-80, MASS SPECTROMETRY, PRENYLATION
RP AT TRP-34; TRP-41; TRP-52; TRP-59; TRP-70 AND TRP-77, AND D-AMINO ACID AT
RP LEU-35; LEU-53 AND LEU-71.
RC STRAIN=NIES-88 / KW-MA1-3;
RX DOI=10.1016/0040-4020(96)00452-8;
RA Ishida K., Matsuda H., Murakami M., Yamaguchi K.;
RT "Kawaguchipeptin A, a novel cyclic undecapeptide from cyanobacterium
RT Microcystis aeruginosa (NIES-88).";
RL Tetrahedron 52:9025-9030(1996).
RN [4]
RP NMR SPECTROSCOPY OF 34-44; 52-62 AND 70-80, ABSENCE OF PTM, AND FUNCTION.
RC STRAIN=NIES-88 / KW-MA1-3;
RX PubMed=9249979; DOI=10.1021/np970146k;
RA Ishida K., Matsuda H., Murakami M., Yamaguchi K.;
RT "Kawaguchipeptin B, an antibacterial cyclic undecapeptide from the
RT cyanobacterium Microcystis aeruginosa.";
RL J. Nat. Prod. 60:724-726(1997).
CC -!- FUNCTION: Both kawaguchipeptin A and B, which only differ by post-
CC translational modifications, have antibacterial activities, since they
CC inhibit the growth of the Gram-positive bacterium S.aureus at a
CC concentration of 1 ug/mL. {ECO:0000269|PubMed:9249979}.
CC -!- PTM: Kawaguchipeptin A contains a D-Leu and 2 prenylated Trp, whereas
CC kawaguchipeptin B only contains unmodified amino acids.
CC {ECO:0000269|PubMed:9249979, ECO:0000269|Ref.3}.
CC -!- PTM: Kawaguchipeptin A is prenylated in vivo (Ref.3). Upon expression
CC in E.coli of the whole operon, Trp residues are prenylated by C-
CC prenyltransferase KgpF (PubMed:26846478). Prenylation by KgpF is likely
CC the last enzymatic step in the biosynthetic maturation of
CC kawaguchipeptin A (PubMed:26846478). {ECO:0000269|PubMed:26846478,
CC ECO:0000269|Ref.3}.
CC -!- MASS SPECTROMETRY: Mass=1421; Method=FAB; Note=Kawaguchipeptin A (with
CC D-Leu and prenylated Trp), in vivo.; Evidence={ECO:0000269|Ref.3};
CC -!- MASS SPECTROMETRY: Mass=1421; Method=Electrospray; Note=Kawaguchipeptin
CC A (with D-Leu and prenylated Trp), when expressed in E.coli.;
CC Evidence={ECO:0000269|PubMed:26846478};
CC -!- MASS SPECTROMETRY: Mass=1285; Method=Electrospray; Note=Kawaguchipeptin
CC B (unmodified), when expressed in E.coli.;
CC Evidence={ECO:0000269|PubMed:26846478};
CC -!- MISCELLANEOUS: This peptide comes from bacteria isolated from a broom
CC on Kawaguchi lake, hence its name. {ECO:0000305|Ref.3}.
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DR EMBL; JXYX01000010; KXS89845.1; -; Genomic_DNA.
DR RefSeq; WP_061432710.1; NZ_JXYX01000010.1.
DR AlphaFoldDB; A0A139GI49; -.
DR EnsemblBacteria; KXS89845; KXS89845; OA58_19045.
DR GeneID; 66708215; -.
DR PATRIC; fig|449441.3.peg.1809; -.
DR Proteomes; UP000070196; Unassembled WGS sequence.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; D-amino acid; Lipoprotein; Prenylation.
FT PROPEP 1..33
FT /evidence="ECO:0000305|PubMed:26846478"
FT /id="PRO_0000450456"
FT PEPTIDE 34..44
FT /note="Kawaguchipeptin A"
FT /evidence="ECO:0000269|Ref.3"
FT /id="PRO_0000450457"
FT PROPEP 45..51
FT /evidence="ECO:0000305|PubMed:26846478"
FT /id="PRO_0000450458"
FT PEPTIDE 52..62
FT /note="Kawaguchipeptin A"
FT /evidence="ECO:0000269|Ref.3"
FT /id="PRO_0000450459"
FT PROPEP 63..69
FT /evidence="ECO:0000305|PubMed:26846478"
FT /id="PRO_0000450460"
FT PEPTIDE 70..80
FT /note="Kawaguchipeptin A"
FT /evidence="ECO:0000269|Ref.3"
FT /id="PRO_0000450461"
FT PROPEP 81..87
FT /evidence="ECO:0000305|PubMed:26846478"
FT /id="PRO_0000450462"
FT MOD_RES 35
FT /note="D-leucine; partial"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 53
FT /note="D-leucine; partial"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 71
FT /note="D-leucine; partial"
FT /evidence="ECO:0000269|Ref.3"
FT LIPID 34
FT /note="3'-prenyl-2',N2-cyclotryptophan; partial"
FT /evidence="ECO:0000269|Ref.3"
FT LIPID 41
FT /note="3'-prenyl-2',N2-cyclotryptophan; partial"
FT /evidence="ECO:0000269|Ref.3"
FT LIPID 52
FT /note="3'-prenyl-2',N2-cyclotryptophan; partial"
FT /evidence="ECO:0000269|Ref.3"
FT LIPID 59
FT /note="3'-prenyl-2',N2-cyclotryptophan; partial"
FT /evidence="ECO:0000269|Ref.3"
FT LIPID 70
FT /note="3'-prenyl-2',N2-cyclotryptophan; partial"
FT /evidence="ECO:0000269|Ref.3"
FT LIPID 77
FT /note="3'-prenyl-2',N2-cyclotryptophan; partial"
FT /evidence="ECO:0000269|Ref.3"
FT CROSSLNK 34..44
FT /note="Cyclopeptide (Trp-Pro)"
FT /evidence="ECO:0000269|Ref.3"
FT CROSSLNK 52..62
FT /note="Cyclopeptide (Trp-Pro)"
FT /evidence="ECO:0000269|Ref.3"
FT CROSSLNK 70..80
FT /note="Cyclopeptide (Trp-Pro)"
FT /evidence="ECO:0000269|Ref.3"
SQ SEQUENCE 87 AA; 9216 MW; 2FA2612C55A23029 CRC64;
MKNPTLLPKL TAPVERPAVT SSDLKQASSV DAAWLNGDNN WSTPFAGVNA AWLNGDNNWS
TPFAGVNAAW LNGDNNWSTP FAADGAE
