ID   NDB27_VAEME             Reviewed;          82 AA.
AC   F1AWB0;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Vejovine {ECO:0000303|PubMed:20969885};
DE   AltName: Full=Non-disulfide-bridged peptide 2.7 {ECO:0000303|PubMed:24184590};
DE            Short=NDBP-2.7 {ECO:0000303|PubMed:24184590};
DE   Flags: Precursor;
OS   Vaejovis mexicanus (Mexican scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Chactoidea; Vaejovidae; Vaejovis.
OX   NCBI_TaxID=993612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-42, SYNTHESIS OF 23-69,
RP   SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND CIRCULAR DICHROISM.
RC   TISSUE=Venom gland;
RX   PubMed=20969885; DOI=10.1016/j.toxicon.2010.10.008;
RA   Hernandez-Aponte C.A., Silva-Sanchez J., Quintero-Hernandez V.,
RA   Rodriguez-Romero A., Balderas C., Possani L.D., Gurrola G.B.;
RT   "Vejovine, a new antibiotic from the scorpion venom of Vaejovis
RT   mexicanus.";
RL   Toxicon 57:84-92(2011).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=24184590; DOI=10.1016/j.peptides.2013.10.021;
RA   Almaaytah A., Albalas Q.;
RT   "Scorpion venom peptides with no disulfide bridges: a review.";
RL   Peptides 51:35-45(2014).
CC   -!- FUNCTION: Displays significant potent antimicrobial activity against
CC       clinical isolates of Gram-negative multidrug resistant strains of
CC       E.coli, P.aeruginosa and A.baumanii with MIC values as low as 4.4 uM.
CC       Additionally, it displays low cytolytic and hemolytic activity against
CC       human erythrocytes reaching 50% hemolysis at 100 uM.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20969885}. Target
CC       cell membrane {ECO:0000305|PubMed:20969885}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=4873; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:20969885};
CC   -!- MISCELLANEOUS: Adopts the characteristic alpha-helical amphipathic
CC       structure in TFE solution, but an unexpected random coil conformation
CC       in water. {ECO:0000269|PubMed:20969885}.
CC   -!- MISCELLANEOUS: Is an unstable peptide when the venom is stored after
CC       milking. This produces a shorter peptide, named Vm36, which lacks the 8
CC       amino acid residues at the N-terminus. {ECO:0000269|PubMed:20969885}.
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Long chain multifunctional peptide (group 2) family.
CC       {ECO:0000305}.
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DR   EMBL; HM102352; ADZ24463.1; -; mRNA.
DR   AlphaFoldDB; F1AWB0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR012526; Antimicrobial_7.
DR   Pfam; PF08102; Antimicrobial_7; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis;
KW   Membrane; Secreted; Signal; Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:20969885"
FT   CHAIN           23..69
FT                   /note="Vejovine"
FT                   /id="PRO_5000725160"
FT   PROPEP          70..82
FT                   /evidence="ECO:0000269|PubMed:20969885"
FT                   /id="PRO_0000432336"
SQ   SEQUENCE   82 AA;  8869 MW;  2393887A21126D22 CRC64;
     MNAKTLFVVF LIGMLVTEQV EAGIWSSIKN LASKAWNSDI GQSLRNKAAG AINKFVADKI
     GVTPSQAASM TLDEIVDAMY YD