ID   AMP1_TITDI              Reviewed;          61 AA.
AC   P0CF39;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Bactridin-1 {ECO:0000303|PubMed:19540868};
DE            Short=Bact1 {ECO:0000303|PubMed:19540868};
DE            Short=Bactridine 1 {ECO:0000303|PubMed:19540868};
DE   AltName: Full=P-Arthr-Antm-beta* NaTx2.6;
OS   Tityus discrepans (Venezuelan scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=57059;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=19540868; DOI=10.1016/j.toxicon.2009.06.014;
RA   Diaz P., D'Suze G., Salazar V., Sevcik C., Shannon J.D., Sherman N.E.,
RA   Fox J.W.;
RT   "Antibacterial activity of six novel peptides from Tityus discrepans
RT   scorpion venom. A fluorescent probe study of microbial membrane Na+
RT   permeability changes.";
RL   Toxicon 54:802-817(2009).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=22355312; DOI=10.1371/journal.pone.0030478;
RA   Guerrero-Vargas J.A., Mourao C.B., Quintero-Hernandez V., Possani L.D.,
RA   Schwartz E.F.;
RT   "Identification and phylogenetic analysis of Tityus pachyurus and Tityus
RT   obscurus novel putative Na+-channel scorpion toxins.";
RL   PLoS ONE 7:E30478-E30478(2012).
CC   -!- FUNCTION: Shows antibacterial activity against both Gram-positive
CC       bacteria (B.subtilis, M.luteus, E.faecalis) and Gram-negative bacteria
CC       (P.aeruginosa, Y.enterocolitica, A.calcoaceticus) (PubMed:19540868).
CC       Modifies membrane sodium permeability on Y.enterocolitica
CC       (PubMed:19540868). Is toxic to cockroaches and crabs, but is not toxic
CC       to mice. Does not induce haemolysis in human erythrocytes
CC       (PubMed:19540868). Acts by inhibiting the sodium (Nav) currents (By
CC       similarity). {ECO:0000250|UniProtKB:P0C1X7,
CC       ECO:0000269|PubMed:19540868}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19540868}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19540868}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=6916; Method=Electrospray; Note=Monoisotopic.;
CC       Evidence={ECO:0000269|PubMed:19540868};
CC   -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0CF39; -.
DR   SMR; P0CF39; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR   InterPro; IPR003614; Scorpion_toxin-like.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR018218; Scorpion_toxinL.
DR   InterPro; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
DR   PRINTS; PR00285; SCORPNTOXIN.
DR   SMART; SM00505; Knot1; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51863; LCN_CSAB; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..61
FT                   /note="Bactridin-1"
FT                   /evidence="ECO:0000269|PubMed:19540868"
FT                   /id="PRO_0000393444"
FT   DOMAIN          1..61
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        11..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        15..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        23..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        27..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   61 AA;  6928 MW;  673E48C4E8387FB7 CRC64;
     KDGYIIEHRG CKYSCFFGTN SWCNTECTLK KGSSGYCAWP ACWCYGLPDN VKIFDSNNLK
     C