ID   NDB32_CENSU             Reviewed;          25 AA.
AC   P0DL41;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Css54 {ECO:0000303|PubMed:23093034};
DE   AltName: Full=Non-disulfide-bridged peptide 3.2 {ECO:0000303|PubMed:24184590};
DE            Short=NDBP-3.2 {ECO:0000303|PubMed:24184590};
OS   Centruroides suffusus (Durango bark scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=6880;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SYNTHESIS, SUBCELLULAR LOCATION, CIRCULAR
RP   DICHROISM, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=23093034; DOI=10.1038/ja.2012.87;
RA   Garcia F., Villegas E., Espino-Solis G.P., Rodriguez A.,
RA   Paniagua-Solis J.F., Sandoval-Lopez G., Possani L.D., Corzo G.;
RT   "Antimicrobial peptides from arachnid venoms and their microbicidal
RT   activity in the presence of commercial antibiotics.";
RL   J. Antibiot. 66:3-10(2013).
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: Amphipathic peptide that shows antibacterial activity against
CC       E.coli (MIC=12.5 ug/ml) and S.aureus (MIC=12.5 ug/ml). Increases
CC       efficacy of antibiotics (ethambutol, pyrazinamide, isoniazid,
CC       rifampicin) when tested against S.aureus, probably by facilitating
CC       their incorporation into the bacteria. Has hemolytic activity against
CC       human erythrocytes (25 uM provokes 83% of hemolysis).
CC       {ECO:0000269|PubMed:23093034}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23093034}. Target
CC       cell membrane {ECO:0000305|PubMed:23093034}. Note=Forms a helical
CC       membrane channel in the prey. {ECO:0000305|PubMed:23093034}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=2870.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:23093034};
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Medium-length antimicrobial peptide (group 3) family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DL41; -.
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; IPR012523; Antimicrobial_4.
DR   Pfam; PF08024; Antimicrobial_4; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis;
KW   Membrane; Secreted; Target cell membrane; Target membrane.
FT   PEPTIDE         1..25
FT                   /note="Css54"
FT                   /id="PRO_0000432338"
SQ   SEQUENCE   25 AA;  2870 MW;  AEFE8E87DDB8D6FC CRC64;
     FFGSLLSLGS KLLPSVFKLF QRKKE