ID   LAT3B_LACTA             Reviewed;          82 AA.
AC   Q1ELU2;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=M-zodatoxin-Lt3b {ECO:0000305};
DE            Short=M-ZDTX-Lt3b {ECO:0000305};
DE   AltName: Full=Latarcin-3b {ECO:0000303|PubMed:16735513};
DE            Short=Ltc-3b {ECO:0000303|PubMed:16735513};
DE   Flags: Precursor;
OS   Lachesana tarabaevi (Spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Entelegynae incertae sedis; Zodariidae;
OC   Lachesana.
OX   NCBI_TaxID=379576;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 62-81, SYNTHESIS OF 62-81,
RP   AMIDATION AT ALA-81, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=16735513; DOI=10.1074/jbc.m602168200;
RA   Kozlov S.A., Vassilevski A.A., Feofanov A.V., Surovoy A.Y., Karpunin D.V.,
RA   Grishin E.V.;
RT   "Latarcins, antimicrobial and cytolytic peptides from the venom of the
RT   spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular
RT   diversity.";
RL   J. Biol. Chem. 281:20983-20992(2006).
RN   [2]
RP   SUBCELLULAR LOCATION, PQM MOTIF, MASS SPECTROMETRY, AND AMIDATION AT
RP   ALA-81.
RC   TISSUE=Venom;
RX   PubMed=27287558; DOI=10.1042/bcj20160436;
RA   Kuzmenkov A.I., Sachkova M.Y., Kovalchuk S.I., Grishin E.V.,
RA   Vassilevski A.A.;
RT   "Lachesana tarabaevi, an expert in membrane-active toxins.";
RL   Biochem. J. 473:2495-2506(2016).
CC   -!- FUNCTION: It has antimicrobial activity against Gram-positive bacteria
CC       (A.globiformis VKM Ac-1112 (MIC=0.7 uM), and B.subtilis VKM B-501
CC       (MIC=2.9 uM)), Gram-negative bacteria (E.coli DH5-alpha (MIC=23 uM),
CC       E.coli MH1 (MIC=28 uM), and P.aeruginosa PAO1 (MIC>45 uM)), and yeasts
CC       (P.pastoris GS115 (MIC=23 uM), and S.cerevisiae Y190 (MIC=23 uM)). Does
CC       not have hemolytic against rabbit erythrocytes. Causes paralysis, but
CC       is not lethal when injected into insect (M.domestica) larvae.
CC       {ECO:0000269|PubMed:16735513}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16735513,
CC       ECO:0000269|PubMed:27287558}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:16735513, ECO:0000305|PubMed:27287558}.
CC   -!- DOMAIN: The mature peptide (62-81) probably forms alpha-helices which
CC       disrupt target cell membranes. {ECO:0000303|PubMed:16735513}.
CC   -!- PTM: Cleavage of the propeptide depends on the processing quadruplet
CC       motif (XXXR, with at least one of X being E).
CC       {ECO:0000303|PubMed:27287558}.
CC   -!- MASS SPECTROMETRY: Mass=2424.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16735513};
CC   -!- MASS SPECTROMETRY: Mass=2426.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:27287558};
CC   -!- SIMILARITY: Belongs to the cationic peptide 03 (latarcin) family. 03
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AM232697; CAJ81657.1; -; mRNA.
DR   AlphaFoldDB; Q1ELU2; -.
DR   SMR; Q1ELU2; -.
DR   ArachnoServer; AS000053; M-zodatoxin-Lt3b.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR018802; Latarcin_precursor.
DR   Pfam; PF10279; Latarcin; 1.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Direct protein sequencing; Fungicide;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..61
FT                   /evidence="ECO:0000269|PubMed:16735513"
FT                   /id="PRO_0000249742"
FT   PEPTIDE         62..81
FT                   /note="M-zodatoxin-Lt3b"
FT                   /id="PRO_0000249743"
FT   MOTIF           58..61
FT                   /note="Processing quadruplet motif"
FT                   /evidence="ECO:0000303|PubMed:27287558"
FT   MOD_RES         81
FT                   /note="Alanine amide"
FT                   /evidence="ECO:0000269|PubMed:16735513,
FT                   ECO:0000269|PubMed:27287558"
SQ   SEQUENCE   82 AA;  9360 MW;  CAAE2FDB8C63755C CRC64;
     MKTYAVLLAL VVAFVCIAES TGYPVEDLED DELTELEAEA LLEDLLEDLE LEDLDYNEEA
     RSWASMAKKL KEYMEKLKQR AG