B11A_TETBN
ID B11A_TETBN Reviewed; 79 AA.
AC W8GNV3;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=M-myrmicitoxin(01)-Tb1a {ECO:0000305};
DE Short=M-MYRTX(01)-Tb1a {ECO:0000305};
DE AltName: Full=Ant peptide P16 {ECO:0000303|PubMed:22960382};
DE AltName: Full=Bicarinalin {ECO:0000303|PubMed:22960382};
DE AltName: Full=Bicarinaline {ECO:0000312|EMBL:AHK22716.1};
DE AltName: Full=M-myrmicitoxin-Tb1a {ECO:0000303|PubMed:26805882};
DE Short=M-MYRTX-Tb1a {ECO:0000303|PubMed:26805882};
DE Flags: Precursor;
OS Tetramorium bicarinatum (Tramp ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Tetramorium.
OX NCBI_TaxID=219812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SYNTHESIS OF 57-66, AND 3D-STRUCTURE
RP MODELING.
RC TISSUE=Venom gland;
RX PubMed=27058430; DOI=10.1016/j.peptides.2016.04.001;
RA Tene N., Bonnafe E., Berger F., Rifflet A., Guilhaudis L.,
RA Segalas-Milazzo I., Pipy B., Coste A., Leprince J., Treilhou M.;
RT "Biochemical and biophysical combined study of bicarinalin, an ant venom
RT antimicrobial peptide.";
RL Peptides 79:103-113(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=23584016; DOI=10.1016/j.toxicon.2013.03.010;
RA Bouzid W., Klopp C., Verdenaud M., Ducancel F., Vetillard A.;
RT "Profiling the venom gland transcriptome of Tetramorium bicarinatum
RT (Hymenoptera: Formicidae): the first transcriptome analysis of an ant
RT species.";
RL Toxicon 70:70-81(2013).
RN [3]
RP PROTEIN SEQUENCE OF 57-76, SYNTHESIS OF 57-76, FUNCTION, MASS SPECTROMETRY,
RP AMIDATION AT VAL-76, SUBCELLULAR LOCATION, AND CIRCULAR DICHROISM.
RC TISSUE=Venom;
RX PubMed=22960382; DOI=10.1016/j.peptides.2012.08.018;
RA Rifflet A., Gavalda S., Tene N., Orivel J., Leprince J., Guilhaudis L.,
RA Genin E., Vetillard A., Treilhou M.;
RT "Identification and characterization of a novel antimicrobial peptide from
RT the venom of the ant Tetramorium bicarinatum.";
RL Peptides 38:363-370(2012).
RN [4]
RP FUNCTION, AND SYNTHESIS OF 57-76.
RX PubMed=29286296; DOI=10.3390/toxins10010021;
RA Guzman J., Tene N., Touchard A., Castillo D., Belkhelfa H.,
RA Haddioui-Hbabi L., Treilhou M., Sauvain M.;
RT "Anti-helicobacter pylori properties of the ant-venom peptide
RT bicarinalin.";
RL Toxins 10:1-10(2017).
RN [5]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=26805882; DOI=10.3390/toxins8010030;
RA Touchard A., Aili S.R., Fox E.G., Escoubas P., Orivel J., Nicholson G.M.,
RA Dejean A.;
RT "The biochemical toxin arsenal from ant venoms.";
RL Toxins 8:1-28(2016).
CC -!- FUNCTION: Antimicrobial peptide that shows antimicrobial activities
CC against all microorganisms tested with minimal inhibitory
CC concentrations (MICs) values ranging from 0.45 to 97.5 umol/L
CC (PubMed:27058430). This peptide kills the microorganisms by
CC permeabilizating the membranes (PubMed:27058430). It shows a very weak
CC hemolytic activity (HC(50)=325 umol/L) and weak cytotoxicity against
CC human lymphocytes (LC(50)=67.8 umol/L) (PubMed:27058430,
CC PubMed:22960382). Gram-negative bacteria tested are E.coli (MIC=24.4
CC umol/L), C.sakazakii (MIC=5.8 umol/L), P.aeruginosa (MIC=8.7-12.2
CC umol/L), S.enterica (MIC=5.4 umol/L), and H.pylori (MIC=0.99-3.9
CC umol/L) (PubMed:22960382, PubMed:29286296). Gram-positive bacteria
CC tested are E.hirae (MIC=12.2 umol/L), S.aureus (MIC=3.0-6.4 umol/L),
CC methicillin-resistant S.aureus (MRSA) (MIC=8.7 umol/L), S.xylosus
CC (MIC=0.45-1.3 umol/L), and B.subtilis (MIC=24.4 umol/L)
CC (PubMed:27058430, PubMed:22960382). Fungi tested are A.niger (MIC=0.75
CC umol/L), C.albicans (MIC=17.3 umol/L), G.candidum (MIC=97.5 umol/L),
CC and S.cerevisiae (MIC=6.1 umol/L) (PubMed:27058430). Finally the
CC parasite tested is L.infantum (MIC=1.5 umol/L) (PubMed:27058430).
CC {ECO:0000269|PubMed:22960382, ECO:0000269|PubMed:27058430}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22960382}. Target
CC cell membrane {ECO:0000305|PubMed:27058430}. Note=Forms a helical
CC membrane channel in the prey. {ECO:0000305|PubMed:22960382}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:22960382}.
CC -!- PTM: The C-terminal amidation is important for antimicrobial activity,
CC since a non-amidated synthetic peptide shows a reduced antimicrobial
CC activity (2-20-fold depending on the strain tested). The amidation may
CC play a positive role in the peptide conformation, since amidated
CC peptide shows an increase of about 5% of helical content.
CC {ECO:0000269|PubMed:22960382}.
CC -!- MASS SPECTROMETRY: Mass=2213.06; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:22960382};
CC -!- MISCELLANEOUS: This is the most abundant peptide from the venom of
CC T.bicarinatum. {ECO:0000305|PubMed:27058430}.
CC -!- SIMILARITY: Belongs to the formicidae venom precursor-01 superfamily.
CC {ECO:0000305}.
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DR EMBL; KF929552; AHK22716.1; -; mRNA.
DR EMBL; JZ168535; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; W8GNV3; -.
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.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Direct protein sequencing; Membrane;
KW Secreted; Signal; Target cell membrane; Target membrane.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..56
FT /evidence="ECO:0000305|PubMed:22960382"
FT /id="PRO_0000447049"
FT PEPTIDE 57..76
FT /note="M-myrmicitoxin(01)-Tb1a"
FT /evidence="ECO:0000269|PubMed:22960382"
FT /id="PRO_5004909437"
FT MOD_RES 76
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:22960382"
SQ SEQUENCE 79 AA; 8172 MW; 37319082CCED2E49 CRC64;
MKLSFLSLVL AIILVMALMY TPHAEAKAWA DADADATAAA DADADAVADA LADAVAKIKI
PWGKVKDFLV GGMKAVGKK
