ID   LL1_LASLA               Reviewed;          15 AA.
AC   C0HK42;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   02-JUN-2021, entry version 5.
DE   RecName: Full=Lasioglossin-1 {ECO:0000303|PubMed:19591185};
DE            Short=LL-I {ECO:0000303|PubMed:19591185};
OS   Lasioglossum laticeps (Bee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Halictidae; Halictinae; Halictini; Lasioglossum; Evylaeus.
OX   NCBI_TaxID=88510 {ECO:0000303|PubMed:19591185};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP   IDENTIFICATION BY MASS SPECTROMETRY, STRUCTURE BY NMR, MUTAGENESIS OF
RP   1-VAL-ASN-2 AND GLY-8, AND AMIDATION AT LYS-15.
RC   TISSUE=Venom {ECO:0000303|PubMed:19591185};
RX   PubMed=19591185; DOI=10.1002/cbic.200900133;
RA   Cerovsky V., Budesinsky M., Hovorka O., Cvacka J., Voburka Z.,
RA   Slaninova J., Borovickova L., Fucik V., Bednarova L., Votruba I.,
RA   Straka J.;
RT   "Lasioglossins: three novel antimicrobial peptides from the venom of the
RT   eusocial bee Lasioglossum laticeps (Hymenoptera: Halictidae).";
RL   ChemBioChem 10:2089-2099(2009).
CC   -!- FUNCTION: Antimicrobial peptide which assumes an amphiphilic alpha-
CC       helix conformation upon contact with membranes (PubMed:19591185).
CC       Insertion into membranes involves Trp-3 (By similarity). Penetrates
CC       into cells once membrane has been permeated (By similarity). Active
CC       against Gram-negative bacteria E.coli (MIC=1.7 uM), P.aeruginosa
CC       (MIC=15.8 uM) and Gram-positive bacteria S.aureus (MIC=14.3 uM) and
CC       B.subtilis (MIC=0.8 uM). Has cytotoxic but no hemolytic activity
CC       (PubMed:19591185). Binds DNA in vitro (By similarity).
CC       {ECO:0000250|UniProtKB:C0HK43, ECO:0000250|UniProtKB:C0HK44,
CC       ECO:0000269|PubMed:19591185}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19591185}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19591185}.
CC   -!- PTM: The C-terminal amidation is required for full activity.
CC       {ECO:0000250|UniProtKB:C0HK44}.
CC   -!- MASS SPECTROMETRY: Mass=1722.1; Mass_error=0.1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19591185};
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; 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;
KW   DNA-binding; Secreted.
FT   PEPTIDE         1..15
FT                   /note="Lasioglossin-1"
FT                   /evidence="ECO:0000269|PubMed:19591185"
FT                   /id="PRO_0000437650"
FT   MOD_RES         15
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:19591185"
FT   MUTAGEN         1..2
FT                   /note="VN->NV: Reduced antimicrobial activity."
FT                   /evidence="ECO:0000269|PubMed:19591185"
FT   MUTAGEN         8
FT                   /note="G->A: Slightly increased activity against all
FT                   bacteria except P.aeruginosa."
FT                   /evidence="ECO:0000269|PubMed:19591185"
FT   MUTAGEN         8
FT                   /note="G->K: Slightly increased activity against B.subtilis
FT                   and E.coli, reduced activity aginst S.aureus and
FT                   P.aeruginosa."
FT                   /evidence="ECO:0000269|PubMed:19591185"
FT   MUTAGEN         8
FT                   /note="G->P: Reduced antimicrobial activity."
FT                   /evidence="ECO:0000269|PubMed:19591185"
SQ   SEQUENCE   15 AA;  1724 MW;  2603143CD4C7E7B6 CRC64;
     VNWKKVLGKI IKVAK