ASTX3_ASTEC
ID ASTX3_ASTEC Reviewed; 49 AA.
AC E8RUP8;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Astexin-3 {ECO:0000303|PubMed:23862624, ECO:0000303|PubMed:26534965, ECO:0000303|PubMed:27998080};
DE AltName: Full=Class II lasso peptide {ECO:0000303|PubMed:23862624, ECO:0000303|PubMed:26534965};
DE AltName: Full=Ribosomally synthesized and post-translationally modified peptide {ECO:0000303|PubMed:23862624};
DE Short=RiPP {ECO:0000303|PubMed:23862624};
DE Flags: Precursor;
GN Name=AtxA3 {ECO:0000303|PubMed:23862624};
GN OrderedLocusNames=Astex_2447 {ECO:0000312|EMBL:ADU14098.1};
OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS NCIMB 9791 / VKM B-1370 / CB 48).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=573065;
RN [1] {ECO:0000312|Proteomes:UP000001492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 / CB
RC 48;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Brun Y.V., Woyke T.;
RT "Complete sequence of chromosome 2 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:2M8F}
RP STRUCTURE BY NMR OF 26-49, BIOPHYSICOCHEMICAL PROPERTIES, AND EXPRESSION IN
RP E.COLI.
RX PubMed=23862624; DOI=10.1021/ja4054256;
RA Maksimov M.O., Link A.J.;
RT "Discovery and characterization of an isopeptidase that linearizes lasso
RT peptides.";
RL J. Am. Chem. Soc. 135:12038-12047(2013).
RN [3] {ECO:0007744|PDB:2N6V}
RP STRUCTURE BY NMR OF 26-49, MUTAGENESIS OF SER-35; VAL-36; SER-37 AND
RP GLN-39, AND EXPRESSION IN E.COLI.
RX PubMed=26534965; DOI=10.1074/jbc.m115.694083;
RA Maksimov M.O., Koos J.D., Zong C., Lisko B., Link A.J.;
RT "Elucidating the specificity determinants of the AtxE2 lasso peptide
RT isopeptidase.";
RL J. Biol. Chem. 290:30806-30812(2015).
RN [4] {ECO:0007744|PDB:5TXE}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 26-49 IN COMPLEX WITH ATXE2, AND
RP EXPRESSION IN E.COLI.
RX PubMed=27998080; DOI=10.1021/jacs.6b10389;
RA Chekan J.R., Koos J.D., Zong C., Maksimov M.O., Link A.J., Nair S.K.;
RT "Structure of the lasso peptide isopeptidase identifies a topology for
RT processing threaded substrates.";
RL J. Am. Chem. Soc. 138:16452-16458(2016).
CC -!- FUNCTION: Shows weak antimicrobial activity against its phylogenetic
CC relative Caulobacter crescentus. Does not show activity against other
CC bacteria tested (E.coli, Vibrio sp, Burkhoderia thailandensis, and
CC Salmonella newport). {ECO:0000250|UniProtKB:E8RMD3}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Highly thermostable. {ECO:0000269|PubMed:23862624};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23862624}. Secreted
CC {ECO:0000305|PubMed:23862624}. Note=Intracellular, when expressed in
CC E.coli. The gene cluster lacks the ABC transporter usually responsible
CC for export of the mature peptide (Probable). May be secreted in vivo
CC (Probable). {ECO:0000305|PubMed:23862624, ECO:0000305|PubMed:26534965,
CC ECO:0000305|PubMed:27998080}.
CC -!- DOMAIN: Is composed of a ring composed by 9 residues, a 5 residue-loop
CC (SVSGQ) and a C-terminal tail (PubMed:26534965). The peptide is
CC threaded when the C-terminal tail is inserted throught the isopeptide-
CC bonded ring. The loop region serves as a recognition element for the
CC isopeptidase AtxE2 (Probable) (PubMed:27998080).
CC {ECO:0000269|PubMed:26534965, ECO:0000269|PubMed:27998080,
CC ECO:0000305|PubMed:23862624, ECO:0000305|PubMed:26534965}.
CC -!- PTM: This lasso peptide is hydrolyzed to a linear form by the
CC isopeptidase AtxE2, in vitro. The isopeptidase AtxE2 only recognizes
CC the threaded form (but not the unthreaded form).
CC {ECO:0000269|PubMed:23862624}.
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DR EMBL; CP002396; ADU14098.1; -; Genomic_DNA.
DR PDB; 2M8F; NMR; -; A=26-49.
DR PDB; 2N6V; NMR; -; A=26-49.
DR PDB; 5TXE; X-ray; 2.20 A; C/D=26-49.
DR PDBsum; 2M8F; -.
DR PDBsum; 2N6V; -.
DR PDBsum; 5TXE; -.
DR AlphaFoldDB; E8RUP8; -.
DR BMRB; E8RUP8; -.
DR SMR; E8RUP8; -.
DR STRING; 573065.Astex_2447; -.
DR EnsemblBacteria; ADU14098; ADU14098; Astex_2447.
DR KEGG; aex:Astex_2447; -.
DR HOGENOM; CLU_3131825_0_0_5; -.
DR Proteomes; UP000001492; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Cytoplasm; Isopeptide bond;
KW Reference proteome; Secreted.
FT PROPEP 1..25
FT /evidence="ECO:0000305|PubMed:23862624,
FT ECO:0000305|PubMed:26534965"
FT /id="PRO_0000450592"
FT PEPTIDE 26..49
FT /note="Astexin-3"
FT /evidence="ECO:0000305|PubMed:23862624,
FT ECO:0000305|PubMed:26534965"
FT /id="PRO_0000450593"
FT CROSSLNK 26..34
FT /note="Isoaspartyl glycine isopeptide (Gly-Asp)"
FT /evidence="ECO:0000269|PubMed:23862624,
FT ECO:0000269|PubMed:26534965"
FT MUTAGEN 35
FT /note="S->A: Decrease in cleavage by the isopeptidase
FT AtxE2."
FT /evidence="ECO:0000269|PubMed:26534965"
FT MUTAGEN 36
FT /note="V->A: Decrease in cleavage by the isopeptidase
FT AtxE2."
FT /evidence="ECO:0000269|PubMed:26534965"
FT MUTAGEN 37
FT /note="S->A: Decrease in cleavage by the isopeptidase
FT AtxE2."
FT /evidence="ECO:0000269|PubMed:26534965"
FT MUTAGEN 39
FT /note="Q->A: Decrease in cleavage by the isopeptidase
FT AtxE2."
FT /evidence="ECO:0000269|PubMed:26534965"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:5TXE"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:5TXE"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2M8F"
SQ SEQUENCE 49 AA; 5312 MW; 19FC18888E91C908 CRC64;
MRTYNRSLPA RAGLTDLGKV TTHTKGPTPM VGLDSVSGQY WDQHAPLAD
