ASTX1_ASTEC
ID ASTX1_ASTEC Reviewed; 51 AA.
AC E8RMD3;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Astexin-1 {ECO:0000303|PubMed:22949633, ECO:0000303|PubMed:23601645, ECO:0000303|PubMed:23862624};
DE AltName: Full=Class II lasso peptide {ECO:0000303|PubMed:22949633, ECO:0000303|PubMed:23601645, ECO:0000303|PubMed:23862624};
DE AltName: Full=Ribosomally synthesized and post-translationally modified peptide {ECO:0000303|PubMed:22949633, ECO:0000303|PubMed:23862624};
DE Short=RiPP {ECO:0000303|PubMed:23862624};
DE Flags: Precursor;
GN Name=AtxA1 {ECO:0000303|PubMed:22949633, ECO:0000303|PubMed:23862624};
GN OrderedLocusNames=Astex_2228 {ECO:0000312|EMBL:ADU13884.1};
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 1 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP EXPRESSION IN 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:0000305, ECO:0007744|PDB:2LTI}
RP STRUCTURE BY NMR OF 29-51, FUNCTION, CROSS-LINK, EXPRESSION IN E.COLI, AND
RP MASS SPECTROMETRY.
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 / CB
RC 48;
RX PubMed=22949633; DOI=10.1073/pnas.1208978109;
RA Maksimov M.O., Pelczer I., Link A.J.;
RT "Precursor-centric genome-mining approach for lasso peptide discovery.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:15223-15228(2012).
RN [4] {ECO:0000305, ECO:0007744|PDB:2M37}
RP STRUCTURE BY NMR OF 29-47, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP CROSS-LINK, EXPRESSION IN E.COLI, AND MUTAGENESIS OF TYR-42; PHE-43 AND
RP ARG-47.
RX PubMed=23601645; DOI=10.1016/j.chembiol.2013.03.013;
RA Zimmermann M., Hegemann J.D., Xie X., Marahiel M.A.;
RT "The astexin-1 lasso peptides: biosynthesis, stability, and structural
RT studies.";
RL Chem. Biol. 20:558-569(2013).
RN [5] {ECO:0007744|PDB:2N68}
RP STRUCTURE BY NMR OF 29-51.
RX PubMed=26492187; DOI=10.1021/acschembio.5b00745;
RA Zong C., Maksimov M.O., Link A.J.;
RT "Construction of lasso peptide fusion proteins.";
RL ACS Chem. Biol. 11:61-68(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:0000269|PubMed:22949633}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Irreversibly unfolds upon heat treatment (PubMed:23601645). Between
CC 50 and 65 degrees Celsius, the protein shows an intermediate fold
CC (PubMed:23601645). At more than 65 degrees Celsius, the protein is
CC completely unfolded (PubMed:23601645). {ECO:0000269|PubMed:23601645};
CC -!- DOMAIN: Is composed of a ring composed by 9 residues, a loop and a C-
CC terminal tail (PubMed:23601645). The peptide is threaded when the C-
CC terminal tail is inserted throught the isopeptide-bonded ring
CC (Probable). {ECO:0000269|PubMed:23601645, ECO:0000305}.
CC -!- PTM: This lasso peptide is probably hydrolyzed to a linear form by the
CC isopeptidase AtxE1, in vivo. {ECO:0000269|PubMed:23862624}.
CC -!- MASS SPECTROMETRY: Mass=2563.96; Method=MALDI; Note=when expressed in
CC E.coli.; Evidence={ECO:0000269|PubMed:22949633};
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DR EMBL; CP002395; ADU13884.1; -; Genomic_DNA.
DR PDB; 2LTI; NMR; -; A=29-51.
DR PDB; 2M37; NMR; -; A=29-47.
DR PDB; 2N68; NMR; -; A=29-51.
DR PDBsum; 2LTI; -.
DR PDBsum; 2M37; -.
DR PDBsum; 2N68; -.
DR AlphaFoldDB; E8RMD3; -.
DR BMRB; E8RMD3; -.
DR SMR; E8RMD3; -.
DR STRING; 573065.Astex_2228; -.
DR EnsemblBacteria; ADU13884; ADU13884; Astex_2228.
DR KEGG; aex:Astex_2228; -.
DR HOGENOM; CLU_3095092_0_0_5; -.
DR Proteomes; UP000001492; Chromosome 1.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Isopeptide bond;
KW Reference proteome.
FT PROPEP 1..28
FT /evidence="ECO:0000305"
FT /id="PRO_0000450588"
FT PEPTIDE 29..51
FT /note="Astexin-1"
FT /evidence="ECO:0000305|PubMed:22949633,
FT ECO:0000305|PubMed:23601645"
FT /id="PRO_0000450589"
FT SITE 42
FT /note="Important for stabilization of the lasso structure"
FT /evidence="ECO:0000305|PubMed:23601645"
FT SITE 43
FT /note="Important for stabilization of the lasso structure"
FT /evidence="ECO:0000305|PubMed:23601645"
FT CROSSLNK 29..37
FT /note="Isoaspartyl glycine isopeptide (Gly-Asp)"
FT /evidence="ECO:0000269|PubMed:22949633,
FT ECO:0000269|PubMed:23601645"
FT MUTAGEN 42
FT /note="Y->A: Almost complete loss of Astexin-1 production.
FT Is unfolded."
FT /evidence="ECO:0000269|PubMed:23601645"
FT MUTAGEN 42
FT /note="Y->W: No change in thermostability."
FT /evidence="ECO:0000269|PubMed:23601645"
FT MUTAGEN 43
FT /note="F->A: Loss of Astexin-1 production. No change in
FT thermostability."
FT /evidence="ECO:0000269|PubMed:23601645"
FT MUTAGEN 43
FT /note="F->W: Gain in thermostability."
FT /evidence="ECO:0000269|PubMed:23601645"
FT MUTAGEN 47
FT /note="R->W: No change in thermostability."
FT /evidence="ECO:0000269|PubMed:23601645"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:2LTI"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2M37"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2LTI"
SQ SEQUENCE 51 AA; 5514 MW; 111DA6B651CCCA3B CRC64;
MHTPIISETV QPKTAGLIVL GKASAETRGL SQGVEPDIGQ TYFEESRINQ D
