LARIA_RHOJO
ID LARIA_RHOJO Reviewed; 46 AA.
AC H7C8I3;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Lariatin {ECO:0000303|PubMed:16756302};
DE AltName: Full=Class II lasso peptide {ECO:0000303|PubMed:16756302};
DE AltName: Full=Lariat peptide {ECO:0000250|UniProtKB:P0DQM5};
DE AltName: Full=Ribosomally synthesized and post-translationally modified peptide {ECO:0000250|UniProtKB:P0DQM5};
DE Short=RiPP {ECO:0000250|UniProtKB:P0DQM5};
DE Contains:
DE RecName: Full=Lariatin-A {ECO:0000303|PubMed:16756302};
DE Contains:
DE RecName: Full=Lariatin-B {ECO:0000303|PubMed:16756302};
GN Name=larA {ECO:0000303|PubMed:22388571};
OS Rhodococcus jostii.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=132919;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K01-B0171;
RX PubMed=22388571; DOI=10.1007/s00253-012-3973-8;
RA Inokoshi J., Matsuhama M., Miyake M., Ikeda H., Tomoda H.;
RT "Molecular cloning of the gene cluster for lariatin biosynthesis of
RT Rhodococcus jostii K01-B0171.";
RL Appl. Microbiol. Biotechnol. 95:451-460(2012).
RN [2]
RP FUNCTION, AND MASS SPECTROMETRY.
RC STRAIN=K01-B0171;
RX PubMed=17617692; DOI=10.1038/ja.2007.48;
RA Iwatsuki M., Uchida R., Takakusagi Y., Matsumoto A., Jiang C.L.,
RA Takahashi Y., Arai M., Kobayashi S., Matsumoto M., Inokoshi J., Tomoda H.,
RA Omura S.;
RT "Lariatins, novel anti-mycobacterial peptides with a lasso structure,
RT produced by Rhodococcus jostii K01-B0171.";
RL J. Antibiot. 60:357-363(2007).
RN [3]
RP MUTAGENESIS OF 43-LYS--PRO-46 AND 44-PRO--PRO-46.
RX PubMed=19362475; DOI=10.1016/j.bmcl.2009.03.033;
RA Iwatsuki M., Koizumi Y., Gouda H., Hirono S., Tomoda H., Omura S.;
RT "Lys17 in the 'lasso' peptide lariatin A is responsible for anti-
RT mycobacterial activity.";
RL Bioorg. Med. Chem. Lett. 19:2888-2890(2009).
RN [4]
RP STRUCTURE BY NMR OF 27-44, PRELIMINARY PROTEIN SEQUENCE OF 27-44, AND
RP CROSS-LINK.
RC STRAIN=K01-B0171;
RX PubMed=16756302; DOI=10.1021/ja056780z;
RA Iwatsuki M., Tomoda H., Uchida R., Gouda H., Hirono S., Omura S.;
RT "Lariatins, antimycobacterial peptides produced by Rhodococcus sp. K01-
RT B0171, have a lasso structure.";
RL J. Am. Chem. Soc. 128:7486-7491(2006).
CC -!- FUNCTION: [Lariatin-A]: Peptide antibiotic with selective activity
CC against Mycobacterium species (M.smegmatis, MIC=3.13 ug/ml and
CC M.tuberculosis, MIC=0.39 ug/ml). it is plausible that the target of
CC lariatins lies within the cell wall in mycobacteria.
CC {ECO:0000269|PubMed:17617692}.
CC -!- FUNCTION: [Lariatin-B]: Peptide antibiotic with selective activity
CC against Mycobacterium species (M.smegmatis, MIC=6.25 ug/ml).
CC {ECO:0000269|PubMed:17617692}.
CC -!- DOMAIN: Is composed of a ring composed by 8 residues, and a tail of 10
CC or 12 residues (Probable). The peptide is threaded when the C-terminal
CC tail is inserted throught the isopeptide-bonded ring (Probable).
CC {ECO:0000305|PubMed:16756302}.
CC -!- PTM: The linear precursor LarA is probably cleaved by the putative
CC peptidase LarD, generating linear 18-residue Lariatin-A or 20-residue
CC Lariatin-B. These linear peptides are probably cross-linked by LarB.
CC Finally, lariatins A and B may be exported by ABC transporter LarE.
CC {ECO:0000305|PubMed:22388571}.
CC -!- MASS SPECTROMETRY: [Lariatin-A]: Mass=2051; Method=FAB;
CC Evidence={ECO:0000269|PubMed:17617692};
CC -!- MASS SPECTROMETRY: [Lariatin-B]: Mass=2205; Method=FAB;
CC Evidence={ECO:0000269|PubMed:17617692};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB593691; BAL72546.1; -; Genomic_DNA.
DR AlphaFoldDB; H7C8I3; -.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW Isopeptide bond.
FT PROPEP 1..26
FT /evidence="ECO:0000305|PubMed:22388571"
FT /id="PRO_0000450655"
FT PEPTIDE 27..46
FT /note="Lariatin-B"
FT /evidence="ECO:0000269|PubMed:17617692"
FT /id="PRO_0000450656"
FT PEPTIDE 27..44
FT /note="Lariatin-A"
FT /evidence="ECO:0000269|PubMed:16756302,
FT ECO:0000269|PubMed:17617692"
FT /id="PRO_0000450657"
FT SITE 43..44
FT /note="Important in resistance to hydrolysis"
FT /evidence="ECO:0000305|PubMed:19362475"
FT CROSSLNK 27..34
FT /note="Isoglutamyl glycine isopeptide (Gly-Glu)"
FT /evidence="ECO:0000269|PubMed:16756302"
FT MUTAGEN 43..46
FT /note="Missing: Loss of antibacterial activity."
FT /evidence="ECO:0000269|PubMed:19362475"
FT MUTAGEN 44..46
FT /note="Missing: No change in antibacterial activity."
FT /evidence="ECO:0000269|PubMed:19362475"
SQ SEQUENCE 46 AA; 5075 MW; AEA820CF5089888B CRC64;
MTSQPSKKTY NAPSLVQRGK FARTTAGSQL VYREWVGHSN VIKPGP
