3CP2_STRSQ
ID 3CP2_STRSQ Reviewed; 21 AA.
AC P85078;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Tricyclic peptide MS-271 {ECO:0000303|PubMed:8689231, ECO:0000303|PubMed:8689232};
DE AltName: Full=Class I lasso peptide {ECO:0000305};
OS Streptomyces sp.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1931;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, D-AMINO ACID AT TRP-21,
RP DISULFIDE BONDS, AND CROSS-LINK.
RC STRAIN=M-271 {ECO:0000269|PubMed:8689231};
RX PubMed=8689231; DOI=10.1016/0968-0896(95)00175-1;
RA Yano K., Toki S., Nakanishi S., Ochiai K., Ando K., Yoshida M., Matsuda Y.,
RA Yamasaki M.;
RT "MS-271, a novel inhibitor of calmodulin-activated myosin light chain
RT kinase from Streptomyces sp. -- I. Isolation, structural determination and
RT biological properties of MS-271.";
RL Bioorg. Med. Chem. 4:115-120(1996).
RN [2] {ECO:0000305}
RP STRUCTURE BY NMR OF 1-21.
RX PubMed=8689232; DOI=10.1016/0968-0896(95)00176-x;
RA Katahira R., Yamasaki M., Matsuda Y., Yoshida M.;
RT "MS-271, a novel inhibitor of calmodulin-activated myosin light chain
RT kinase from Streptomyces sp. -- II. Solution structure of MS-271:
RT characteristic features of the 'lasso' structure.";
RL Bioorg. Med. Chem. 4:121-129(1996).
CC -!- FUNCTION: Inhibits chicken myosin light chain kinase with an IC(50) of
CC 8 M. Does not inhibit bovine cAMP-dependent protein kinase or rat
CC protein kinase C. Antibacterial activity against the Gram-positive
CC bacteria B.subtilis, E.faecium and S.aureus. No antibacterial activity
CC against the Gram-negative bacteria E.coli, K.pneumoniae, P.aeruginosa,
CC P.vulgaris, S.sonnei and S.typhosa. No antifungal activity against
CC C.albicans. {ECO:0000269|PubMed:8689231}.
CC -!- MASS SPECTROMETRY: Mass=2168.8596; Method=FAB;
CC Evidence={ECO:0000269|PubMed:8689231};
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 AlphaFoldDB; P85078; -.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; D-amino acid; Direct protein sequencing;
KW Disulfide bond; Protein kinase inhibitor; Thioether bond.
FT PEPTIDE 1..21
FT /note="Tricyclic peptide MS-271"
FT /evidence="ECO:0000269|PubMed:8689231"
FT /id="PRO_0000278145"
FT MOD_RES 21
FT /note="D-tryptophan"
FT /evidence="ECO:0000269|PubMed:8689231"
FT DISULFID 1..13
FT /evidence="ECO:0000269|PubMed:8689231"
FT DISULFID 7..19
FT /evidence="ECO:0000269|PubMed:8689231"
FT CROSSLNK 1..9
FT /note="3-cysteinyl-aspartic acid (Cys-Asp)"
FT /evidence="ECO:0000269|PubMed:8689231"
SQ SEQUENCE 21 AA; 2186 MW; EF82967204A4FF91 CRC64;
CLGVGSCNDF AGCGYAIVCF W