MRSA_BACSY
ID MRSA_BACSY Reviewed; 68 AA.
AC P43683;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Lantibiotic mersacidin;
DE Flags: Precursor;
GN Name=mrsA;
OS Bacillus sp. (strain HIL-Y85/54728).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=69002;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7737474; DOI=10.1111/j.1574-6968.1995.tb07460.x;
RA Bierbaum G., Broetz H., Koller K.-P., Sahl H.-G.;
RT "Cloning, sequencing and production of the lantibiotic mersacidin.";
RL FEMS Microbiol. Lett. 127:121-126(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10831439; DOI=10.1128/aem.66.6.2565-2571.2000;
RA Altena K., Guder A., Cramer C., Bierbaum G.;
RT "Biosynthesis of the lantibiotic mersacidin: organization of a type B
RT lantibiotic gene cluster.";
RL Appl. Environ. Microbiol. 66:2565-2571(2000).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9210483; DOI=10.1111/j.1432-1033.1997.t01-1-00193.x;
RA Broetz H., Bierbaum G., Reynolds P.E., Sahl H.-G.;
RT "The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the
RT level of transglycosylation.";
RL Eur. J. Biochem. 246:193-199(1997).
RN [4]
RP STRUCTURE BY NMR, DEHYDRATION AT SER-64, AND LANTHIONINE CROSS-LINKS.
RX PubMed=9119018; DOI=10.1111/j.1432-1033.1997.00501.x;
RA Prasch T., Naumann T., Markert R.L.M., Sattler M., Schubert W., Schaal S.,
RA Bauch M., Kogler H., Gresinger C.;
RT "Constitution and solution conformation of the antibiotic mersacidin
RT determined by NMR and molecular dynamics.";
RL Eur. J. Biochem. 244:501-512(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS).
RX PubMed=10818347; DOI=10.1107/s0907444900003711;
RA Schneider T.R., Karcher J., Pohl E., Lubini P., Sheldrick G.M.;
RT "Ab initio structure determination of the lantibiotic mersacidin.";
RL Acta Crystallogr. D 56:705-713(2000).
CC -!- FUNCTION: Kills a number of Gram-positive bacteria. Acts at the level
CC of cell wall biosynthesis by interfering with bacterial peptidoglycan
CC biosynthesis. Specifically inhibits the conversion of the lipid II
CC intermediate into polymeric nascent glycan strands by
CC transglycosylation. May interact with the peptidoglycan precursor
CC rather than with the enzyme.
CC -!- PTM: Maturation of lantibiotics involves the enzymatic conversion of
CC Thr, and Ser into dehydrated AA and the formation of thioether bonds
CC with cysteine. The carboxy-terminal beta-methyllanthionine undergoes
CC decarboxylation. This is followed by membrane translocation and
CC cleavage of the modified precursor.
CC -!- SIMILARITY: Belongs to the type B lantibiotic family. {ECO:0000305}.
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DR EMBL; Z47559; CAA87640.1; -; Genomic_DNA.
DR EMBL; AJ250862; CAB60258.1; -; Genomic_DNA.
DR PDB; 1MQX; NMR; -; A=49-67.
DR PDB; 1MQY; NMR; -; A=49-67.
DR PDB; 1MQZ; NMR; -; A=49-67.
DR PDB; 1QOW; X-ray; 1.06 A; A/B/C/D/E/F=49-67.
DR PDBsum; 1MQX; -.
DR PDBsum; 1MQY; -.
DR PDBsum; 1MQZ; -.
DR PDBsum; 1QOW; -.
DR AlphaFoldDB; P43683; -.
DR SMR; P43683; -.
DR DrugBank; DB02688; 2,3-Didehydroalanine.
DR DrugBank; DB01968; 2-Thioethenamine.
DR DrugBank; DB04454; Alpha-Aminobutyric Acid.
DR EvolutionaryTrace; P43683; -.
DR GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR027635; Lantibiotic2_lead_pep_dom.
DR TIGRFAMs; TIGR03898; lanti_MRSA_kill; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin; D-amino acid;
KW Lantibiotic; Thioether bond.
FT PROPEP 1..48
FT /id="PRO_0000017150"
FT PEPTIDE 49..68
FT /note="Lantibiotic mersacidin"
FT /id="PRO_0000017151"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000269|PubMed:9119018"
FT CROSSLNK 49..50
FT /note="Beta-methyllanthionine (Cys-Thr)"
FT /evidence="ECO:0000269|PubMed:9119018"
FT CROSSLNK 52..60
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:9119018"
FT CROSSLNK 61..66
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:9119018"
FT CROSSLNK 63..68
FT /note="S-(2-aminovinyl)-3-methyl-D-cysteine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:9119018"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1MQY"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1MQZ"
SQ SEQUENCE 68 AA; 7228 MW; 7718B772AE56A51F CRC64;
MSQEAIIRSW KDPFSRENST QNPAGNPFSE LKEAQMDKLV GAGDMEAACT FTLPGGGGVC
TLTSECIC
