MICA_CLAMM
ID MICA_CLAMM Reviewed; 68 AA.
AC Q09T02;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Lantibiotic michiganin-A;
DE Flags: Precursor;
GN Name=micA {ECO:0000312|EMBL:ABE60717.1};
OS Clavibacter michiganensis subsp. michiganensis.
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX NCBI_TaxID=33013;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABE60717.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-68, FUNCTION,
RP DEHYDRATION AT THR-55, LANTHIONINE CROSS-LINKS, AND MASS SPECTROMETRY.
RC STRAIN=NCPPB 1468 / LMG3690 / ICMP 2541 {ECO:0000312|EMBL:ABE60717.1};
RX PubMed=16957199; DOI=10.1128/aem.00639-06;
RA Holtsmark I., Mantzilas D., Eijsink V.G., Brurberg M.B.;
RT "Purification, characterization, and gene sequence of michiganin A, an
RT actagardine-like lantibiotic produced by the tomato pathogen Clavibacter
RT michiganensis subsp. michiganensis.";
RL Appl. Environ. Microbiol. 72:5814-5821(2006).
CC -!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic)
CC active against S.michiganensis subspecies sepedonicus strain 2136
CC (MIC=30 pmol/ml). The bactericidal activity of lantibiotics is based on
CC depolarization of energized bacterial cytoplasmic membranes, initiated
CC by the formation of aqueous transmembrane pores.
CC {ECO:0000269|PubMed:16957199}.
CC -!- SUBCELLULAR LOCATION: Secreted.
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 62-67 beta-methyllanthionine thioether bond is
CC oxidized to a sulfoxide. This is followed by membrane translocation and
CC cleavage of the modified precursor. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=2145; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16957199};
CC -!- SIMILARITY: Belongs to the type B lantibiotic family. {ECO:0000255}.
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DR EMBL; DQ458780; ABE60717.1; -; Genomic_DNA.
DR RefSeq; WP_012038654.1; NZ_QODA01000011.1.
DR AlphaFoldDB; Q09T02; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0046931; P:pore complex assembly; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW Lantibiotic; Oxidation; Secreted; Thioether bond.
FT PROPEP 1..47
FT /evidence="ECO:0000269|PubMed:16957199"
FT /id="PRO_0000283821"
FT PEPTIDE 48..68
FT /note="Lantibiotic michiganin-A"
FT /id="PRO_5000141526"
FT MOD_RES 55
FT /note="2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:16957199"
FT CROSSLNK 49..54
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000269|PubMed:16957199"
FT CROSSLNK 57..65
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:16957199"
FT CROSSLNK 62..67
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:16957199"
SQ SEQUENCE 68 AA; 7572 MW; 0423E7DDA3856F61 CRC64;
MNDILETETP VMVSPRWDML LDAGEDTSPS VQTQIDAEFR RVVSPYMSSS GWLCTLTIEC
GTIICACR