ID   B1Z3I4_BURA4            Unreviewed;       500 AA.
AC   B1Z3I4;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Microcystinase C {ECO:0000256|PIRNR:PIRNR012702};
DE            Short=MlrC {ECO:0000256|PIRNR:PIRNR012702};
GN   OrderedLocusNames=BamMC406_5859 {ECO:0000313|EMBL:ACB68297.1};
OS   Burkholderia ambifaria (strain MC40-6).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=398577 {ECO:0000313|EMBL:ACB68297.1, ECO:0000313|Proteomes:UP000001680};
RN   [1] {ECO:0000313|Proteomes:UP000001680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC40-6 {ECO:0000313|Proteomes:UP000001680};
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA   Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 3 of Burkholderia ambifaria MC40-6.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in peptidolytic degradation of cyclic heptapeptide
CC       hepatotoxin microcystin (MC). {ECO:0000256|PIRNR:PIRNR012702}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR012702};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR012702};
CC   -!- SIMILARITY: Belongs to the peptidase M81 family.
CC       {ECO:0000256|PIRNR:PIRNR012702}.
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DR   EMBL; CP001027; ACB68297.1; -; Genomic_DNA.
DR   RefSeq; WP_012372206.1; NC_010557.1.
DR   AlphaFoldDB; B1Z3I4; -.
DR   KEGG; bac:BamMC406_5859; -.
DR   HOGENOM; CLU_028172_1_0_4; -.
DR   OrthoDB; 5288421at2; -.
DR   Proteomes; UP000001680; Chromosome 3.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR009197; MlrC.
DR   InterPro; IPR010799; MlrC_C.
DR   InterPro; IPR015995; MlrC_N.
DR   Pfam; PF07364; DUF1485; 1.
DR   Pfam; PF07171; MlrC_C; 1.
DR   PIRSF; PIRSF012702; UCP012702; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR012702};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR012702};
KW   Metalloprotease {ECO:0000256|PIRNR:PIRNR012702};
KW   Protease {ECO:0000256|PIRNR:PIRNR012702}.
FT   DOMAIN          2..285
FT                   /note="Microcystin LR degradation protein MlrC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07364"
FT   DOMAIN          299..478
FT                   /note="Microcystin LR degradation protein MlrC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07171"
SQ   SEQUENCE   500 AA;  52699 MW;  4E853B01BDC84510 CRC64;
     MKILIARMNH ETNTFSPVPT PLTAFGRNGP DWGDDAYRAN HGMRTAMAAF IDAAVREGAE
     IVTPVSAAAN PSGPVAADAY AAICDAIVAA TPGCDAVMLD LHGAMVAEQS ADGEGDLLAR
     VRAALPDAPV AVALDLHANV TQKMIDHADV IVSFKTYPHV DMYETGEHAA RVLLERLHGR
     ARPVLAWRQP PLMTSTLRSA SAEGAMRLAV EAARAAEADG MLAVSVLPGF ALADIPAPCI
     SVVVVADGDR AAGDAVAERI ARQIWDARDA FVYRSAPLAE SVAQAAALAR GADRPVLMLD
     HGDNCMSGGP CDTMDLLEAA LAQGLDGIVS GPLCDPEAVA ALIGAGVGAT VTVPVGNRMP
     SHGGARHAPF RATGIVRAIT DGEYVITGPT YTGQRAYMGR AAVLDIGVAT LIVTERTQEP
     WDLGVFESVG IDPRRARFLL LKSRMYCRPV FVPIAAALVE CDSRGVTGSD FGLFRYERLA
     RPVYPLDDVR QWEGAGPRTR
//