ID   A0A157RDW3_9BORD        Unreviewed;       513 AA.
AC   A0A157RDW3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Microcystinase C {ECO:0000256|PIRNR:PIRNR012702};
DE            Short=MlrC {ECO:0000256|PIRNR:PIRNR012702};
GN   ORFNames=SAMEA3906487_01531 {ECO:0000313|EMBL:SAI68810.1};
OS   Bordetella trematum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI68810.1, ECO:0000313|Proteomes:UP000076825};
RN   [1] {ECO:0000313|EMBL:SAI68810.1, ECO:0000313|Proteomes:UP000076825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H044680328 {ECO:0000313|EMBL:SAI68810.1,
RC   ECO:0000313|Proteomes:UP000076825};
RG   Pathogen Informatics;
RL   Submitted (APR-2016) 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; LT546645; SAI68810.1; -; Genomic_DNA.
DR   RefSeq; WP_052125795.1; NZ_JPQP01000020.1.
DR   AlphaFoldDB; A0A157RDW3; -.
DR   STRING; 123899.SAMEA3906487_01531; -.
DR   KEGG; btrm:SAMEA390648701531; -.
DR   PATRIC; fig|123899.6.peg.1510; -.
DR   eggNOG; COG5476; Bacteria.
DR   Proteomes; UP000076825; Chromosome 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076825}.
FT   DOMAIN          20..314
FT                   /note="Microcystin LR degradation protein MlrC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07364"
FT   DOMAIN          327..507
FT                   /note="Microcystin LR degradation protein MlrC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07171"
SQ   SEQUENCE   513 AA;  54375 MW;  2C0D8C73FF77D117 CRC64;
     MTPLSSPMPP VSSCGARRKR LAVARFWFEG NAFTPIPCTL ADFQRQEWGE GAQVLAAARE
     TASEMGAVEQ FARQHPDWDV TVLRCAAAQP GGPIEDAAFE AIRADILAGL QAGQQQAPWD
     AIYLSLHGAA ITDARQNPEL ELLQAVRALA PHTPLGASFD LHGNLGPEIA PLLDAAAAYK
     TYPHIDQFDT ASRVLDLLAA NVQHGARTRV WLDKPGLLLS SFNMRTQAGP MCELQHLART
     LTQGPIRDIS VFGGFPYSDT VNTGASVVIT ADDDATGEAA ARQALATLSQ ALRQAAPEFA
     ISLPSATQGL AQALALLAQG PGLIAVNDPG DNPASGGSGD TTTLLRAVLD TPFDEPCVVA
     SFADPQAMRA VEQAGPGAEL TLSLGGRYNR AFGEPVTVQV RIERLTDGDF TNVGPKETGV
     LMRCGPTALL SLVARPNIRV ILTEHVVPAN DPGFFLMHGI DPVRQRLLCV KAKNHFRAAF
     GSLCRAIIDI DAPGPAALDL SLLPFRHARA QAV
//