ID   A0A0P1IBU6_9RHOB        Unreviewed;       488 AA.
AC   A0A0P1IBU6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Microcystinase C {ECO:0000256|PIRNR:PIRNR012702};
DE            Short=MlrC {ECO:0000256|PIRNR:PIRNR012702};
GN   ORFNames=RUE5091_02591 {ECO:0000313|EMBL:CUK04117.1};
OS   Ruegeria denitrificans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1715692 {ECO:0000313|EMBL:CUK04117.1, ECO:0000313|Proteomes:UP000051260};
RN   [1] {ECO:0000313|EMBL:CUK04117.1, ECO:0000313|Proteomes:UP000051260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5091 {ECO:0000313|EMBL:CUK04117.1,
RC   ECO:0000313|Proteomes:UP000051260};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) 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; CYUD01000007; CUK04117.1; -; Genomic_DNA.
DR   RefSeq; WP_058282278.1; NZ_CYUD01000007.1.
DR   AlphaFoldDB; A0A0P1IBU6; -.
DR   STRING; 1715692.RUE5091_02591; -.
DR   OrthoDB; 9782658at2; -.
DR   Proteomes; UP000051260; Unassembled WGS sequence.
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..287
FT                   /note="Microcystin LR degradation protein MlrC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07364"
FT   DOMAIN          297..470
FT                   /note="Microcystin LR degradation protein MlrC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07171"
SQ   SEQUENCE   488 AA;  52650 MW;  2ED4711A54906E8F CRC64;
     MRVFCASLAT ETNTFSPLRT DFSDFEQSFY APPGEHPVTP TLCSAVFPAL RKRAQDNELE
     LIEGTATWAE PGGLLNRETW ARLKREVLDQ VNAALPLDGV VLGLHGAMIA EGCVDCEGEL
     IEAIRAIVGP KTVIGASFDP HSHLSQKRVS NANVITVFKE FPHTDFVEAG EACVDLTLRT
     IKGDIRPVIS VFDVRMLDVL PTSQEPMRGF VDQLNQMEAK GEVLSASVIH GFMAGDSPDL
     GAKIVVLTDD DQAKADNIAR NLGTELFSFR GQTKPDYLSP VEALRKAQKA AHGPVVVADV
     WDNPGGGVAG DSTLILEEAI AQNLKSVAFG TIWDPMAVRL CHAAGEGAVF DLRFGGKTSA
     LAGNPIDATV TVVRNQRNAV QSFGASIVPM GDCSVIRLGG IEVVLNSNRS QAFSPDLFTN
     LGIDVTEKKI LVVKSTNHFH GAFSDVAAEI IYAAVEGPYP NDPTKTRYKN LTRPIWPIVK
     NPHEEVVE
//