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Database: UniProt
Entry: R0CJP0_RALPI
LinkDB: R0CJP0_RALPI
Original site: R0CJP0_RALPI 
ID   R0CJP0_RALPI            Unreviewed;       492 AA.
AC   R0CJP0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Microcystinase C {ECO:0000256|PIRNR:PIRNR012702};
DE            Short=MlrC {ECO:0000256|PIRNR:PIRNR012702};
GN   ORFNames=OR214_03429 {ECO:0000313|EMBL:ENZ76690.1};
OS   Ralstonia pickettii OR214.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=1264675 {ECO:0000313|EMBL:ENZ76690.1, ECO:0000313|Proteomes:UP000013280};
RN   [1] {ECO:0000313|EMBL:ENZ76690.1, ECO:0000313|Proteomes:UP000013280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR214 {ECO:0000313|EMBL:ENZ76690.1,
RC   ECO:0000313|Proteomes:UP000013280};
RX   PubMed=23792748;
RA   Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M., Epstein S.E.,
RA   Palumbo A.V., Brown S.D.;
RT   "Draft Genome Sequence for Ralstonia sp. Strain OR214, a Bacterium with
RT   Potential for Bioremediation.";
RL   Genome Announc. 1:0-0(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ENZ76690.1}.
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DR   EMBL; APMQ01000009; ENZ76690.1; -; Genomic_DNA.
DR   RefSeq; WP_004632561.1; NZ_APMQ01000009.1.
DR   AlphaFoldDB; R0CJP0; -.
DR   PATRIC; fig|1264675.3.peg.3360; -.
DR   Proteomes; UP000013280; 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..282
FT                   /note="Microcystin LR degradation protein MlrC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07364"
FT   DOMAIN          296..475
FT                   /note="Microcystin LR degradation protein MlrC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07171"
SQ   SEQUENCE   492 AA;  51675 MW;  2FF72277A96DDE2F CRC64;
     MRILIARFNH ETNTFSPVPT PLASFHPHYG ADAYRAAKGT RTAAGAFIDL AEAAGAEIVV
     PVVAGANPSG RVAAEAYTTL CDAIVAAAPG CDALMLDLHG AMVAENSDDG EGDLLERLRA
     VAPGVPIAVA LDLHGNLTQK FIDLADIAVS FKTYPHVDMY ETGEHAGRLL FDKLAGRANP
     VLAWRRLPMV THTLRSRTDE GAMHRAVALA KQAETDGMLA VSILAGFGLA DIAAPCLSVV
     VVGNGDKHAA DAAAQRIADA IWADREGFVY RSEPLTESIA RAAKLAHAPG SGPVLLLDHG
     DNCMSGGTCD DMHVLHEALK QGLSGIAVGP VCDPEAVAAM IEAGEGATVS LPVGDKVPLV
     QLGIYPVPRA LTGKVVGISD GEYTITGPTY TGQRIRMGRT ALLDIGAAQI VVTETPQEHW
     DLGIFTHIGV DPHAARFVLL KSRMYCRPVF VPIAKAVVEC DGGGVTSSDY SRFPFVKVQR
     PVFPLDADAV PA
//
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