ID S9RUK2_9RALS Unreviewed; 486 AA.
AC S9RUK2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Microcystinase C {ECO:0000256|PIRNR:PIRNR012702};
DE Short=MlrC {ECO:0000256|PIRNR:PIRNR012702};
GN ORFNames=C404_21930 {ECO:0000313|EMBL:EPX95963.1};
OS Ralstonia sp. AU12-08.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1235457 {ECO:0000313|EMBL:EPX95963.1, ECO:0000313|Proteomes:UP000015343};
RN [1] {ECO:0000313|EMBL:EPX95963.1, ECO:0000313|Proteomes:UP000015343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU12-08 {ECO:0000313|EMBL:EPX95963.1,
RC ECO:0000313|Proteomes:UP000015343};
RX PubMed=24503988;
RA Zhang L., Morrison M., Rickard C.M.;
RT "Draft Genome Sequence of Ralstonia pickettii AU12-08, Isolated from an
RT Intravascular Catheter in Australia.";
RL Genome Announc. 2:e00027-14(2014).
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:EPX95963.1}.
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DR EMBL; ASZV01000046; EPX95963.1; -; Genomic_DNA.
DR RefSeq; WP_021196686.1; NZ_ASZV01000046.1.
DR AlphaFoldDB; S9RUK2; -.
DR PATRIC; fig|1235457.3.peg.4374; -.
DR eggNOG; COG5476; Bacteria.
DR Proteomes; UP000015343; 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..288
FT /note="Microcystin LR degradation protein MlrC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07364"
FT DOMAIN 297..471
FT /note="Microcystin LR degradation protein MlrC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07171"
SQ SEQUENCE 486 AA; 52438 MW; 7572420DF19C4F78 CRC64;
MKLFTAQLST ETNTFAPCPT GWGGFEESGI FHGDASLRAP QGMGFALAEA RRLAERDGHE
IVEGICAEAQ PSGPTIRAVY ESLRDEILGK LEAAQPLDGV LLLLHGAMVA EGYDDCEGDL
LSRVRAIVGP EVPIAATLDP HCHFTERMRR SADILIAYKE YPHTDPIDRL REAYQLLLDT
AAGKIRPTTG VYDCRMVGAW HTTSEPMATF VRRMKSLEGR DGVLSVSFGH GFPWGDVPEA
GAKFWVVTDN NLAAATALAT QLGHEFWALR EATRPAWLDV DTGLDRALAV GSGPVVIGDV
ADNPGGGAPG DNTVILRRII ERQIANVAIG CFWDLGAIQI CHDAGVGATF DLRLGGKCGV
ASADPLDLRV TVRALSDQHT QSISGLTIPF GRAVWLEAAN GVDIVLASVR NQVVSVDAFT
GLGIDFESKR LVVVKSTQHF QAEFAPRAKA IFHIAAPGAV TPSFADLHYR HRDLNYWPRV
SNPFEA
//
