ID F7YE91_MESOW Unreviewed; 491 AA.
AC F7YE91;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Microcystinase C {ECO:0000256|PIRNR:PIRNR012702};
DE Short=MlrC {ECO:0000256|PIRNR:PIRNR012702};
GN OrderedLocusNames=Mesop_1153 {ECO:0000313|EMBL:AEH85638.1};
OS Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=536019 {ECO:0000313|EMBL:AEH85638.1, ECO:0000313|Proteomes:UP000001623};
RN [1] {ECO:0000313|EMBL:AEH85638.1, ECO:0000313|Proteomes:UP000001623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24607 / HAMBI 3007 / WSM2075
RC {ECO:0000313|Proteomes:UP000001623};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Mavrommatis K.M., Tiwari R.P.,
RA Howieson J.G., O'Hara G.W., Nandasena K.G., Woyke T.;
RT "Complete sequence of Mesorhizobium opportunistum WSM2075.";
RL Submitted (OCT-2010) 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; CP002279; AEH85638.1; -; Genomic_DNA.
DR RefSeq; WP_013892375.1; NC_015675.1.
DR AlphaFoldDB; F7YE91; -.
DR STRING; 536019.Mesop_1153; -.
DR KEGG; mop:Mesop_1153; -.
DR eggNOG; COG5476; Bacteria.
DR HOGENOM; CLU_028172_1_0_5; -.
DR Proteomes; UP000001623; Chromosome.
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 301..476
FT /note="Microcystin LR degradation protein MlrC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07171"
SQ SEQUENCE 491 AA; 53092 MW; 906192D63D0DCA9E CRC64;
MRIFTASLAT ETNTFSPVPT DRASFEMAFY AGPGKHPETP TLCSSPIVAL RRRAAAEGLT
VIEGTATWAE PGGLVQRQTY EALRDEILGQ LKAALPVDAV ILGLHGAMVA QGYDDCEGDL
LERVRAMVGP DVVIASEFDP HSHLTPKRVA ASDIMAYFLE FPHTDFYERG EHVVELGLAA
ARGEIKPVIS TFDCRMIQVL PTSREPMRSF VDRIKALQGK DGVLSVSVIH GFMAADVPEM
GTRILVVTDN DKEKGDALAE RLGRELYAMR EKTAMTMLSA ADGIDRALAV RAERQDRPVV
IADIWDNPGG GVAGDGTVVL RAMLERGLKN VGVATIWDPI AVTFCQAAGE GAVIDLRFGG
KAGPLAGEPI DARVKVLKAV PEGWQSFGPS RVTLGPAALV RIEGTEVDII LNTNRTQTFE
PDIFSNIGVD PMSKDVLLIK STNHFYAGFE PIAAEIIYVS APSSYPSNPA VTDYKKLTRP
VWPRVADPWK A
//