ID A0A146AIV8_9BORD Unreviewed; 509 AA.
AC A0A146AIV8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-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=SAMEA3906487_01143 {ECO:0000313|EMBL:SAI68215.1};
OS Bordetella trematum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI68215.1, ECO:0000313|Proteomes:UP000076825};
RN [1] {ECO:0000313|EMBL:SAI68215.1, ECO:0000313|Proteomes:UP000076825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H044680328 {ECO:0000313|EMBL:SAI68215.1,
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT546645; SAI68215.1; -; Genomic_DNA.
DR RefSeq; WP_063491677.1; NZ_UFUJ01000001.1.
DR AlphaFoldDB; A0A146AIV8; -.
DR STRING; 123899.SAMEA3906487_01143; -.
DR GeneID; 56587452; -.
DR KEGG; btrm:SAMEA390648701143; -.
DR PATRIC; fig|123899.6.peg.1121; -.
DR eggNOG; COG5476; Bacteria.
DR OrthoDB; 5288421at2; -.
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 2..293
FT /note="Microcystin LR degradation protein MlrC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07364"
FT DOMAIN 303..484
FT /note="Microcystin LR degradation protein MlrC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07171"
SQ SEQUENCE 509 AA; 54446 MW; A080B4C27CCCD289 CRC64;
MKFVIALIRH ETNTFSPVGT ELSDFRRGTS GSGPAYGEAA RLACEGTNNA AAAYLDLARE
MGAEVDFSIY ASAVPSGLVS RAAFEALCEA VLDSARQGCD AILLDLHGAM VVDGYPDAEG
ELLRRLRACT PAGLPIGVAL DFHANFSSEL VCNATAIAGY CTYPHVDVYE TGARVGRSIR
ALLEGRSQPV VLWRRLPMLT HMLRQTPAMQ PMKDIMERAM QAERDGEVCN ASVFGGFPLA
DIACAGLSVV IVAERARVDA ARRLLDELCD LAWSRRADFV FPSEPVADSI AHARTLEQGP
VILVDHGDNC GAGGTTDVMD VLEEVLRQGL QDVVAGPFCD PAAVAALFEQ GVGADVTLEV
GGKTDMPALG LAGRPLRLSG VVERLTDGDY TVTGPMFTGV RLSLGRTAVL RVGTVRVFIS
ERPQEPYDTG VFTHAGVDPA QSRYVLLKSR QHFRAGFEPF ARHIVLVGGP GVCSSDYGIF
PFKHLSRPIY PLDADATLEH AQSWLAGNA
//
