ID S5XVA3_PARAH Unreviewed; 499 AA.
AC S5XVA3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Microcystinase C {ECO:0000256|PIRNR:PIRNR012702};
DE Short=MlrC {ECO:0000256|PIRNR:PIRNR012702};
GN ORFNames=JCM7686_0179 {ECO:0000313|EMBL:AGT07290.1};
OS Paracoccus aminophilus JCM 7686.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT07290.1, ECO:0000313|Proteomes:UP000015480};
RN [1] {ECO:0000313|EMBL:AGT07290.1, ECO:0000313|Proteomes:UP000015480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT07290.1};
RX PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA Schluter A., Puhler A., Bartosik D.;
RT "Architecture and functions of a multipartite genome of the methylotrophic
RT bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT chromids.";
RL BMC Genomics 15:124-124(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}.
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DR EMBL; CP006650; AGT07290.1; -; Genomic_DNA.
DR RefSeq; WP_020948930.1; NC_022041.1.
DR AlphaFoldDB; S5XVA3; -.
DR STRING; 1367847.JCM7686_0179; -.
DR KEGG; pami:JCM7686_0179; -.
DR PATRIC; fig|1367847.3.peg.121; -.
DR eggNOG; COG5476; Bacteria.
DR HOGENOM; CLU_028172_1_0_5; -.
DR OrthoDB; 9782658at2; -.
DR Proteomes; UP000015480; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000015480}.
FT DOMAIN 5..296
FT /note="Microcystin LR degradation protein MlrC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07364"
FT DOMAIN 307..484
FT /note="Microcystin LR degradation protein MlrC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07171"
SQ SEQUENCE 499 AA; 53356 MW; 7B8E33A4B7B48FD1 CRC64;
MSFTVLTAEF MHESNTFSRY RTDLPQFQVD ALHYGEAAFA ARGAANTELA GFLDVAGPAG
WRVIHAISAH AVPGGQVTQA AYDHIAGVIL DKARAHQGQL DGVLLGLHGS MVPEFCQDGE
GHLLGLLREV LGDEIPIAVT LDLHAMVSEE MVERAQIFVS YKTYPHVDMR ETGTHAARLL
DRAMKGEIAP RTARAHVPML DEANSGRSDI PETFALYQRA SAAEASGLLA VSVNAAFTGA
DVACAGPTVL ATYDRRDPTQ QAEAEALVED LAAQIWDGRL KKRNVFIEVD EAAAEALGWT
GEKPLVIADY ADNPGAGSYG DSTALLSGLM AAGVTGAVFT PMIDPEAAAE LHRHREGETV
TLHIGGKGDP RFGGGPIEVT GVIRHLSDGA YTGDGPIQGG LAHSFGPTAV LDLGGIEVLI
VSEAQQMVDL QQLRAFGIEP TQRRVLALKS MQHFRAAFEP IAGKVIICDA GALATPRAER
RPYLRAPRPL WPLDRDFER
//
