ID W4HIZ7_9RHOB Unreviewed; 521 AA.
AC W4HIZ7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Microcystinase C {ECO:0000256|PIRNR:PIRNR012702};
DE Short=MlrC {ECO:0000256|PIRNR:PIRNR012702};
GN ORFNames=ATO8_11744 {ECO:0000313|EMBL:ETW12689.1};
OS Roseivivax marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1379903 {ECO:0000313|EMBL:ETW12689.1, ECO:0000313|Proteomes:UP000019063};
RN [1] {ECO:0000313|EMBL:ETW12689.1, ECO:0000313|Proteomes:UP000019063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-s10s {ECO:0000313|EMBL:ETW12689.1,
RC ECO:0000313|Proteomes:UP000019063};
RX PubMed=24567080; DOI=10.1007/s10482-014-0140-5;
RA Li G., Lai Q., Liu X., Sun F., Shao Z.;
RT "Roseivivax atlanticus sp. nov., isolated from surface seawater of the
RT Atlantic Ocean.";
RL Antonie Van Leeuwenhoek 105:863-869(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:ETW12689.1}.
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DR EMBL; AQQW01000006; ETW12689.1; -; Genomic_DNA.
DR RefSeq; WP_043844688.1; NZ_AQQW01000006.1.
DR AlphaFoldDB; W4HIZ7; -.
DR STRING; 1379903.ATO8_11744; -.
DR PATRIC; fig|1317118.6.peg.2420; -.
DR eggNOG; COG5476; Bacteria.
DR Proteomes; UP000019063; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019063}.
FT DOMAIN 2..294
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"
FT REGION 496..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 53518 MW; 1F13DCADDE63F81B CRC64;
MRVALAGFVH ETNTFAPAPA DMAAFEAGGG YIPLSRGDEI AARGTGVNLG ISGALAVAEA
RGWDGVPILW AGAIPSAPVT RDAFETIADE IVSGLRAAGP LDGVLLDLHG AMVADHLDDG
EAEIAERVRA AVGQDVPVVA ALDLHGNISE RFARTVDGLF GFRTYPHVDM AETGRRAADL
LAHLMATGAR PACTVRRMDY LVPIAAQSTD TQPGRDLYAG LADVEREVPG VRAASLFMGF
PAADIPDCGP TAIVYADTQE AADAGADRIA GAYADAESRF DIATYEAADA VAEAARRAAG
ASGPVVLADT QDNPGAGGVS ATTGLLRALV AADARNAAIG LIVDPASARQ AHEAGQGATA
TFRLGAHPDF TADRPFEVEA VVEALSDGRL TASGPFYGGT KLDLGPSACL RIGGVSVAVS
SRIAQTADRE MFRFVGIVPE DASILAVKSS THFRADFTPI ASDILIAIAP GPMPYDPADL
PFTRLRAGLR LSPNGPAFGD ARADDARSGR GGSSAAASQY H
//
