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Database: UniProt
Entry: G9ZYY3_9PROT
LinkDB: G9ZYY3_9PROT
Original site: G9ZYY3_9PROT 
ID   G9ZYY3_9PROT            Unreviewed;       496 AA.
AC   G9ZYY3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, 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=HMPREF9946_01768 {ECO:0000313|EMBL:EHM01701.1};
OS   Acetobacteraceae bacterium AT-5844.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae.
OX   NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHM01701.1, ECO:0000313|Proteomes:UP000003292};
RN   [1] {ECO:0000313|EMBL:EHM01701.1, ECO:0000313|Proteomes:UP000003292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2011) 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   -!- 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:EHM01701.1}.
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DR   EMBL; AGEZ01000060; EHM01701.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9ZYY3; -.
DR   STRING; 1054213.HMPREF9946_01768; -.
DR   PATRIC; fig|1054213.3.peg.1632; -.
DR   eggNOG; COG5476; Bacteria.
DR   HOGENOM; CLU_028172_1_0_5; -.
DR   OrthoDB; 9782658at2; -.
DR   BioCyc; ABAC1054213:G1H32-1641-MONOMER; -.
DR   Proteomes; UP000003292; 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:UP000003292}.
FT   DOMAIN          5..288
FT                   /note="Microcystin LR degradation protein MlrC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07364"
FT   DOMAIN          299..473
FT                   /note="Microcystin LR degradation protein MlrC C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07171"
SQ   SEQUENCE   496 AA;  52751 MW;  980196C89224A8D6 CRC64;
     MSRKRILAGG IAQESHSFNP VLTNRARFNI RSGAAAIASA RGTNSLLGGI LDAAERAGAE
     VVVPTLFRAQ SGGPVEDAVF AEMRDMMCDA AKRGDFDAIV LPLHGGMLTP TLHDPEGALM
     ASLRAITGPD LPMTVAFDLH AHVTPQILET CDLLAGYLTN PHGDQGDTGR RACRAVLDIL
     DGRLRPVLSA VHVPMLTLGH DRTDEEPLMG LHARARAAVE SGLAYDVSIF NAQQFLDVPG
     LGNWVLAYGN GPDAKRDALA LELAQALWDQ RRALIGTYPS LEECLDRAER GTERPLILGD
     QGDRVAGGGP GDSTYVLRAL LARPGLPPSV VPLTEPEAVQ ACHKAGKGAR VTLEVGGRYS
     TVAPPVTVTG EILGLGTEAQ VTYDGPADAG YTAKLGAYAV LGVGKLRILL TDQPYSYLDP
     DYFRAMGVDP AEMGVVVTRS GYHFTLNFAA TGECITVDTP GMTSYRVQEL PFTVARPFFP
     LDEPDFKPAL ARLGRP
//
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