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}.
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; 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
//