ID B4EJ99_BURCJ Unreviewed; 497 AA.
AC B4EJ99;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Microcystinase C {ECO:0000256|PIRNR:PIRNR012702};
DE Short=MlrC {ECO:0000256|PIRNR:PIRNR012702};
GN ORFNames=BCAM2546 {ECO:0000313|EMBL:CAR56411.1};
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR56411.1, ECO:0000313|Proteomes:UP000001035};
RN [1] {ECO:0000313|EMBL:CAR56411.1, ECO:0000313|Proteomes:UP000001035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC CF5610 {ECO:0000313|Proteomes:UP000001035};
RX PubMed=18931103; DOI=10.1128/JB.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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; AM747721; CAR56411.1; -; Genomic_DNA.
DR RefSeq; WP_006484490.1; NC_011001.1.
DR AlphaFoldDB; B4EJ99; -.
DR KEGG; bcj:BCAM2546; -.
DR eggNOG; COG5476; Bacteria.
DR HOGENOM; CLU_028172_1_0_4; -.
DR BioCyc; BCEN216591:G1G1V-6657-MONOMER; -.
DR Proteomes; UP000001035; Chromosome 2.
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}.
FT DOMAIN 4..292
FT /note="Microcystin LR degradation protein MlrC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07364"
FT DOMAIN 304..480
FT /note="Microcystin LR degradation protein MlrC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07171"
SQ SEQUENCE 497 AA; 52626 MW; 10F7CF3D25C39E34 CRC64;
MTRRILVAGF QHETNTFAPT KAAYANFERG EGFPALVRGA DVLALRDVNI PAGGFINAAE
RRGWRLLPVI WAGASPSAHV TEDAFERIAG EIVEAARRGG CDAVYLDLHG AMVAEHTDDG
EGTLLERVRA AVGPDVPVVA SLDLHANVTD LMLRHADALV AFRTYPHVDM AETGERAAAL
LERLLAGRGP LHRAARRLPF LIPINGMCTL LDPACTMYAR LAALEAGGVV SLSFAPGFPA
ADFPECGPVI WGYGDADAVE AAVQTLYDTM LADEAQWQVP FLSPDDAVRE AMRLAADASK
PVVIADTQDN PGAGGDSNTT GLLRALLRHG AQDAALGLLW DPAAVAAAWR AGAGARIDLS
LGGSGVPGDE PLRARFEVVA LSDGICRYDG PMMNGMQADV GPVACLRIDG VRIVVSAGKA
QMLDRNLYRV GGIEPEAMKI LVNKSSVHFR ADFQDIAHAV LVAKAPGPMQ ADPADLPWTR
LARGMRMKPM GRAFGGA
//
