ID A9MC39_BRUC2 Unreviewed; 489 AA.
AC A9MC39;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Microcystinase C {ECO:0000256|PIRNR:PIRNR012702};
DE Short=MlrC {ECO:0000256|PIRNR:PIRNR012702};
GN OrderedLocusNames=BCAN_B0760 {ECO:0000313|EMBL:ABX63926.1};
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179 {ECO:0000313|EMBL:ABX63926.1, ECO:0000313|Proteomes:UP000001385};
RN [1] {ECO:0000313|EMBL:ABX63926.1, ECO:0000313|Proteomes:UP000001385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854 {ECO:0000313|Proteomes:UP000001385};
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-2007) 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}.
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DR EMBL; CP000873; ABX63926.1; -; Genomic_DNA.
DR RefSeq; WP_004692202.1; NC_010104.1.
DR AlphaFoldDB; A9MC39; -.
DR GeneID; 55592402; -.
DR KEGG; bcs:BCAN_B0760; -.
DR HOGENOM; CLU_028172_1_0_5; -.
DR PhylomeDB; A9MC39; -.
DR Proteomes; UP000001385; Chromosome II.
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 2..288
FT /note="Microcystin LR degradation protein MlrC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07364"
FT DOMAIN 301..476
FT /note="Microcystin LR degradation protein MlrC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07171"
SQ SEQUENCE 489 AA; 52928 MW; 95C279A2D489BF51 CRC64;
MRIFTASLAT ETNTFSPVPT DRASFEMAFY AAPGKHPETP TLCSSPIVAL RKRAAAEGLT
VIEGTATWAE PGGLLQRQAF EELRDEILDQ LKAAMPVDAV VLGLHGAMMA QGYDDCEGDL
LERARAIVGP GVLVASEFDP HSHLTPKRVQ NLNIFASFLE FPHTDFYERG EHVVELALDA
LKGRTKPVIS TFDCRMIAVL PTSKEPMRSF VDRIKALQGK DGILSISVIH GFMAADVPEM
GTRILVVTDN DPQKGAALAE KLGRELIAMR EQTSMAMLDT DQGIDRALAA HAANPSKPAV
IADVWDNPGG GVAGDGTYIL RRLIERGVNN AGIATIWDPI AVTFCHAAGE GAVIDLRFGG
KSGPLGGEPI DARVTVLKVA NEGWQSFGPS RVTLGPSAVV RIEDTGIDII LNTNRTQTFE
PDIFFNLGID PMTKNVLVVK STNHFHAGFA PVAAEIIYVD APSSYPSNPR TTNYRKLNRA
IWPRVEDPW
//
