MLRC_SPHSX
ID MLRC_SPHSX Reviewed; 507 AA.
AC Q93CA6;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Microcystinase C {ECO:0000303|PubMed:22591122};
DE Short=MlrC {ECO:0000303|PubMed:11769251, ECO:0000312|EMBL:AAL10288.1};
DE Flags: Precursor; Fragment;
GN Name=mlrC {ECO:0000312|EMBL:AAL10288.1};
OS Sphingomonas sp.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=28214;
RN [1] {ECO:0000312|EMBL:AAL10288.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ACM-3962 {ECO:0000312|EMBL:AAL10288.1};
RX PubMed=11769251; DOI=10.1002/tox.10013.abs;
RA Bourne D.G., Riddles P., Jones G.J., Smith W., Blakeley R.L.;
RT "Characterisation of a gene cluster involved in bacterial degradation of
RT the cyanobacterial toxin microcystin LR.";
RL Environ. Toxicol. 16:523-534(2001).
RN [2]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=ACM-3962 {ECO:0000303|PubMed:8899999};
RX PubMed=8899999; DOI=10.1128/aem.62.11.4086-4094.1996;
RA Bourne D.G., Jones G.J., Blakeley R.L., Jones A., Negri A.P., Riddles P.;
RT "Enzymatic pathway for the bacterial degradation of the cyanobacterial
RT cyclic peptide toxin microcystin LR.";
RL Appl. Environ. Microbiol. 62:4086-4094(1996).
RN [3]
RP FUNCTION.
RC STRAIN=ACM-3962 {ECO:0000303|PubMed:22591122};
RX PubMed=22591122; DOI=10.1021/tx300174e;
RA Dziga D., Wasylewski M., Szetela A., Bochenska O., Wladyka B.;
RT "Verification of the role of MlrC in microcystin biodegradation by studies
RT using a heterologously expressed enzyme.";
RL Chem. Res. Toxicol. 25:1192-1194(2012).
CC -!- FUNCTION: Involved in peptidolytic degradation of cyclic heptapeptide
CC hepatotoxin microcystin (MC) (PubMed:11769251,PubMed:8899999). Cleaves
CC both linear MC and the tetrapeptide degradation product of MC
CC (PubMed:11769251). Cleaves the Adda-Glu peptide bond of linear MC
CC heptapeptides (PubMed:22591122). {ECO:0000269|PubMed:11769251,
CC ECO:0000269|PubMed:22591122, ECO:0000269|PubMed:8899999}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by the metal chelators EDTA and 1,10-
CC phenanthroline. {ECO:0000269|PubMed:8899999}.
CC -!- SIMILARITY: Belongs to the peptidase M81 family. {ECO:0000305}.
CC -!- CAUTION: MC degradation was originally described as sequential, three-
CC step process catalyzed by enzymes subsequently named as MlrA, MlrB and
CC MlrC, where MlrC catalyzes hydrolysis of tetrapeptides generated by
CC MlrB (PubMed:8899999). It is shown later that purified MlrC hydrolyzes
CC also linear MC (PubMed:11769251,PubMed:22591122) so it is not clear if
CC MlrB is indispensable in this pathway. {ECO:0000269|PubMed:11769251,
CC ECO:0000269|PubMed:22591122, ECO:0000269|PubMed:8899999}.
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; AF411070; AAL10288.1; -; Genomic_DNA.
DR AlphaFoldDB; Q93CA6; -.
DR SMR; Q93CA6; -.
DR MEROPS; M81.001; -.
DR PRIDE; Q93CA6; -.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
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; Metal-binding; Metalloprotease; Protease; Signal; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..>507
FT /note="Microcystinase C"
FT /id="PRO_0000431512"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT NON_TER 507
FT /evidence="ECO:0000312|EMBL:AAL10288.1"
SQ SEQUENCE 507 AA; 54788 MW; 7A56DBB2F239285D CRC64;
MLDRRTLMGG ILSMAGSKAT GAALPGRRLR VFVATLGTET NSFSPLPTGL DAFRATMLWR
PGEHPDFATE ATGPLWAARE RAREGRYEVI EGTCAFAMPG GPVSAQAYQL LRDEILDQLR
RAMPVDIVAF GLHGAMLAFG EDECEADLLE RARAIVGPDV ALGAELDLHA HLSQRLVRAA
DVLVAFKYYP HIDYVERARD LLDLLERIRA GEIMPTSSLF NCQMVAGLAT QSSPMKELVA
DLFEFERRGE VLSGSLIQGF RAGDVARMGS KVLIYTNNDQ PAAASIAQDF GRRYQAMASI
MKGNGPERSF AADIELAKAA TAYPVILVDS SDNPGGGASG DNMALARAML DNDLVPSCIG
PIWDPLAVQL GFEAGLGADF SLRVGGKVGE ASGLPLDVRG KITGLAENVT QNLQGSRPPL
GRVVCISTAG LDIIVSEIRD QCYGPDMFRA LGVEPANKRY VAVKSSEQWR IGFGDMGRSV
IYVASSQQSS IRHYHKRSRP MWPFEPV
