ID Q98EP9_RHILO Unreviewed; 508 AA.
AC Q98EP9;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Microcystinase C {ECO:0000256|PIRNR:PIRNR012702};
DE Short=MlrC {ECO:0000256|PIRNR:PIRNR012702};
GN OrderedLocusNames=mll4144 {ECO:0000313|EMBL:BAB50869.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB50869.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB50869.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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; BA000012; BAB50869.1; -; Genomic_DNA.
DR RefSeq; WP_010912211.1; NC_002678.2.
DR AlphaFoldDB; Q98EP9; -.
DR KEGG; mlo:mll4144; -.
DR PATRIC; fig|266835.9.peg.3273; -.
DR eggNOG; COG5476; Bacteria.
DR HOGENOM; CLU_028172_1_0_5; -.
DR Proteomes; UP000000552; Chromosome.
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"
FT REGION 486..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 54903 MW; D4ABA16896D33711 CRC64;
MRIFTASLAT ETNTFSPVPT DRASFEMAFY AGPGRHPETP TLCSSPIVAL RRRAAKEGLT
VIEGTATWAE PGGLVQRQTF EALRDEILDQ LKAALPVDAV ILGLHGAMVA QGYDDCEGDL
LERVRAIVGP DVVIASEFDP HSHLTPKRVA ASDIMAYFLE FPHTDFYERG EHVVELGLAA
ARGEIKPVIS TFDCRMIQVL PTSREPMRSF VDRIKALHGK DGVLSVSVIH GFMAADVPEM
GTRILVVTDN DKARGDALAE LLGRELYELR EKTAMTMLDT ADGIDRALAV RAKKPGKPVV
IADIWDNPGG GVPGDGTFVL RQMLARGLDR FGVATIWDPI AVTFCLAAGE GAVIDLRFGG
KAGPQAGEPI DARVKVLKAV AEGWQSFGPS RVTLGPTALV RIEGTEVDII LNTNRTQTFE
PDIFSNIGVD PLGKDMLLIK STNHFYAGFE PIAAEIIYVT APSSYPSNPA VTDYKKLRRP
VWPRVADPWK DEAPPSPLVG EGVAEGDG
//
