ID N9Q992_9GAMM Unreviewed; 507 AA.
AC N9Q992;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Microcystinase C {ECO:0000256|PIRNR:PIRNR012702};
DE Short=MlrC {ECO:0000256|PIRNR:PIRNR012702};
GN ORFNames=F893_01382 {ECO:0000313|EMBL:ENX23492.1};
OS Acinetobacter sp. CIP 102136.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1144665 {ECO:0000313|EMBL:ENX23492.1, ECO:0000313|Proteomes:UP000013199};
RN [1] {ECO:0000313|EMBL:ENX23492.1, ECO:0000313|Proteomes:UP000013199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102136 {ECO:0000313|EMBL:ENX23492.1,
RC ECO:0000313|Proteomes:UP000013199};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. CIP 102136.";
RL Submitted (FEB-2013) 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:ENX23492.1}.
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DR EMBL; APRV01000025; ENX23492.1; -; Genomic_DNA.
DR RefSeq; WP_005251178.1; NZ_KB850142.1.
DR AlphaFoldDB; N9Q992; -.
DR PATRIC; fig|1144665.3.peg.1314; -.
DR HOGENOM; CLU_028172_1_0_6; -.
DR Proteomes; UP000013199; 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}.
FT DOMAIN 3..291
FT /note="Microcystin LR degradation protein MlrC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07364"
FT DOMAIN 305..482
FT /note="Microcystin LR degradation protein MlrC C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07171"
SQ SEQUENCE 507 AA; 56197 MW; C0C0AE23F884A6C4 CRC64;
MKKIIIAGFQ HETNTFAPTK ARYVDFVQGG GFPPLSRGAD VLKFREQNIP IGGFIQQAEQ
FGYQLLPVIW AGTSPSAHVE QDTYQRICDE IIASIQQHPA DAVYLDLHGA MVSEQVDDGE
GELLRRVREA VGSDIPVIAS LDFHANVTQA MFAHSDALIC YRTYPHVDMA QTGQRCAQLL
NQIFEGKKLY KKMYKLPFLI ALNAQCTELE PTQSCMNLLE QLEQNNPVQM NFTPGFPAAD
FEECGGCIWG YSENAEQLDQ AMQRYIDHVL QQEAHWNMDF LSPDHAVQQA IQLYQQHYSA
KPVVIADTQD NPGAGGDSNT TGMLSALYRH PVKNALIGLI VDPAVVQQAY QFELGQHFYA
QLGGTSGIVG DAPFSAEFKI KAYSDGKFSY GGPMMHGVEA DIGPSILLEI DGIEIAVSSY
KAQLLDRNMF RIFGVVPEDK SIIVVKSSVH FRADFQDMAA AILVAKAPGA MKADPNDLPW
QKIEPDRRLV PMGESLAQRD QPLRRTV
//