ID   Y536_MOOTA              Reviewed;         229 AA.
AC   Q2RL23;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=UPF0758 protein Moth_0536;
GN   OrderedLocusNames=Moth_0536;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
CC   -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR   EMBL; CP000232; ABC18866.1; -; Genomic_DNA.
DR   RefSeq; WP_011392073.1; NC_007644.1.
DR   RefSeq; YP_429409.1; NC_007644.1.
DR   AlphaFoldDB; Q2RL23; -.
DR   SMR; Q2RL23; -.
DR   STRING; 264732.Moth_0536; -.
DR   EnsemblBacteria; ABC18866; ABC18866; Moth_0536.
DR   GeneID; 61289221; -.
DR   KEGG; mta:Moth_0536; -.
DR   PATRIC; fig|264732.11.peg.578; -.
DR   eggNOG; COG2003; Bacteria.
DR   HOGENOM; CLU_073529_0_2_9; -.
DR   OMA; AMPDYEL; -.
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   CDD; cd08071; MPN_DUF2466; 1.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR025657; RadC_JAB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR001405; UPF0758.
DR   InterPro; IPR020891; UPF0758_CS.
DR   PANTHER; PTHR30471; PTHR30471; 1.
DR   Pfam; PF04002; RadC; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   TIGRFAMs; TIGR00608; radc; 1.
DR   PROSITE; PS50249; MPN; 1.
DR   PROSITE; PS01302; UPF0758; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..229
FT                   /note="UPF0758 protein Moth_0536"
FT                   /id="PRO_1000001668"
FT   DOMAIN          107..229
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           178..191
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   229 AA;  24884 MW;  2A7033F7893F81AC CRC64;
     MTGGQGVTIK ELPAELRPRE RLLAAGVQAL SNAELLAILL RTGTRTESAL DVARRLLSGP
     DGLQFLAGAT LEELQQQKGI GLAKAAELKA ALELGRRLAA FTLSRTVIRN PRDVAGLLLD
     EMRYLDRENF RTVSLNTKNQ VLGIDNVSVG SLNSSLAHPR EVFKDPIRRS AAAIILAHNH
     PSGDPTPSQE DIMVTRRLVE AGHILGIEVL DHLIIGDGRF TSLKERNLL