ID   Y2303_METBF             Reviewed;         229 AA.
AC   Q46A65;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=UPF0758 protein Mbar_A2303;
GN   OrderedLocusNames=Mbar_A2303;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
CC   -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR   EMBL; CP000099; AAZ71227.1; -; Genomic_DNA.
DR   RefSeq; WP_011307273.1; NC_007355.1.
DR   AlphaFoldDB; Q46A65; -.
DR   SMR; Q46A65; -.
DR   STRING; 269797.Mbar_A2303; -.
DR   EnsemblBacteria; AAZ71227; AAZ71227; Mbar_A2303.
DR   GeneID; 3625173; -.
DR   KEGG; mba:Mbar_A2303; -.
DR   eggNOG; arCOG04919; Archaea.
DR   HOGENOM; CLU_073529_0_2_2; -.
DR   OMA; AMPDYEL; -.
DR   OrthoDB; 63755at2157; -.
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; IPR001405; UPF0758.
DR   InterPro; IPR020891; UPF0758_CS.
DR   PANTHER; PTHR30471; PTHR30471; 1.
DR   Pfam; PF04002; RadC; 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 Mbar_A2303"
FT                   /id="PRO_1000001665"
FT   DOMAIN          106..228
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           177..190
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         190
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;  25731 MW;  5D1DB930816A4D45 CRC64;
     MEISKVRIQD IPEEERPRER LIRNGPESLS NSELLGVILR TGSNKENVVS LSSRIFSEYS
     IKQLSLANVS RLMKVHGVGK AKAAQIAAVF ELARRLETFV EEPKRKVCSP KDVYTLMYPK
     MREQKKEKFI TLCLDTKNQI LKEEVVSIGS LNASIVHPRE VFKSALMESS ASVIMIHNHP
     SGDPSPSRED IMVTEKMVEG GKLLGIDVLD HIIIGEGRYV SLKDEGFVR