ID   Y1330_BRUMB             Reviewed;         249 AA.
AC   C0RJP6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=UPF0758 protein BMEA_A1330;
GN   OrderedLocusNames=BMEA_A1330;
OS   Brucella melitensis biotype 2 (strain ATCC 23457).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=546272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23457;
RA   Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA   Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA   Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA   Han C., Detter J.C., Bruce D., Brettin T.S.;
RT   "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR   EMBL; CP001488; ACO01054.1; -; Genomic_DNA.
DR   RefSeq; WP_004686411.1; NC_012441.1.
DR   AlphaFoldDB; C0RJP6; -.
DR   SMR; C0RJP6; -.
DR   EnsemblBacteria; ACO01054; ACO01054; BMEA_A1330.
DR   KEGG; bmi:BMEA_A1330; -.
DR   HOGENOM; CLU_073529_0_0_5; -.
DR   OMA; AMPDYEL; -.
DR   Proteomes; UP000001748; Chromosome I.
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..249
FT                   /note="UPF0758 protein BMEA_A1330"
FT                   /id="PRO_1000195287"
FT   DOMAIN          127..249
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           198..211
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         198
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   249 AA;  27706 MW;  1CF77F826027B8FD CRC64;
     MAKKKDTPGD GEFPGFSDTL QRTPKLEKPH YAGHRDRLKQ RFRDAPDALA DYELLELLLF
     RAIRRADTKP IAKALLNRFG SIAEVLTAPE NLIAEIPGAG PTVALELKLV EAIAKRSARS
     TVMEREVLGS WDKVINYCTA AMAFETREQF RILFLDKKNK LIADEVQQTG TVDHTPVYPR
     EVVKRALELS ATAIILVHNH PSGDPTPSRA DIDMTKQLVN AAKALNITVH DHVIIGKHGH
     ASLRSLRLI