ID   Y3126_ACIAD             Reviewed;         271 AA.
AC   Q6F7Z8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=UPF0758 protein ACIAD3126;
GN   OrderedLocusNames=ACIAD3126;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR   EMBL; CR543861; CAG69817.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6F7Z8; -.
DR   SMR; Q6F7Z8; -.
DR   STRING; 62977.ACIAD3126; -.
DR   EnsemblBacteria; CAG69817; CAG69817; ACIAD3126.
DR   KEGG; aci:ACIAD3126; -.
DR   eggNOG; COG2003; Bacteria.
DR   HOGENOM; CLU_073529_0_2_6; -.
DR   OMA; AMPDYEL; -.
DR   Proteomes; UP000000430; 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   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   PANTHER; PTHR30471; PTHR30471; 1.
DR   Pfam; PF04002; RadC; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   TIGRFAMs; TIGR00608; radc; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..271
FT                   /note="UPF0758 protein ACIAD3126"
FT                   /id="PRO_0000190674"
FT   DOMAIN          120..242
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           191..204
FT                   /note="JAMM motif"
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"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   271 AA;  31108 MW;  01E0F5DE502DE93A CRC64;
     MSFSNQNYNV HTFIIMNQSI KFWPEQERPR ERLLHSGPES LSDAELLAIF LRTGSKQHSA
     VELARLMIQH FGGLNPVFDA SLQELSHFHG IGTTKYAHLM AVKELGRRYL NHYFHQDALN
     LNSSRLVLDY LRYELLGEKQ EVFAVLCLDS ELRKLNFKKL FYGSLNACNI SINHTLRYAL
     QQHACHIVIA HNHPFGKAEP SAADLDLTHQ LYQACQLVEI KLLDHFIIAK DGTFSFAERA
     LLSQKKCMHT DIDKPDLTGE DHHKKSCDRS P