ID   Y4229_AERS4             Reviewed;         220 AA.
AC   A4STD5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=UPF0758 protein ASA_4229;
GN   OrderedLocusNames=ASA_4229;
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449;
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA   Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA   Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT   the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
CC   -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABO92157.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000644; ABO92157.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_005321280.1; NC_009348.1.
DR   AlphaFoldDB; A4STD5; -.
DR   SMR; A4STD5; -.
DR   STRING; 382245.ASA_4229; -.
DR   EnsemblBacteria; ABO92157; ABO92157; ASA_4229.
DR   KEGG; asa:ASA_4229; -.
DR   eggNOG; COG2003; Bacteria.
DR   HOGENOM; CLU_073529_0_1_6; -.
DR   OrthoDB; 1833204at2; -.
DR   Proteomes; UP000000225; 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   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..220
FT                   /note="UPF0758 protein ASA_4229"
FT                   /id="PRO_0000322662"
FT   DOMAIN          95..220
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           169..182
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   220 AA;  24345 MW;  14C263FB21FE9CE1 CRC64;
     MSIKEWPEDE RPREKLLRQG PATLSDAELL AIFLRTGVNG LSAVDLSRQL LQQFGSLRAL
     LGADQGAFCH AHGLGPAKYA QLQAVLEMGK RHLAEQLQRG DALTSPQLTR DYLQAQLREV
     FALLLLDNQH RVIQFVELFY GTLDSASVWP REIVQIALKH NAAAVILAHN HPSGVAEPSR
     ADRQITDRIL AALALIDIRV LDHLVIGDGI TVSFAERGWL