ID   Y528_ACIF5              Reviewed;         224 AA.
AC   B5EMA3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=UPF0758 protein Lferr_0528;
GN   OrderedLocusNames=Lferr_0528;
OS   Acidithiobacillus ferrooxidans (strain ATCC 53993 / BNL-5-31)
OS   (Leptospirillum ferrooxidans (ATCC 53993)).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=380394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53993 / BNL-5-31;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Borole A.P.;
RT   "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR   EMBL; CP001132; ACH82782.1; -; Genomic_DNA.
DR   RefSeq; WP_012536103.1; NC_011206.1.
DR   AlphaFoldDB; B5EMA3; -.
DR   SMR; B5EMA3; -.
DR   GeneID; 66431414; -.
DR   KEGG; afe:Lferr_0528; -.
DR   eggNOG; COG2003; Bacteria.
DR   HOGENOM; CLU_073529_0_1_6; -.
DR   OMA; HEEFWII; -.
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..224
FT                   /note="UPF0758 protein Lferr_0528"
FT                   /id="PRO_1000089784"
FT   DOMAIN          102..224
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           173..186
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   224 AA;  25071 MW;  495005A6B0ED014D CRC64;
     MAITDWPVDE RPRERLLQKG AATLSDAELL AIFLRVGVVG KSAVDLAREM LLNFGSLRAL
     LTASHHDFCV HKGLGDAKYA LLQAVLEMGR RHLAEEWQRG DGLDSPLRVR QYLSATLRDR
     CREVFAVIFL DNRHRVLRFE EMFLGTIDGA TVHIREVLKR ALELNAAALI VAHNHPSGVA
     EPSAADLSLT RRLDQAMQLL DLRLLDHFIV GDGEPLSLRE QGGW