ID   Y1266_STAHJ             Reviewed;         228 AA.
AC   Q4L700;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=UPF0758 protein SH1266;
GN   OrderedLocusNames=SH1266;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR   EMBL; AP006716; BAE04575.1; -; Genomic_DNA.
DR   RefSeq; WP_011275564.1; NC_007168.1.
DR   AlphaFoldDB; Q4L700; -.
DR   SMR; Q4L700; -.
DR   STRING; 279808.SH1266; -.
DR   EnsemblBacteria; BAE04575; BAE04575; SH1266.
DR   GeneID; 58062540; -.
DR   KEGG; sha:SH1266; -.
DR   eggNOG; COG2003; Bacteria.
DR   HOGENOM; CLU_073529_0_2_9; -.
DR   OMA; AMPDYEL; -.
DR   OrthoDB; 1833204at2; -.
DR   Proteomes; UP000000543; 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..228
FT                   /note="UPF0758 protein SH1266"
FT                   /id="PRO_1000001699"
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   228 AA;  25498 MW;  8FDF39B0BAB8C66B CRC64;
     MRIKSMAKSE LPRERLIHNG AKSLSNSELL AILINTGRHG FSSLDIANEL LISFNGLKEL
     KHLSINDLTT IKGIGLYKAV ILKAAFELGE RMYARDFNEK IKITSPSDVS NIMMSKMKDL
     TQEHFVVLLL NSKNIVIKEE TIYKGTLNSS VIHPREVFKA AIRASSNAII VLHNHPSGDV
     TPSKEDIETT IRLKECGELL GIQVLDHIII GDQKYASLVE EGYFDLRN