ID   Y144_HAES1              Reviewed;         222 AA.
AC   Q0I0X9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=UPF0758 protein HS_0144;
GN   OrderedLocusNames=HS_0144;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
CC   -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR   EMBL; CP000436; ABI24422.1; -; Genomic_DNA.
DR   RefSeq; WP_011608296.1; NC_008309.1.
DR   AlphaFoldDB; Q0I0X9; -.
DR   SMR; Q0I0X9; -.
DR   STRING; 205914.HS_0144; -.
DR   EnsemblBacteria; ABI24422; ABI24422; HS_0144.
DR   GeneID; 56963985; -.
DR   KEGG; hso:HS_0144; -.
DR   eggNOG; COG2003; Bacteria.
DR   HOGENOM; CLU_073529_0_1_6; -.
DR   OMA; AMPDYEL; -.
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..222
FT                   /note="UPF0758 protein HS_0144"
FT                   /id="PRO_0000322691"
FT   DOMAIN          99..222
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           171..184
FT                   /note="JAMM motif"
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         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   222 AA;  25554 MW;  E3A9A6817E69A43E CRC64;
     MTQQNTTLMP REKLLKYGAS SLDDKELLAI FLRTGIKNCP VMQLSELVLA HFSSLRGLIN
     ADQKHFCQMK GLGITQFVQL QACTEMTKRY LLQELQFAQE FTSPDTVRMY LQTELENKDR
     EIFMVLFLDN QHRLIKKEEM FLGTINQANV YPREIIKTAL FCNAAALILA HNHPSGVSTP
     SMADRKMTEN IKQLSELMEI RVLDHFIIGK GNYFSFAEQG WI