Y240_IDILO
ID Y240_IDILO Reviewed; 224 AA.
AC Q5QZB4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=UPF0758 protein IL0240;
GN OrderedLocusNames=IL0240;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR EMBL; AE017340; AAV81083.1; -; Genomic_DNA.
DR RefSeq; WP_011233503.1; NC_006512.1.
DR AlphaFoldDB; Q5QZB4; -.
DR SMR; Q5QZB4; -.
DR STRING; 283942.IL0240; -.
DR EnsemblBacteria; AAV81083; AAV81083; IL0240.
DR KEGG; ilo:IL0240; -.
DR eggNOG; COG2003; Bacteria.
DR HOGENOM; CLU_073529_0_2_6; -.
DR OMA; HEEFWII; -.
DR OrthoDB; 1833204at2; -.
DR Proteomes; UP000001171; 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; Reference proteome;
KW Zinc.
FT CHAIN 1..224
FT /note="UPF0758 protein IL0240"
FT /id="PRO_0000190705"
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; 24772 MW; 5ED0882674DC4BBE CRC64;
MSVKEWPVSE RPREKLQTQG AEYLSDAELL AILLGSGSGG QDVVSFARRL LSDFGGVGAL
LTATPEQLLA CNGIGPARVN QLRVVLELSR RYLKWQLERS DGFTEPTMVK DYLTSQLRHQ
GREVFAILLL DSQHRLLRYE ELFQGTINAA PVYPREVIKL VMQYNAAAVI LAHNHPSGVA
EPSQADQRVT ERVKKALTLI DVALLDHFVV GAGDPISFAE RGLL