ID   YICR_ECOK1              Reviewed;         222 AA.
AC   A1AHG9;
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 YicR {ECO:0000255|HAMAP-Rule:MF_00018};
GN   Name=yicR {ECO:0000255|HAMAP-Rule:MF_00018}; OrderedLocusNames=Ecok1_36150;
GN   ORFNames=APECO1_2823;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
CC   -!- SIMILARITY: Belongs to the UPF0758 family. YicR subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00018}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ03109.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000468; ABJ03109.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001297375.1; NC_008563.1.
DR   AlphaFoldDB; A1AHG9; -.
DR   SMR; A1AHG9; -.
DR   EnsemblBacteria; ABJ03109; ABJ03109; APECO1_2823.
DR   GeneID; 60902671; -.
DR   KEGG; ecv:APECO1_2823; -.
DR   HOGENOM; CLU_073529_0_2_6; -.
DR   Proteomes; UP000008216; 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   HAMAP; MF_00018; UPF0758_YicR; 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   InterPro; IPR022820; UPF0758_YicR.
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 YicR"
FT                   /id="PRO_0000322688"
FT   DOMAIN          100..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;  25258 MW;  D20E070CD5F6F4B6 CRC64;
     MKNNAQLLMP REKMLKFGIS ALTDVELLAL FLRTGTRGKD VLTLAKEMLE NFGSLYGLLT
     SEYEQFSGVH GIGVAKFAQL KGIAELARRY YNVRMREESP LLSPEMTREF LQSQLTGEER
     EIFMVIFLDS QHRVITHSRL FSGTLNHVEV HPREIIREAI KINASALILA HNHPSGCAEP
     SKADKLITER IIKSCQFMDL RVLDHIVIGR GEYVSFAERG WI