YICR_ECOSM
ID YICR_ECOSM Reviewed; 222 AA.
AC B1LK75;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=UPF0758 protein YicR {ECO:0000255|HAMAP-Rule:MF_00018};
GN Name=yicR {ECO:0000255|HAMAP-Rule:MF_00018};
GN OrderedLocusNames=EcSMS35_3973;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/jb.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
CC -!- SIMILARITY: Belongs to the UPF0758 family. YicR subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00018}.
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DR EMBL; CP000970; ACB17992.1; -; Genomic_DNA.
DR RefSeq; WP_001297375.1; NC_010498.1.
DR AlphaFoldDB; B1LK75; -.
DR SMR; B1LK75; -.
DR EnsemblBacteria; ACB17992; ACB17992; EcSMS35_3973.
DR GeneID; 60902671; -.
DR KEGG; ecm:EcSMS35_3973; -.
DR HOGENOM; CLU_073529_0_1_6; -.
DR OMA; AMPDYEL; -.
DR Proteomes; UP000007011; 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_1000116358"
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