YICR_ECODH
ID YICR_ECODH Reviewed; 222 AA.
AC B1X972;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=UPF0758 protein YicR {ECO:0000255|HAMAP-Rule:MF_00018};
GN Name=yicR {ECO:0000255|HAMAP-Rule:MF_00018};
GN OrderedLocusNames=ECDH10B_3820;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
CC -!- SIMILARITY: Belongs to the UPF0758 family. YicR subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00018}.
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DR EMBL; CP000948; ACB04688.1; -; Genomic_DNA.
DR RefSeq; WP_001350561.1; NC_010473.1.
DR AlphaFoldDB; B1X972; -.
DR SMR; B1X972; -.
DR KEGG; ecd:ECDH10B_3820; -.
DR HOGENOM; CLU_073529_0_1_6; -.
DR OMA; AMPDYEL; -.
DR BioCyc; ECOL316385:ECDH10B_RS19445-MON; -.
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_1000089815"
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; 25343 MW; 1E825DEB596D742A CRC64;
MKNNSQLLMP REKMLKFGIS ALTDVELLAL FLRTGTRGKD VLTLAKEMLE NFGSLYGLLT
SEYEQFSGVH GIGVAKFAQL KGIAELARRY YNVRMREESP LLSPEMTREF LQSQLTGEER
EIFMVIFLDS QHRVITHRRL FSGTLNHVEV HPREIIREAI KINASALILA HNHPSGCAEP
SKADKLITER IIKSCQFMDL RVLDHIVIGR GEYVSFAERG WI