YICR_ESCF3
ID YICR_ESCF3 Reviewed; 222 AA.
AC B7LVJ9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=UPF0758 protein YicR {ECO:0000255|HAMAP-Rule:MF_00018};
GN Name=yicR {ECO:0000255|HAMAP-Rule:MF_00018}; OrderedLocusNames=EFER_3929;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- SIMILARITY: Belongs to the UPF0758 family. YicR subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00018}.
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DR EMBL; CU928158; CAQ91363.1; -; Genomic_DNA.
DR RefSeq; WP_001297375.1; NC_011740.1.
DR AlphaFoldDB; B7LVJ9; -.
DR SMR; B7LVJ9; -.
DR EnsemblBacteria; CAQ91363; CAQ91363; EFER_3929.
DR GeneID; 60902671; -.
DR KEGG; efe:EFER_3929; -.
DR HOGENOM; CLU_073529_0_1_6; -.
DR OMA; AMPDYEL; -.
DR OrthoDB; 1833204at2; -.
DR BioCyc; EFER585054:EFER_RS19630-MON; -.
DR Proteomes; UP000000745; 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_1000116359"
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