YICR_SALPC
ID YICR_SALPC Reviewed; 221 AA.
AC C0Q1X1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=UPF0758 protein YicR {ECO:0000255|HAMAP-Rule:MF_00018};
GN Name=yicR {ECO:0000255|HAMAP-Rule:MF_00018}; OrderedLocusNames=SPC_3811;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
CC -!- SIMILARITY: Belongs to the UPF0758 family. YicR subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00018}.
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DR EMBL; CP000857; ACN47887.1; -; Genomic_DNA.
DR RefSeq; WP_000380129.1; NC_012125.1.
DR AlphaFoldDB; C0Q1X1; -.
DR SMR; C0Q1X1; -.
DR EnsemblBacteria; ACN47887; ACN47887; SPC_3811.
DR KEGG; sei:SPC_3811; -.
DR HOGENOM; CLU_073529_0_1_6; -.
DR OMA; AMPDYEL; -.
DR Proteomes; UP000001599; 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..221
FT /note="UPF0758 protein YicR"
FT /id="PRO_1000195303"
FT DOMAIN 99..221
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 170..183
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 221 AA; 24890 MW; 07E83A9DD9D50444 CRC64;
MDTLDELLPR EKMLRSGIAS LSDVELLALF LRTGTPGKDV MTLAKEILQH FGSLYGLLSA
DFAQFRGVNG IGLAKFAQLK GIAELARRYY SVRMNEESAL LSPEMTREFL QSQLTGEERE
IFLVIFLDAQ HRVLQHSRLF SGTLNHVEVH PREIVREAIK LNASAVILAH NHPSGCAEPS
KADKLITERV IKCCQFMDIR VLDHLIIGRG EYVSFAERGW I