ID   Y4100_PECCP             Reviewed;         221 AA.
AC   C6DIC1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=UPF0758 protein PC1_4100 {ECO:0000255|HAMAP-Rule:MF_00018};
GN   OrderedLocusNames=PC1_4100;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the UPF0758 family. YicR subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00018}.
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DR   EMBL; CP001657; ACT15115.1; -; Genomic_DNA.
DR   RefSeq; WP_015842189.1; NC_012917.1.
DR   AlphaFoldDB; C6DIC1; -.
DR   SMR; C6DIC1; -.
DR   STRING; 561230.PC1_4100; -.
DR   EnsemblBacteria; ACT15115; ACT15115; PC1_4100.
DR   KEGG; pct:PC1_4100; -.
DR   eggNOG; COG2003; Bacteria.
DR   HOGENOM; CLU_073529_0_1_6; -.
DR   OMA; HEEFWII; -.
DR   OrthoDB; 1833204at2; -.
DR   Proteomes; UP000002736; 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 PC1_4100"
FT                   /id="PRO_1000201879"
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;  24830 MW;  689487DA104598B3 CRC64;
     MGWEKGLAPR EKLVRLGAES LTDVELLAIF LRTGLPGVHV MQLAEDLLVQ FGSLYQLMTA
     DQSAFRTAKG VGISKYTQIK AIAELSRRLF FSRLAKEDAM LNPQATGQYL QLLLSRRERE
     VFLVLFLDNQ HHVIRHQEMF VGTINSVEVH PREIVREALK ANAAALILAH NHPSGKAEPS
     QADRAITEQI VKACLLMEIR VLDHLVIGHG EYVSFAERGW I