ID   Y4033_VARPS             Reviewed;         225 AA.
AC   C5CWP0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=UPF0758 protein Vapar_4033;
GN   OrderedLocusNames=Vapar_4033;
OS   Variovorax paradoxus (strain S110).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=543728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S110;
RX   PubMed=21183664; DOI=10.1128/jb.00925-10;
RA   Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA   O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA   Ovchinnikova G., Goodwin L., Han C.;
RT   "Complete genome sequence of the metabolically versatile plant growth-
RT   promoting endophyte, Variovorax paradoxus S110.";
RL   J. Bacteriol. 193:1183-1190(2011).
CC   -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR   EMBL; CP001635; ACS20647.1; -; Genomic_DNA.
DR   RefSeq; WP_015866809.1; NC_012791.1.
DR   AlphaFoldDB; C5CWP0; -.
DR   SMR; C5CWP0; -.
DR   STRING; 543728.Vapar_4033; -.
DR   EnsemblBacteria; ACS20647; ACS20647; Vapar_4033.
DR   GeneID; 45058290; -.
DR   KEGG; vap:Vapar_4033; -.
DR   eggNOG; COG2003; Bacteria.
DR   HOGENOM; CLU_073529_0_1_4; -.
DR   OMA; AMPDYEL; -.
DR   OrthoDB; 1833204at2; -.
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   InterPro; IPR037518; MPN.
DR   InterPro; IPR025657; RadC_JAB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR001405; UPF0758.
DR   InterPro; IPR020891; UPF0758_CS.
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..225
FT                   /note="UPF0758 protein Vapar_4033"
FT                   /id="PRO_1000201884"
FT   DOMAIN          103..225
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           174..187
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   225 AA;  24493 MW;  001FB73E7EBC337D CRC64;
     MAFKDLPAHA RPREKLIARG AAALADAELL ALLLRTGVAG KNVLQLAQEL LDHFGGLSGL
     LQTSAEDLKV IKGMGGDAKR AELIAVLELA RRAMAERLKE RTVFDSPGTV KQYLQLHIGS
     RPYEVFAVLF LDAQHRLIVL EELFRGTLTQ TSVYPREVVT RALHHQAAAV VLSHNHPSGS
     IEPSRADESL TQTLRAALSL IDVRVLDHVI VSAGQSYSMA EKGLL