ID   VAPC_RICBR              Reviewed;         134 AA.
AC   Q1RHR2;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Ribonuclease VapC {ECO:0000303|PubMed:22046301};
DE            Short=RNase VapC {ECO:0000305};
DE            EC=3.1.-.- {ECO:0000305};
DE   AltName: Full=Toxin VapC {ECO:0000303|PubMed:22046301};
GN   Name=vapC {ECO:0000305}; Synonyms=vapC1 {ECO:0000303|PubMed:22046301};
GN   OrderedLocusNames=RBE_1021;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
RN   [2]
RP   FUNCTION, AND EXPRESSION IN MOUSE.
RC   STRAIN=RML369-C;
RX   PubMed=22046301; DOI=10.1371/journal.pone.0026528;
RA   Audoly G., Vincentelli R., Edouard S., Georgiades K., Mediannikov O.,
RA   Gimenez G., Socolovschi C., Mege J.L., Cambillau C., Raoult D.;
RT   "Effect of rickettsial toxin VapC on its eukaryotic host.";
RL   PLoS ONE 6:E26528-E26528(2011).
CC   -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Has
CC       ssRNase activity. Its RNase activity is partially neutralized by
CC       cognate antitoxin VapB. Rapidly induces apoptosis upon microinjection
CC       into mouse fibroblasts (L929 line). Probably contributes to host cell
CC       death if bacterial cell lysis occurs during host infection.
CC       {ECO:0000269|PubMed:22046301}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O66399};
CC   -!- SIMILARITY: Belongs to the PINc/VapC protein family. {ECO:0000305}.
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DR   EMBL; CP000087; ABE05102.1; -; Genomic_DNA.
DR   RefSeq; WP_011477680.1; NC_007940.1.
DR   AlphaFoldDB; Q1RHR2; -.
DR   SMR; Q1RHR2; -.
DR   STRING; 336407.RBE_1021; -.
DR   EnsemblBacteria; ABE05102; ABE05102; RBE_1021.
DR   KEGG; rbe:RBE_1021; -.
DR   eggNOG; COG1487; Bacteria.
DR   HOGENOM; CLU_118482_7_0_5; -.
DR   OMA; QAYISPI; -.
DR   OrthoDB; 1968541at2; -.
DR   Proteomes; UP000001951; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR002716; PIN_dom.
DR   Pfam; PF01850; PIN; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease; Toxin-antitoxin system.
FT   CHAIN           1..134
FT                   /note="Ribonuclease VapC"
FT                   /id="PRO_0000432235"
FT   DOMAIN          4..124
FT                   /note="PINc"
FT   BINDING         6
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O66399"
SQ   SEQUENCE   134 AA;  15280 MW;  1B8D861CD6529B4E CRC64;
     MGLIVDTSII IALERGKIST KAWSNYDQAY INPIVLTELL IGIDRVKDEN KRGQCLTFIE
     YVKSLFTLLP FGIEEAYVYA KIIDNLYKER ITIGVHDLLI AATAITYNYP ILTLNTKDFK
     RIPELEVLTV PLKD