ID   VAPC1_RICFE             Reviewed;         134 AA.
AC   Q4UMB0;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Ribonuclease VapC1 {ECO:0000255|HAMAP-Rule:MF_00265};
DE            Short=RNase VapC1 {ECO:0000255|HAMAP-Rule:MF_00265};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE   AltName: Full=Toxin VapC1 {ECO:0000255|HAMAP-Rule:MF_00265};
GN   Name=vapC1 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=RF_0456;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2 {ECO:0000312|Proteomes:UP000008548};
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
RN   [2]
RP   FUNCTION, AND EXPRESSION IN E.COLI.
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
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. Upon expression in E.coli inhibits growth in liquid
CC       culture; this toxic effect is neutralized by coexpression with cognate
CC       antitoxin VapB1. Its RNase activity is partially inhibited in vitro by
CC       VapB1 (PubMed:22046301). {ECO:0000255|HAMAP-Rule:MF_00265,
CC       ECO:0000269|PubMed:22046301}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00265};
CC   -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR   EMBL; CP000053; AAY61307.1; -; Genomic_DNA.
DR   RefSeq; WP_011270789.1; NC_007109.1.
DR   AlphaFoldDB; Q4UMB0; -.
DR   SMR; Q4UMB0; -.
DR   STRING; 315456.RF_0456; -.
DR   EnsemblBacteria; AAY61307; AAY61307; RF_0456.
DR   KEGG; rfe:RF_0456; -.
DR   eggNOG; COG1487; Bacteria.
DR   HOGENOM; CLU_118482_7_0_5; -.
DR   OMA; QAYISPI; -.
DR   OrthoDB; 1968541at2; -.
DR   Proteomes; UP000008548; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR   HAMAP; MF_00265; VapC_Nob1; 1.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR002716; PIN_dom.
DR   InterPro; IPR022907; VapC_family.
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 VapC1"
FT                   /id="PRO_0000432236"
FT   DOMAIN          4..123
FT                   /note="PINc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT   BINDING         6
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ   SEQUENCE   134 AA;  15177 MW;  6D93DE5AA8BE7416 CRC64;
     MGLIIDTSII IALERGKVST KQWSHYGQAY ISPIVLTELL IGVDRVNNEN KRIKCLAFIE
     YVKSLFTILP FGIEEVYTYA RIINDLYKQR ITIGTHDMLI AATAITHGYS LLTLNVKDFK
     RIQGLEVLTV SSKD