VAPC2_RICFE
ID VAPC2_RICFE Reviewed; 134 AA.
AC Q4UNB2;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Ribonuclease VapC2 {ECO:0000255|HAMAP-Rule:MF_00265};
DE Short=RNase VapC2 {ECO:0000255|HAMAP-Rule:MF_00265};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC2 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC2 {ECO:0000255|HAMAP-Rule:MF_00265};
GN OrderedLocusNames=RF_0095 {ECO:0000312|EMBL:AAY60946.1};
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;
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; S.CEREVISIAE OR MOUSE.
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH VAPB2 AND DNA,
RP SUBUNIT, AND MUTAGENESIS OF ASP-6.
RX PubMed=22140099; DOI=10.1093/nar/gkr1167;
RA Mate M.J., Vincentelli R., Foos N., Raoult D., Cambillau C.,
RA Ortiz-Lombardia M.;
RT "Crystal structure of the DNA-bound VapBC2 antitoxin/toxin pair from
RT Rickettsia felis.";
RL Nucleic Acids Res. 40:3245-3258(2012).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Has
CC ssRNase activity. Upon expression in E.coli or S.cerevisiae inhibits
CC growth in liquid culture; in S.cerevisiae its expression leads to
CC apoptosis-like characteristics. Rapidly induces apoptosis (within 2
CC hours) upon microinjection into mouse fibroblasts (L929 line);
CC pretreatment of cells with dexamethasone protects them. Probably
CC contributes to host cell death if bacterial cell lysis occurs during
CC host infection. Its toxic effect is neutralized by coexpression with
CC cognate antitoxin VapB2, its RNase activity is partially inhibited in
CC vitro by VapB2 (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 -!- SUBUNIT: Forms complexes with VapB2; probably VapC2(4):VapB2(2) in the
CC absence of DNA, and VapC2(4):VapB2(4) in the presence of DNA.
CC Crystallizes as heterodimers with stoichiometry VapC2(4):VapB2(4) in
CC the presence of its probable promoter DNA. The heterodimers are in
CC contact via alternative VapC-VapC and VapB-VapB interactions. This
CC subunit does not contact DNA. {ECO:0000269|PubMed:22140099}.
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR EMBL; CP000053; AAY60946.1; -; Genomic_DNA.
DR RefSeq; WP_011270449.1; NC_007109.1.
DR PDB; 3ZVK; X-ray; 2.50 A; A/B/C/D=1-134.
DR PDBsum; 3ZVK; -.
DR AlphaFoldDB; Q4UNB2; -.
DR SMR; Q4UNB2; -.
DR STRING; 315456.RF_0095; -.
DR EnsemblBacteria; AAY60946; AAY60946; RF_0095.
DR KEGG; rfe:RF_0095; -.
DR eggNOG; COG1487; Bacteria.
DR HOGENOM; CLU_118482_5_3_5; -.
DR OMA; PYDLQIA; -.
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 SMART; SM00670; PINc; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Toxin-antitoxin system.
FT CHAIN 1..134
FT /note="Ribonuclease VapC2"
FT /id="PRO_0000432237"
FT DOMAIN 3..124
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 MUTAGEN 6
FT /note="D->G: Probably inactivates toxin."
FT /evidence="ECO:0000305|PubMed:22140099"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3ZVK"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:3ZVK"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:3ZVK"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3ZVK"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:3ZVK"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:3ZVK"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:3ZVK"
FT HELIX 75..90
FT /evidence="ECO:0007829|PDB:3ZVK"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:3ZVK"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:3ZVK"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:3ZVK"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3ZVK"
SQ SEQUENCE 134 AA; 15360 MW; 1F75A781F1DD9856 CRC64;
MIYMLDTNIC VYAINKHPDS YYNNLELLAK NNTIAISSIV LAELQYGVSK SKKKEQNQSK
LDIFLSRLEI IDFSAKCTFY YGELRTELEQ KGLIIGNNDL LIASHAIAEN ATLVTNNIKE
FKRIPNLILE NWDK
