ID   VAPC2_HAEI8             Reviewed;         132 AA.
AC   Q4QLW0;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Ribonuclease VapC {ECO:0000255|HAMAP-Rule:MF_00265};
DE            Short=RNase VapC {ECO:0000255|HAMAP-Rule:MF_00265};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE   AltName: Full=Toxin VapC {ECO:0000255|HAMAP-Rule:MF_00265};
GN   Name=vapC {ECO:0000255|HAMAP-Rule:MF_00265, ECO:0000303|PubMed:27672196};
GN   OrderedLocusNames=NTHI1120;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT   influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
RN   [2]
RP   FUNCTION.
RC   STRAIN=86-028NP;
RX   PubMed=27672196; DOI=10.1128/jb.00529-16;
RA   Walling L.R., Butler J.S.;
RT   "Structural determinants for antitoxin identity and insulation of cross
RT   talk between homologous toxin-antitoxin systems.";
RL   J. Bacteriol. 198:3287-3295(2016).
CC   -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system
CC       (PubMed:27672196). Acts as an RNase (Probable). Its toxic effect is
CC       neutralized by cognate antitoxin VapB2 but not by non-cognate antitoxin
CC       VapB1 (PubMed:27672196). {ECO:0000255|HAMAP-Rule:MF_00265,
CC       ECO:0000269|PubMed:27672196}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00265};
CC   -!- SUBUNIT: Probably forms a complex with cognate antitoxin VapB2.
CC       {ECO:0000305|PubMed:27672196}.
CC   -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR   EMBL; CP000057; AAX87987.1; -; Genomic_DNA.
DR   RefSeq; WP_005651560.1; NC_007146.2.
DR   AlphaFoldDB; Q4QLW0; -.
DR   SMR; Q4QLW0; -.
DR   EnsemblBacteria; AAX87987; AAX87987; NTHI1120.
DR   KEGG; hit:NTHI1120; -.
DR   HOGENOM; CLU_118482_5_3_6; -.
DR   OMA; PYDLQIA; -.
DR   OrthoDB; 1968541at2; -.
DR   Proteomes; UP000002525; 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   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease; Toxin-antitoxin system.
FT   CHAIN           1..132
FT                   /note="Ribonuclease VapC"
FT                   /id="PRO_0000440071"
FT   DOMAIN          4..123
FT                   /note="PINc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT   BINDING         98
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ   SEQUENCE   132 AA;  15148 MW;  A04CBBCCE407B65A CRC64;
     MLKYMLDTNI VIYVIKRRPL EILSRFNQNA GKMCVSSITV AELYYGAEKS EYPERNIAVI
     EDFLSRLTIL DYQPKHAAHF GNIKAELSKQ GKLIGENDIH IAAHARSEGL ILVSNNLREF
     ERVIALRTEN WV