VAPC1_HAEI6
ID VAPC1_HAEI6 Reviewed; 134 AA.
AC E4QWH2;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=R2866_0251;
OS Haemophilus influenzae (strain R2866).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=262728;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R2866;
RA VanWagoner T.M., Erwin A.L., Kaul R., Mahaffey M., Zhou Y., Aggarwal G.,
RA Chang J., Deng H., Gillett W., Haugen E., Kibukawa M., Phelps K.,
RA Saenphimmachak C., Sivam D., Worthey E.A., Olson M.V., Stull T.L.,
RA Smith A.L.;
RT "Genome sequence of the invasive non-typeable isolate Haemophilus
RT influenzae R2866.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP EXPRESSION IN E.COLI, FUNCTION AS AN RNASE TOXIN, SUBUNIT, INDUCTION, AND
RP OPERON STRUCTURE.
RC STRAIN=R2866;
RX PubMed=17496075; DOI=10.1128/jb.00290-07;
RA Daines D.A., Wu M.H., Yuan S.Y.;
RT "VapC-1 of nontypeable Haemophilus influenzae is a ribonuclease.";
RL J. Bacteriol. 189:5041-5048(2007).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system.
CC Upon expression in E.coli inhibits growth in liquid culture. Its toxic
CC effect is neutralized by coexpression with antitoxin VapB1. Degrades
CC RNA but not ss- or ds-DNA in vitro, degradation is inhibited by VapB1
CC antitoxin. {ECO:0000269|PubMed:17496075}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265};
CC -!- SUBUNIT: Forms a complex with VapB1. {ECO:0000269|PubMed:17496075}.
CC -!- INDUCTION: More highly expressed in early growth phase, expression
CC decreases as cell density increases. Part of the vapB1-vapC1 operon.
CC {ECO:0000269|PubMed:17496075}.
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR EMBL; CP002277; ADO80240.1; -; Genomic_DNA.
DR RefSeq; WP_005649049.1; NC_017451.1.
DR AlphaFoldDB; E4QWH2; -.
DR SMR; E4QWH2; -.
DR GeneID; 66614920; -.
DR KEGG; hiz:R2866_0251; -.
DR PATRIC; fig|262728.6.peg.258; -.
DR HOGENOM; CLU_118482_5_0_6; -.
DR OMA; IVVACEL; -.
DR Proteomes; UP000002314; 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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Toxin-antitoxin system.
FT CHAIN 1..134
FT /note="Ribonuclease VapC1"
FT /id="PRO_0000407863"
FT DOMAIN 3..132
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 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ SEQUENCE 134 AA; 15692 MW; 77CC91D217A854F9 CRC64;
MIYMLDTNII IYLMKNRPKI IAERVSQLLP NDRLVMSFIT YAELIKGAFG SQNYEQSIRA
IELLTERVNV LYPNEQICLH YGKWANTLKK QGRPIGNNDL WIACHALSLN AVLITHNVKE
FQRITDLQWQ DWTK
