VAPC1_HAEI8
ID VAPC1_HAEI8 Reviewed; 134 AA.
AC Q4QNL7;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Ribonuclease VapC1 {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=NTHi VapC1 {ECO:0000303|PubMed:25391136};
DE AltName: Full=Toxin VapC {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC1 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=NTHI0440;
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 INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=86-028NP;
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).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF ASP-6; THR-7; SER-37; GLU-43; VAL-70; TRP-84;
RP ALA-85; GLY-92; ASP-99; TRP-101; ALA-103; CYS-104; THR-115;
RP 117-ASN--GLU-120; ASN-117; GLU-120; PHE-121 AND LEU-127.
RX PubMed=25391136; DOI=10.1371/journal.pone.0112921;
RA Hamilton B., Manzella A., Schmidt K., DiMarco V., Butler J.S.;
RT "Analysis of non-typeable Haemophilous influenzae VapC1 mutations reveals
RT structural features required for toxicity and flexibility in the active
RT site.";
RL PLoS ONE 9:E112921-E112921(2014).
RN [4]
RP FUNCTION, AND SUBUNIT.
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:25391136, PubMed:27672196). Acts as an RNase (Probable). Its
CC toxic effect is neutralized by cognate antitoxin VapB1
CC (PubMed:25391136, PubMed:27672196) but not by non-cognate antitoxin
CC VapB2 (PubMed:25391136, PubMed:27672196). {ECO:0000269|PubMed:25391136,
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: Forms a complex with VapB1 (PubMed:27672196).
CC {ECO:0000269|PubMed:27672196}.
CC -!- INDUCTION: More highly expressed in early growth phase, expression
CC decreases as cell density decreases. 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; CP000057; AAX87380.1; -; Genomic_DNA.
DR RefSeq; WP_005649049.1; NC_007146.2.
DR AlphaFoldDB; Q4QNL7; -.
DR SMR; Q4QNL7; -.
DR EnsemblBacteria; AAX87380; AAX87380; NTHI0440.
DR GeneID; 66614920; -.
DR KEGG; hit:NTHI0440; -.
DR HOGENOM; CLU_118482_5_0_6; -.
DR OMA; IVVACEL; -.
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; IDA:CACAO.
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_0000407862"
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"
FT MUTAGEN 6
FT /note="D->A: Decreased protein stability."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 7
FT /note="T->P: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 37
FT /note="S->G,N: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 43
FT /note="E->A: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 70
FT /note="V->A: Partial loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 84
FT /note="W->R: Partial loss of toxicity, still neutralized by
FT VapB1."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 85
FT /note="A->P: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 92
FT /note="G->V: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 99
FT /note="D->G: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 101
FT /note="W->C: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 103
FT /note="A->T,V: Partial loss of toxicity, still neutralized
FT by VapB1."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 104
FT /note="C->R: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 115
FT /note="T->A,I: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 117..120
FT /note="NVKE->DVKG: Nearly complete loss of toxicity, still
FT neutralized by VapB1."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 117
FT /note="N->I: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 120
FT /note="E->G: Partial loss of toxicity, still neutralized by
FT VapB1."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 121
FT /note="F->S: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
FT MUTAGEN 127
FT /note="L->H: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:25391136"
SQ SEQUENCE 134 AA; 15692 MW; 77CC91D217A854F9 CRC64;
MIYMLDTNII IYLMKNRPKI IAERVSQLLP NDRLVMSFIT YAELIKGAFG SQNYEQSIRA
IELLTERVNV LYPNEQICLH YGKWANTLKK QGRPIGNNDL WIACHALSLN AVLITHNVKE
FQRITDLQWQ DWTK
