VAPC1_HAEIN
ID VAPC1_HAEIN Reviewed; 134 AA.
AC Q57122; O05016;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=HI_0322;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system.
CC Acts as an RNase, its toxic effect is neutralized by VapB1 antitoxin
CC (By similarity). {ECO:0000250|UniProtKB:Q4QNL7}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L42023; AAC21985.1; -; Genomic_DNA.
DR PIR; G64061; G64061.
DR RefSeq; NP_438487.1; NC_000907.1.
DR RefSeq; WP_010868975.1; NC_000907.1.
DR PDB; 6NKL; X-ray; 2.20 A; A/B=1-134.
DR PDBsum; 6NKL; -.
DR AlphaFoldDB; Q57122; -.
DR SMR; Q57122; -.
DR STRING; 71421.HI_0322; -.
DR EnsemblBacteria; AAC21985; AAC21985; HI_0322.
DR KEGG; hin:HI_0322; -.
DR PATRIC; fig|71421.8.peg.339; -.
DR eggNOG; COG1487; Bacteria.
DR HOGENOM; CLU_118482_5_0_6; -.
DR OMA; IVVACEL; -.
DR PhylomeDB; Q57122; -.
DR BioCyc; HINF71421:G1GJ1-338-MON; -.
DR Proteomes; UP000000579; 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 3D-structure; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..134
FT /note="Ribonuclease VapC1"
FT /id="PRO_0000077910"
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 STRAND 2..5
FT /evidence="ECO:0007829|PDB:6NKL"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:6NKL"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:6NKL"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:6NKL"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:6NKL"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:6NKL"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:6NKL"
FT HELIX 76..91
FT /evidence="ECO:0007829|PDB:6NKL"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:6NKL"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6NKL"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:6NKL"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6NKL"
SQ SEQUENCE 134 AA; 15726 MW; 7EC5014217A854F9 CRC64;
MIYMLDTNII IYLMKNRPKI IAERVSQLLP NDRLVMSFIT YAELIKGAFG SQNYEQSIRA
IELLTERVNV LYPNEQICLH YGKWANTLKK QGRPIGNNDL WFACHALSLN AVLITHNVKE
FQRITDLQWQ DWTK