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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}.
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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
 
 
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