HIGA2_VIBCH
ID HIGA2_VIBCH Reviewed; 104 AA.
AC Q9KMA5;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Antitoxin HigA-2;
GN Name=higA-2; OrderedLocusNames=VC_A0469;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=17020579; DOI=10.1111/j.1365-2958.2006.05385.x;
RA Christensen-Dalsgaard M., Gerdes K.;
RT "Two higBA loci in the Vibrio cholerae superintegron encode mRNA cleaving
RT enzymes and can stabilize plasmids.";
RL Mol. Microbiol. 62:397-411(2006).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system
CC that counteracts the effect of the HigB-2 toxin. Binds to its own
CC promoter and regulates transcription of the higB-2/higA-2 operon.
CC {ECO:0000269|PubMed:17020579}.
CC -!- INDUCTION: Induced by amino acid starvation and the protein synthesis
CC inhibitor chloramphenicol. {ECO:0000269|PubMed:17020579}.
CC -!- MISCELLANEOUS: HigB-2/HigA-2 has been shown to stabilize plasmids very
CC efficiently in E.coli.
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DR EMBL; AE003853; AAF96373.1; -; Genomic_DNA.
DR PIR; E82455; E82455.
DR RefSeq; NP_232861.1; NC_002506.1.
DR RefSeq; WP_000071008.1; NZ_LT906615.1.
DR PDB; 5J9I; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-104.
DR PDB; 5JAA; X-ray; 2.99 A; A/B=2-104.
DR PDBsum; 5J9I; -.
DR PDBsum; 5JAA; -.
DR AlphaFoldDB; Q9KMA5; -.
DR SMR; Q9KMA5; -.
DR STRING; 243277.VC_A0469; -.
DR PRIDE; Q9KMA5; -.
DR DNASU; 2611844; -.
DR EnsemblBacteria; AAF96373; AAF96373; VC_A0469.
DR GeneID; 57741883; -.
DR GeneID; 57992134; -.
DR KEGG; vch:VC_A0469; -.
DR PATRIC; fig|243277.26.peg.3095; -.
DR eggNOG; COG2944; Bacteria.
DR HOGENOM; CLU_144725_3_1_6; -.
DR OMA; WEQGRAK; -.
DR BioCyc; VCHO:VCA0469-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd00093; HTH_XRE; 1.
DR DisProt; DP01289; -.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR032758; MqsA/HigA-2.
DR Pfam; PF15731; MqsA_antitoxin; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Toxin-antitoxin system;
KW Transcription; Transcription regulation.
FT CHAIN 1..104
FT /note="Antitoxin HigA-2"
FT /id="PRO_0000278767"
FT DOMAIN 45..98
FT /note="HTH cro/C1-type"
FT DNA_BIND 56..75
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:5JAA"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:5JAA"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:5J9I"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:5J9I"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:5J9I"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:5J9I"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:5J9I"
SQ SEQUENCE 104 AA; 11696 MW; 9E6CC9D8FBEDDFAA CRC64;
MSNRDLFAEL SSALVEAKQH SEGKLTLKTH HVNDVGELNI SPDEIVSIRE QFNMSRGVFA
RLLHTSSRTL ENWEQGRSVP NGQAVTLLKL VQRHPETLSH IAEL