HIGB2_VIBCH
ID HIGB2_VIBCH Reviewed; 110 AA.
AC Q9KMA6;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Toxin HigB-2;
GN Name=higB-2; OrderedLocusNames=VC_A0468;
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: Toxic component of a type II toxin-antitoxin (TA) system.
CC Inhibits translation by cleavage of mRNA.
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. Three hours of ectopic expression of higB-2
CC results in bacteriostasis without any detectable loss of viability.
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DR EMBL; AE003853; AAF96372.1; -; Genomic_DNA.
DR PIR; D82455; D82455.
DR RefSeq; NP_232860.1; NC_002506.1.
DR RefSeq; WP_000843587.1; NZ_LT906615.1.
DR PDB; 5JA8; X-ray; 2.49 A; A/C/E/G=1-110.
DR PDB; 5JA9; X-ray; 1.85 A; C/D=1-110.
DR PDB; 5JAA; X-ray; 2.99 A; C/D=2-110.
DR PDB; 5MJE; X-ray; 2.60 A; A=1-110.
DR PDBsum; 5JA8; -.
DR PDBsum; 5JA9; -.
DR PDBsum; 5JAA; -.
DR PDBsum; 5MJE; -.
DR AlphaFoldDB; Q9KMA6; -.
DR SMR; Q9KMA6; -.
DR STRING; 243277.VC_A0468; -.
DR ABCD; Q9KMA6; 3 sequenced antibodies.
DR DNASU; 2611854; -.
DR EnsemblBacteria; AAF96372; AAF96372; VC_A0468.
DR GeneID; 57741882; -.
DR GeneID; 57992135; -.
DR KEGG; vch:VC_A0468; -.
DR PATRIC; fig|243277.26.peg.3094; -.
DR eggNOG; COG4737; Bacteria.
DR HOGENOM; CLU_110687_1_2_6; -.
DR OMA; MAYPKST; -.
DR BioCyc; VCHO:VCA0468-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
DR InterPro; IPR009387; HigB-2.
DR Pfam; PF06296; RelE; 1.
DR PIRSF; PIRSF039032; HigB-2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..110
FT /note="Toxin HigB-2"
FT /id="PRO_0000278769"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:5JA9"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:5JA9"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:5JA9"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:5JA9"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5JA9"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:5JA9"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:5JA9"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:5JA9"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:5JA9"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:5JA9"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:5JA9"
SQ SEQUENCE 110 AA; 13006 MW; 0D59666D5C079066 CRC64;
MKSVFVESTI FEKYRDEYLS DEEYRLFQAE LMLNPKLGDV IQGTGGLRKI RVASKGKGKR
GGSRIIYYFL DEKRRFYLLT IYGKNEMSDL NANQRKQLMA FMEAWRNEQS