HIPB_SHEON
ID HIPB_SHEON Reviewed; 78 AA.
AC Q8EIX4;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Antitoxin HipB {ECO:0000303|PubMed:25056321};
GN Name=hipB {ECO:0000303|PubMed:25056321}; OrderedLocusNames=SO_0705;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH
RP HIPA AND DNA, FUNCTION, SUBUNIT, INDUCTION, DISRUPTION PHENOTYPE, AND
RP DNA-BINDING.
RC STRAIN=MR-1;
RX PubMed=25056321; DOI=10.1093/nar/gku665;
RA Wen Y., Behiels E., Felix J., Elegheert J., Vergauwen B., Devreese B.,
RA Savvides S.N.;
RT "The bacterial antitoxin HipB establishes a ternary complex with operator
RT DNA and phosphorylated toxin HipA to regulate bacterial persistence.";
RL Nucleic Acids Res. 42:10134-10147(2014).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Neutralizes the toxic effect of cognate toxin HipA; overexpression in
CC wild-type or a hipAB deletion temporarily inhibits cell growth. Binds
CC operator DNA; in the ternary phosphoserine-HipA-HipB-DNA complex the
CC DNA is bent about 125 degrees. {ECO:0000269|PubMed:25056321}.
CC -!- SUBUNIT: Homodimer, binds DNA. Forms a HipA(2)HipB(2)-DNA complex with
CC cognate toxin HipA; has higher affinity for the latter when HipB is
CC prebound to DNA and HipA is phosphorylated.
CC {ECO:0000269|PubMed:25056321}.
CC -!- INDUCTION: Expressed in late-exponential phase; part of the hipBA
CC operon. {ECO:0000269|PubMed:25056321}.
CC -!- DISRUPTION PHENOTYPE: Essential; a single hipB deletion cannot be made,
CC probably due to toxicity of HipA. {ECO:0000269|PubMed:25056321}.
CC -!- SIMILARITY: Belongs to the HipB antitoxin family. {ECO:0000305}.
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; AE014299; AAN53783.2; -; Genomic_DNA.
DR RefSeq; NP_716338.2; NC_004347.2.
DR RefSeq; WP_011071023.1; NZ_CP053946.1.
DR PDB; 4PU3; X-ray; 3.39 A; C/D=1-78.
DR PDB; 4PU4; X-ray; 3.79 A; C/D=1-78.
DR PDB; 4PU7; X-ray; 1.85 A; A/B=1-78.
DR PDB; 4PU8; X-ray; 2.35 A; A/B=1-78.
DR PDBsum; 4PU3; -.
DR PDBsum; 4PU4; -.
DR PDBsum; 4PU7; -.
DR PDBsum; 4PU8; -.
DR AlphaFoldDB; Q8EIX4; -.
DR SMR; Q8EIX4; -.
DR STRING; 211586.SO_0705; -.
DR PaxDb; Q8EIX4; -.
DR KEGG; son:SO_0705; -.
DR PATRIC; fig|211586.12.peg.680; -.
DR eggNOG; COG1396; Bacteria.
DR HOGENOM; CLU_066192_47_4_6; -.
DR OrthoDB; 1914633at2; -.
DR BioCyc; SONE211586:G1GMP-665-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR Pfam; PF01381; HTH_3; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor;
KW Toxin-antitoxin system; Transcription; Transcription regulation.
FT CHAIN 1..78
FT /note="Antitoxin HipB"
FT /id="PRO_0000431938"
FT DOMAIN 14..67
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257,
FT ECO:0000269|PubMed:25056321"
FT DNA_BIND 25..44
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257,
FT ECO:0000269|PubMed:25056321"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:4PU7"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:4PU7"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:4PU7"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:4PU7"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4PU7"
SQ SEQUENCE 78 AA; 8502 MW; 00823E857045945D CRC64;
MASPLNQQSL GLLIKERRKS AALTQDVAAM LCGVTKKTLI RVEKGEDVYI STVFKILDGL
GIDIVSAQTS DTETNGWY
