HOKB_ECOLI
ID HOKB_ECOLI Reviewed; 49 AA.
AC P77494;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Toxic protein HokB {ECO:0000305};
GN Name=hokB {ECO:0000303|PubMed:10361310}; Synonyms=ydcB;
GN OrderedLocusNames=b4428, JW5225;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=10361310; DOI=10.1046/j.1365-2958.1999.01431.x;
RA Pedersen K., Gerdes K.;
RT "Multiple hok genes on the chromosome of Escherichia coli.";
RL Mol. Microbiol. 32:1090-1102(1999).
RN [5]
RP FUNCTION IN PERSISTENCE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113, and TOP10;
RX PubMed=26051177; DOI=10.1016/j.molcel.2015.05.011;
RA Verstraeten N., Knapen W.J., Kint C.I., Liebens V., Van den Bergh B.,
RA Dewachter L., Michiels J.E., Fu Q., David C.C., Fierro A.C., Marchal K.,
RA Beirlant J., Versees W., Hofkens J., Jansen M., Fauvart M., Michiels J.;
RT "Obg and membrane depolarization are part of a microbial bet-hedging
RT strategy that leads to antibiotic tolerance.";
RL Mol. Cell 59:9-21(2015).
CC -!- FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system
CC (Probable). When overexpressed kills cells within minutes; causes
CC collapse of the transmembrane potential and arrest of respiration
CC (PubMed:10361310). Expression leads to membrane depolarization; when
CC protein levels are high enough depolarization probably leads to lowered
CC metabolic activity which in turn induces some cells to enter the
CC persistent state in which they transiently survive antibiotic exposure.
CC Its toxic effect is probably neutralized by antisense antitoxin RNA
CC SokB, which is encoded in trans on the opposite DNA strand
CC (PubMed:10361310). {ECO:0000269|PubMed:10361310,
CC ECO:0000269|PubMed:26051177, ECO:0000305|PubMed:10361310}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0ACG4, ECO:0000305|PubMed:26051177}; Single-
CC pass membrane protein {ECO:0000250|UniProtKB:P0ACG4}.
CC -!- INDUCTION: Induced by GTPase Obg expression, which requires alarmone
CC (p)ppGpp. {ECO:0000269|PubMed:26051177}.
CC -!- DISRUPTION PHENOTYPE: Partial loss of Obg-controlled persistence.
CC {ECO:0000269|PubMed:26051177}.
CC -!- SIMILARITY: Belongs to the Hok/Gef family. {ECO:0000305}.
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DR EMBL; U00096; AAT48130.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15042.2; -; Genomic_DNA.
DR RefSeq; WP_001320773.1; NZ_SSZK01000021.1.
DR RefSeq; YP_025301.1; NC_000913.3.
DR AlphaFoldDB; P77494; -.
DR SMR; P77494; -.
DR BioGRID; 4262884; 12.
DR STRING; 511145.b4428; -.
DR TCDB; 1.E.53.1.3; the toxic hok/gef protein (hok/gef) family.
DR PaxDb; P77494; -.
DR PRIDE; P77494; -.
DR EnsemblBacteria; AAT48130; AAT48130; b4428.
DR EnsemblBacteria; BAA15042; BAA15042; BAA15042.
DR GeneID; 2847727; -.
DR GeneID; 66674729; -.
DR KEGG; ecj:JW5225; -.
DR KEGG; eco:b4428; -.
DR EchoBASE; EB1222; -.
DR eggNOG; ENOG50339QC; Bacteria.
DR HOGENOM; CLU_177638_2_1_6; -.
DR BioCyc; EcoCyc:MON0-1604; -.
DR PRO; PR:P77494; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0022611; P:dormancy process; IDA:UniProtKB.
DR InterPro; IPR000021; Hok/gef_toxin.
DR InterPro; IPR018084; Hok/gef_toxin_CS.
DR Pfam; PF01848; HOK_GEF; 1.
DR PRINTS; PR00281; HOKGEFTOXIC.
DR PROSITE; PS00556; HOK_GEF; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Toxin-antitoxin system; Transmembrane; Transmembrane helix.
FT CHAIN 1..49
FT /note="Toxic protein HokB"
FT /id="PRO_0000199030"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 49 AA; 5626 MW; 28B6363BEC11A25C CRC64;
MKHNPLVVCL LIICITILTF TLLTRQTLYE LRFRDGDKEV AALMACTSR
