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HICB_ECOLI
ID   HICB_ECOLI              Reviewed;         138 AA.
AC   P67697; P76107; Q2MBB7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Antitoxin HicB;
GN   Name=hicB; Synonyms=ydcQ; OrderedLocusNames=b1438, JW1433;
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 / 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   [2]
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   [3]
RP   PREDICTION OF FUNCTION.
RX   PubMed=16895922; DOI=10.1093/bioinformatics/btl418;
RA   Makarova K.S., Grishin N.V., Koonin E.V.;
RT   "The HicAB cassette, a putative novel, RNA-targeting toxin-antitoxin system
RT   in archaea and bacteria.";
RL   Bioinformatics 22:2581-2584(2006).
RN   [4]
RP   SUPPRESSION OF RPOE ESSENTIALITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=17172327; DOI=10.1128/jb.01534-06;
RA   Button J.E., Silhavy T.J., Ruiz N.;
RT   "A suppressor of cell death caused by the loss of sigmaE downregulates
RT   extracytoplasmic stress responses and outer membrane vesicle production in
RT   Escherichia coli.";
RL   J. Bacteriol. 189:1523-1530(2007).
RN   [5]
RP   FUNCTION AS AN MRNA INTERFERASE ANTITOXIN, INDUCTION, AND OPERON STRUCTURE.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=19060138; DOI=10.1128/jb.01013-08;
RA   Jorgensen M.G., Pandey D.P., Jaskolska M., Gerdes K.;
RT   "HicA of Escherichia coli defines a novel family of translation-independent
RT   mRNA interferases in bacteria and archaea.";
RL   J. Bacteriol. 191:1191-1199(2009).
CC   -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC       Functions as an mRNA interferase antitoxin; overexpression prevents
CC       HicA-mediated cessation of cell growth and inhibition of cell
CC       proliferation. {ECO:0000269|PubMed:19060138}.
CC   -!- SUBUNIT: Probably forms a complex with the mRNA interferase HicA; when
CC       the 2 dissociate the mRNA interferase becomes active. {ECO:0000250}.
CC   -!- INDUCTION: Induced by amino acid starvation, carbon starvation and when
CC       translation is blocked. Induction no longer occurs in the absence of
CC       Lon protease suggesting, by homology to other toxin-antitoxin systems,
CC       that Lon may degrade the HicB antitoxin. A member of the hicA-hicB
CC       operon. {ECO:0000269|PubMed:19060138}.
CC   -!- PTM: May be degraded by Lon protease. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Disruption suppresses an rpoE disruption; in a
CC       wild-type background disruption down-regulates extracytoplasmic stress
CC       responses and outer membrane vesicle production.
CC       {ECO:0000269|PubMed:17172327}.
CC   -!- SIMILARITY: Belongs to the HicB antitoxin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE76439.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U00096; AAC74520.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76439.1; ALT_INIT; Genomic_DNA.
DR   PIR; A64896; A64896.
DR   RefSeq; NP_415955.2; NC_000913.3.
DR   RefSeq; WP_001270286.1; NZ_SSZK01000021.1.
DR   PDB; 6HPB; X-ray; 2.28 A; B/D=1-138.
DR   PDB; 6HPC; X-ray; 2.26 A; A/B=1-138.
DR   PDBsum; 6HPB; -.
DR   PDBsum; 6HPC; -.
DR   AlphaFoldDB; P67697; -.
DR   SMR; P67697; -.
DR   BioGRID; 4259496; 3.
DR   BioGRID; 850362; 1.
DR   ComplexPortal; CPX-4119; HicAB toxin-antitoxin complex.
DR   DIP; DIP-48269N; -.
DR   IntAct; P67697; 1.
DR   STRING; 511145.b1438; -.
DR   PaxDb; P67697; -.
DR   PRIDE; P67697; -.
DR   EnsemblBacteria; AAC74520; AAC74520; b1438.
DR   EnsemblBacteria; BAE76439; BAE76439; BAE76439.
DR   GeneID; 66674711; -.
DR   GeneID; 946001; -.
DR   KEGG; ecj:JW1433; -.
DR   KEGG; eco:b1438; -.
DR   PATRIC; fig|511145.12.peg.1503; -.
DR   EchoBASE; EB3523; -.
DR   eggNOG; COG1598; Bacteria.
DR   HOGENOM; CLU_140890_2_0_6; -.
DR   OMA; AFEFYFE; -.
DR   BioCyc; EcoCyc:G6749-MON; -.
DR   PRO; PR:P67697; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0110001; C:toxin-antitoxin complex; IPI:ComplexPortal.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0040008; P:regulation of growth; IC:ComplexPortal.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR   CDD; cd00093; HTH_XRE; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR031807; HicB-like.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR035069; TTHA1013/TTHA0281-like.
DR   Pfam; PF15919; HicB_lk_antitox; 1.
DR   Pfam; PF01381; HTH_3; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF143100; SSF143100; 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; Stress response;
KW   Toxin-antitoxin system; Transcription; Transcription regulation.
FT   CHAIN           1..138
FT                   /note="Antitoxin HicB"
FT                   /id="PRO_0000149757"
FT   DOMAIN          82..136
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   DNA_BIND        93..112
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   STRAND          2..9
FT                   /evidence="ECO:0007829|PDB:6HPC"
FT   STRAND          13..21
FT                   /evidence="ECO:0007829|PDB:6HPC"
FT   STRAND          26..31
FT                   /evidence="ECO:0007829|PDB:6HPC"
FT   HELIX           32..53
FT                   /evidence="ECO:0007829|PDB:6HPC"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:6HPC"
FT   HELIX           74..89
FT                   /evidence="ECO:0007829|PDB:6HPC"
FT   HELIX           93..100
FT                   /evidence="ECO:0007829|PDB:6HPC"
FT   HELIX           105..110
FT                   /evidence="ECO:0007829|PDB:6HPC"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:6HPB"
FT   HELIX           119..128
FT                   /evidence="ECO:0007829|PDB:6HPC"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:6HPC"
SQ   SEQUENCE   138 AA;  15247 MW;  C7B6C1F0D0A8BE26 CRC64;
     MRYPVTLTPA PEGGYMVSFV DIPEALTQGE TVAEAMEAAK DALLTAFDFY FEDNELIPLP
     SPLNSHDHFI EVPLSVASKV LLLNAFLQSE ITQQELARRI GKPKQEITRL FNLHHATKID
     AVQLAAKALG KELSLVMV
 
 
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