CHPS_ECOLI
ID CHPS_ECOLI Reviewed; 83 AA.
AC P08365; P76803; Q2M681;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Antitoxin ChpS;
GN Name=chpS; Synonyms=chpBI, yjfB; OrderedLocusNames=b4224, JW5750;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PROBABLE OPERON STRUCTURE.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=8226627; DOI=10.1128/jb.175.21.6850-6856.1993;
RA Masuda Y., Miyakawa K., Nishimura Y., Ohtsubo E.;
RT "chpA and chpB, Escherichia coli chromosomal homologs of the pem locus
RT responsible for stable maintenance of plasmid R100.";
RL J. Bacteriol. 175:6850-6856(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3525538; DOI=10.1016/s0021-9258(18)67610-0;
RA Weiss D.L., Johnson D.I., Weith H.L., Somerville R.L.;
RT "Structural analysis of the ileR locus of Escherichia coli K12.";
RL J. Biol. Chem. 261:9966-9971(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
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 [5]
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 [6]
RP GENE MAPPING, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8083180; DOI=10.1128/jb.176.18.5861-5863.1994;
RA Masuda Y., Ohtsubo E.;
RT "Mapping and disruption of the chpB locus in Escherichia coli.";
RL J. Bacteriol. 176:5861-5863(1994).
RN [7]
RP FUNCTION, AND INTERACTION WITH CHPB.
RX PubMed=16413033; DOI=10.1016/j.jmb.2005.12.033;
RA Kamphuis M.B., Bonvin A.M., Monti M.C., Lemonnier M., Munoz-Gomez A.,
RA van den Heuvel R.H., Diaz-Orejas R., Boelens R.;
RT "Model for RNA binding and the catalytic site of the RNase Kid of the
RT bacterial parD toxin-antitoxin system.";
RL J. Mol. Biol. 357:115-126(2006).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC May be involved in the regulation of cell growth. It acts as a
CC suppressor of the endoribonuclease (inhibitory function) of ChpB
CC protein. Both ChpS and ChpB probably bind to the promoter region of the
CC chpS-chpB operon to autoregulate their synthesis.
CC {ECO:0000269|PubMed:16413033, ECO:0000269|PubMed:8226627}.
CC -!- SUBUNIT: Interacts with ChpB, inhibiting its endoribonuclease activity.
CC {ECO:0000269|PubMed:16413033}.
CC -!- INTERACTION:
CC P08365; P0A9M8: pta; NbExp=3; IntAct=EBI-556499, EBI-555015;
CC -!- INDUCTION: Part of the chpS-chpB operon. {ECO:0000269|PubMed:8226627}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:8083180}.
CC -!- SIMILARITY: Belongs to the PemI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24011.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA97121.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D16451; BAA41179.1; -; Genomic_DNA.
DR EMBL; M14018; AAA24011.1; ALT_INIT; Genomic_DNA.
DR EMBL; U14003; AAA97121.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77181.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78225.1; -; Genomic_DNA.
DR PIR; S56450; QQECR8.
DR RefSeq; NP_418645.2; NC_000913.3.
DR RefSeq; WP_001223208.1; NZ_SSZK01000013.1.
DR AlphaFoldDB; P08365; -.
DR SMR; P08365; -.
DR ComplexPortal; CPX-4063; ChpBS toxin-antitoxin complex.
DR DIP; DIP-9280N; -.
DR IntAct; P08365; 1.
DR STRING; 511145.b4224; -.
DR PaxDb; P08365; -.
DR PRIDE; P08365; -.
DR EnsemblBacteria; AAC77181; AAC77181; b4224.
DR EnsemblBacteria; BAE78225; BAE78225; BAE78225.
DR GeneID; 66671858; -.
DR GeneID; 948739; -.
DR KEGG; ecj:JW5750; -.
DR KEGG; eco:b4224; -.
DR PATRIC; fig|1411691.4.peg.2477; -.
DR EchoBASE; EB1230; -.
DR eggNOG; COG2336; Bacteria.
DR HOGENOM; CLU_150554_2_2_6; -.
DR OMA; EQMHASV; -.
DR PhylomeDB; P08365; -.
DR BioCyc; EcoCyc:EG11250-MON; -.
DR BioCyc; MetaCyc:EG11250-MON; -.
DR PRO; PR:P08365; -.
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:0030307; P:positive regulation of cell growth; IMP:EcoCyc.
DR GO; GO:0040008; P:regulation of growth; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0044010; P:single-species biofilm formation; IC:ComplexPortal.
DR InterPro; IPR007159; SpoVT-AbrB_dom.
DR InterPro; IPR037914; SpoVT-AbrB_sf.
DR Pfam; PF04014; MazE_antitoxin; 1.
DR SMART; SM00966; SpoVT_AbrB; 1.
DR SUPFAM; SSF89447; SSF89447; 1.
DR PROSITE; PS51740; SPOVT_ABRB; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Repressor; Toxin-antitoxin system;
KW Transcription; Transcription regulation.
FT CHAIN 1..83
FT /note="Antitoxin ChpS"
FT /id="PRO_0000089651"
FT DOMAIN 3..48
FT /note="SpoVT-AbrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
SQ SEQUENCE 83 AA; 9272 MW; A680B3BD47985A2D CRC64;
MRITIKRWGN SAGMVIPNIV MKELNLQPGQ SVEAQVSNNQ LILTPISRRY SLDELLAQCD
MNAAELSEQD VWGKSTPAGD EIW
