ATOC_ECOLI
ID ATOC_ECOLI Reviewed; 461 AA.
AC Q06065;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Regulatory protein AtoC {ECO:0000305};
DE AltName: Full=Acetoacetate metabolism regulatory protein {ECO:0000305};
DE AltName: Full=DNA-binding transcriptional regulator AtoC {ECO:0000305};
DE AltName: Full=Ornithine decarboxylase antizyme {ECO:0000303|PubMed:8346225};
GN Name=atoC; Synonyms=az {ECO:0000303|PubMed:8346225};
GN OrderedLocusNames=b2220, JW2214;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Chen C., Cooke P.A., Rudd K.E., Shanley M.S.;
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-461, AND FUNCTION.
RC STRAIN=K12;
RX PubMed=8346225; DOI=10.1073/pnas.90.15.7129;
RA Canellakis E.S., Paterakis A.A., Huang S.-C., Panagiotidis C.A.,
RA Kyriakidis D.A.;
RT "Identification, cloning, and nucleotide sequencing of the ornithine
RT decarboxylase antizyme gene of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7129-7133(1993).
RN [6]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=2883171; DOI=10.1128/jb.169.5.2096-2102.1987;
RA Jenkins L.S., Nunn W.D.;
RT "Regulation of the ato operon by the atoC gene in Escherichia coli.";
RL J. Bacteriol. 169:2096-2102(1987).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT ASP-55 AND HIS-73, AND
RP MUTAGENESIS OF ASP-55 AND HIS-73.
RX PubMed=16153782; DOI=10.1016/j.bbagen.2005.06.019;
RA Lioliou E.E., Mimitou E.P., Grigoroudis A.I., Panagiotidis C.H.,
RA Panagiotidis C.A., Kyriakidis D.A.;
RT "Phosphorylation activity of the response regulator of the two-component
RT signal transduction system AtoS-AtoC in E. coli.";
RL Biochim. Biophys. Acta 1725:257-268(2005).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ASP-55 AND HIS-73.
RC STRAIN=K12;
RX PubMed=16564134; DOI=10.1016/j.bbagen.2006.01.020;
RA Theodorou M.C., Panagiotidis C.A., Panagiotidis C.H., Pantazaki A.A.,
RA Kyriakidis D.A.;
RT "Involvement of the AtoS-AtoC signal transduction system in poly-(R)-3-
RT hydroxybutyrate biosynthesis in Escherichia coli.";
RL Biochim. Biophys. Acta 1760:896-906(2006).
RN [9]
RP FUNCTION.
RX PubMed=17475408; DOI=10.1016/j.bbagen.2007.03.009;
RA Theodorou M.C., Theodorou E.C., Panagiotidis C.A., Kyriakidis D.A.;
RT "Spermidine triggering effect to the signal transduction through the AtoS-
RT AtoC/Az two-component system in Escherichia coli.";
RL Biochim. Biophys. Acta 1770:1104-1114(2007).
RN [10]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=17616594; DOI=10.1128/jb.00214-07;
RA Matta M.K., Lioliou E.E., Panagiotidis C.H., Kyriakidis D.A.,
RA Panagiotidis C.A.;
RT "Interactions of the antizyme AtoC with regulatory elements of the
RT Escherichia coli atoDAEB operon.";
RL J. Bacteriol. 189:6324-6332(2007).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22083893; DOI=10.1007/s00726-011-1140-7;
RA Theodorou M.C., Theodorou E.C., Kyriakidis D.A.;
RT "Involvement of AtoSC two-component system in Escherichia coli flagellar
RT regulon.";
RL Amino Acids 43:833-844(2012).
CC -!- FUNCTION: Member of the two-component regulatory system AtoS/AtoC. In
CC the presence of acetoacetate, AtoS/AtoC stimulates the expression of
CC the atoDAEB operon, leading to short chain fatty acid catabolism and
CC activation of the poly-(R)-3-hydroxybutyrate (cPHB) biosynthetic
CC pathway. Also induces the operon in response to spermidine
CC (PubMed:2883171, PubMed:16153782, PubMed:16564134, PubMed:17475408).
CC Involved in the regulation of motility and chemotaxis, via
CC transcriptional induction of the flagellar regulon (PubMed:22083893).
CC AtoC acts by binding directly to the promoter region of the target
CC genes (PubMed:17616594). In addition to its role as a transcriptional
CC regulator, functions as a post-translational regulator that inhibits
CC polyamine biosynthesis via regulation of ornithine decarboxylase (ODC)
CC (PubMed:8346225). {ECO:0000269|PubMed:16153782,
CC ECO:0000269|PubMed:16564134, ECO:0000269|PubMed:17475408,
CC ECO:0000269|PubMed:17616594, ECO:0000269|PubMed:22083893,
CC ECO:0000269|PubMed:2883171, ECO:0000269|PubMed:8346225}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16153782}.
CC Note=Membrane-associated in the presence of AtoS.
CC {ECO:0000269|PubMed:16153782}.
CC -!- PTM: Phosphorylated by AtoS (PubMed:16153782). Contains two
CC phosphorylation sites, which are both involved in the transduction of
CC the acetoacetate signal (PubMed:16153782). Asp-55 is probably the
CC primary phosphorylation site, but either both residues can be
CC phosphorylated independently by AtoS or the phosphate group can be
CC transferred between them (PubMed:16153782).
CC {ECO:0000269|PubMed:16153782}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000305|PubMed:8346225}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the atoSC locus renders cells not
CC motile or responsive against any chemoattractant or repellent
CC independently of the atoSC inducer's presence.
CC {ECO:0000269|PubMed:22083893}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23450.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U17902; AAA60332.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75280.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16016.1; -; Genomic_DNA.
DR EMBL; L13078; AAA23450.1; ALT_FRAME; Genomic_DNA.
DR PIR; B64992; B64992.
DR RefSeq; NP_416724.1; NC_000913.3.
DR RefSeq; WP_000125282.1; NZ_LN832404.1.
DR AlphaFoldDB; Q06065; -.
DR SMR; Q06065; -.
DR BioGRID; 4261974; 1.
DR DIP; DIP-9190N; -.
DR IntAct; Q06065; 10.
DR STRING; 511145.b2220; -.
DR iPTMnet; Q06065; -.
DR jPOST; Q06065; -.
DR PaxDb; Q06065; -.
DR PRIDE; Q06065; -.
DR EnsemblBacteria; AAC75280; AAC75280; b2220.
DR EnsemblBacteria; BAA16016; BAA16016; BAA16016.
DR GeneID; 947444; -.
DR KEGG; ecj:JW2214; -.
DR KEGG; eco:b2220; -.
DR PATRIC; fig|1411691.4.peg.15; -.
DR EchoBASE; EB1619; -.
DR eggNOG; COG2204; Bacteria.
DR HOGENOM; CLU_000445_0_5_6; -.
DR InParanoid; Q06065; -.
DR OMA; ARYIHQQ; -.
DR PhylomeDB; Q06065; -.
DR BioCyc; EcoCyc:ATOC-MON; -.
DR PRO; PR:Q06065; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; IDA:EcoCyc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0010967; P:regulation of polyamine biosynthetic process; IDA:EcoCyc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW Activator; ATP-binding; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..461
FT /note="Regulatory protein AtoC"
FT /id="PRO_0000081020"
FT DOMAIN 6..120
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 145..374
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 433..452
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 173..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 236..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 55
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:16153782"
FT MOD_RES 73
FT /note="Phosphohistidine"
FT /evidence="ECO:0000269|PubMed:16153782"
FT MUTAGEN 55
FT /note="D->G: Decreases phosphorylation. Significant
FT decrease in ability to respond to acetoacetate induction.
FT 40% decrease in cPHB accumulation. Cannot respond to
FT acetoacetate induction; when associated with L-73."
FT /evidence="ECO:0000269|PubMed:16153782,
FT ECO:0000269|PubMed:16564134"
FT MUTAGEN 73
FT /note="H->L: Decreases phosphorylation. Decrease in ability
FT to respond to acetoacetate induction. 70% decrease in cPHB
FT accumulation. Cannot respond to acetoacetate induction;
FT when associated with G-55."
FT /evidence="ECO:0000269|PubMed:16153782,
FT ECO:0000269|PubMed:16564134"
FT CONFLICT 99
FT /note="A -> R (in Ref. 5; AAA23450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 52176 MW; 478D5795790E339A CRC64;
MTAINRILIV DDEDNVRRML STAFALQGFE THCANNGRTA LHLFADIHPD VVLMDIRMPE
MDGIKALKEM RSHETRTPVI LMTAYAEVET AVEALRCGAF DYVIKPFDLD ELNLIVQRAL
QLQSMKKEIR HLHQALSTSW QWGHILTNSP AMMDICKDTA KIALSQASVL ISGESGTGKE
LIARAIHYNS RRAKGPFIKV NCAALPESLL ESELFGHEKG AFTGAQTLRQ GLFERANEGT
LLLDEIGEMP LVLQAKLLRI LQEREFERIG GHQTIKVDIR IIAATNRDLQ AMVKEGTFRE
DLFYRLNVIH LILPPLRDRR EDISLLANHF LQKFSSENQR DIIDIDPMAM SLLTAWSWPG
NIRELSNVIE RAVVMNSGPI IFSEDLPPQI RQPVCNAGEV KTAPVGERNL KEEIKRVEKR
IIMEVLEQQE GNRTRTALML GISRRALMYK LQEYGIDPAD V
