ATOS_ECOLI
ID ATOS_ECOLI Reviewed; 608 AA.
AC Q06067;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Signal transduction histidine-protein kinase AtoS {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000269|PubMed:16153782, ECO:0000269|PubMed:18534200};
GN Name=atoS; OrderedLocusNames=b2219, JW2213;
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;
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 [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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
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 [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP FUNCTION.
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 [8]
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PHOSPHORYLATION AT HIS-398, AND
RP MUTAGENESIS OF HIS-398 AND GLY-565.
RX PubMed=18534200; DOI=10.1016/j.bbagen.2008.05.002;
RA Filippou P.S., Kasemian L.D., Panagiotidis C.A., Kyriakidis D.A.;
RT "Functional characterization of the histidine kinase of the E. coli two-
RT component signal transduction system AtoS-AtoC.";
RL Biochim. Biophys. Acta 1780:1023-1031(2008).
RN [10]
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:16153782, PubMed:16564134, PubMed:17475408). Involved in the
CC regulation of motility and chemotaxis, via transcriptional induction of
CC the flagellar regulon (PubMed:22083893). AtoS is a membrane-associated
CC kinase that phosphorylates and activates AtoC in response to
CC environmental signals (PubMed:16153782, PubMed:18534200).
CC {ECO:0000269|PubMed:16153782, ECO:0000269|PubMed:16564134,
CC ECO:0000269|PubMed:17475408, ECO:0000269|PubMed:18534200,
CC ECO:0000269|PubMed:22083893}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:16153782,
CC ECO:0000269|PubMed:18534200};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18534200}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:16153782}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Autophosphorylated (PubMed:16153782, PubMed:18534200). Each AtoS
CC molecule may phosphorylate its partner within the dimer rather than
CC phosphorylating itself (PubMed:18534200). {ECO:0000269|PubMed:16153782,
CC ECO:0000269|PubMed:18534200}.
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}.
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DR EMBL; L13078; AAA23449.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75279.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16015.1; -; Genomic_DNA.
DR PIR; A64992; A64992.
DR RefSeq; NP_416723.1; NC_000913.3.
DR RefSeq; WP_000559125.1; NZ_STEB01000002.1.
DR AlphaFoldDB; Q06067; -.
DR SMR; Q06067; -.
DR BioGRID; 4262011; 20.
DR IntAct; Q06067; 2.
DR STRING; 511145.b2219; -.
DR iPTMnet; Q06067; -.
DR PaxDb; Q06067; -.
DR PRIDE; Q06067; -.
DR EnsemblBacteria; AAC75279; AAC75279; b2219.
DR EnsemblBacteria; BAA16015; BAA16015; BAA16015.
DR GeneID; 949011; -.
DR KEGG; ecj:JW2213; -.
DR KEGG; eco:b2219; -.
DR PATRIC; fig|1411691.4.peg.16; -.
DR EchoBASE; EB1618; -.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_89_29_6; -.
DR InParanoid; Q06067; -.
DR OMA; LTFWAVN; -.
DR PhylomeDB; Q06067; -.
DR BioCyc; EcoCyc:ATOS-MON; -.
DR BioCyc; MetaCyc:ATOS-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR PRO; PR:Q06067; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IMP:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; IMP:EcoCyc.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:1904583; P:response to polyamine macromolecule; IDA:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..608
FT /note="Signal transduction histidine-protein kinase AtoS"
FT /id="PRO_0000074695"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..189
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..608
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 212..262
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 260..305
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 326..382
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 395..602
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 398
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000269|PubMed:18534200"
FT MUTAGEN 398
FT /note="H->L: Lack of phosphorylation. Cannot respond to
FT acetoacetate induction."
FT /evidence="ECO:0000269|PubMed:18534200"
FT MUTAGEN 565
FT /note="G->A: Cannot bind ATP and is unable to
FT autophosphorylate."
FT /evidence="ECO:0000269|PubMed:18534200"
SQ SEQUENCE 608 AA; 67790 MW; 4669888F98985C9C CRC64;
MHYMKWIYPR RLRNQMILMA ILMVIVPTLT IGYIVETEGR SAVLSEKEKK LSAVVNLLNQ
ALGDRYDLYI DLPREERIRA LNAELAPITE NITHAFPGIG AGYYNKMLDA IITYAPSALY
QNNVGVTIAA DHPGREVMRT NTPLVYSGRQ VRGDILNSML PIERNGEILG YIWANELTED
IRRQAWKMDV RIIIVLTAGL LISLLLIVLF SRRLSANIDI ITDGLSTLAQ NIPTRLPQLP
GEMGQISQSV NNLAQALRET RTLNDLIIEN AADGVIAIDR QGDVTTMNPA AEVITGYQRH
ELVGQPYSML FDNTQFYSPV LDTLEHGTEH VALEISFPGR DRTIELSVTT SRIHNTHGEM
IGALVIFSDL TARKETQRRM AQAERLATLG ELMAGVAHEV RNPLTAIRGY VQILRQQTSD
PIHQEYLSVV LKEIDSINKV IQQLLEFSRP RHSQWQQVSL NALVEETLVL VQTAGVQARV
DFISELDNEL SPINADRELL KQVLLNILIN AVQAISARGK IRIQTWQYSD SQQAISIEDN
GCGIDLSLQK KIFDPFFTTK ASGTGLGLAL SQRIINAHQG DIRVASLPGY GATFTLILPI
NPQGNQTV
