DCUS_ECO57
ID DCUS_ECO57 Reviewed; 543 AA.
AC P0AEC9; P39272; P76795;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Sensor histidine kinase DcuS;
DE EC=2.7.13.3;
GN Name=dcuS; OrderedLocusNames=Z5727, ECs5107;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Member of the two-component regulatory system DcuR/DcuS.
CC Involved in the C4-dicarboxylate-stimulated regulation of the genes
CC encoding the anaerobic fumarate respiratory system (frdABCD; nuoAN;
CC dcuB; dcuC; sdhCDAB; etc.). Weakly regulates the aerobic C4-
CC dicarboxylate transporter dctA. Activates DcuR by phosphorylation (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: The periplasmic domain is involved in C4-dicarboxylate binding
CC and sensing. The structural disorder in the cytoplasmic PAS domain has
CC an important role in signal transduction to the kinase domain and may
CC be the decisive structural feature that characterizes the activated
CC kinase (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated. The phosphoryl group is rapidly transferred to
CC DcuR (By similarity). {ECO:0000250}.
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DR EMBL; AE005174; AAG59324.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38530.1; -; Genomic_DNA.
DR PIR; C91267; C91267.
DR PIR; H86107; H86107.
DR RefSeq; NP_313134.1; NC_002695.1.
DR RefSeq; WP_001216477.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEC9; -.
DR BMRB; P0AEC9; -.
DR SMR; P0AEC9; -.
DR STRING; 155864.EDL933_5471; -.
DR EnsemblBacteria; AAG59324; AAG59324; Z5727.
DR EnsemblBacteria; BAB38530; BAB38530; ECs_5107.
DR GeneID; 914212; -.
DR KEGG; ece:Z5727; -.
DR KEGG; ecs:ECs_5107; -.
DR PATRIC; fig|386585.9.peg.5337; -.
DR eggNOG; COG3290; Bacteria.
DR HOGENOM; CLU_020211_11_2_6; -.
DR OMA; HYQNGWL; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:UniProt.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR InterPro; IPR039506; SPOB_a.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR Pfam; PF14689; SPOB_a; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF103190; SSF103190; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF55890; SSF55890; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 3: Inferred from homology;
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..543
FT /note="Sensor histidine kinase DcuS"
FT /id="PRO_0000074751"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..181
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 212..323
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 346..538
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 107..110
FT /ligand="(R)-malate"
FT /ligand_id="ChEBI:CHEBI:15588"
FT /evidence="ECO:0000250|UniProtKB:P0AEC8"
FT BINDING 121
FT /ligand="(R)-malate"
FT /ligand_id="ChEBI:CHEBI:15588"
FT /evidence="ECO:0000250|UniProtKB:P0AEC8"
FT BINDING 140..142
FT /ligand="(R)-malate"
FT /ligand_id="ChEBI:CHEBI:15588"
FT /evidence="ECO:0000250|UniProtKB:P0AEC8"
FT BINDING 147
FT /ligand="(R)-malate"
FT /ligand_id="ChEBI:CHEBI:15588"
FT /evidence="ECO:0000250|UniProtKB:P0AEC8"
FT MOD_RES 349
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 543 AA; 60551 MW; 653C369344CBA238 CRC64;
MRHSLPYRML RKRPMKLSTT VILMVSAVLF SVLLVVHLIY FSQISDMTRD GLANKALAVA
RTLADSPEIR QGLQKKPQES GIQAIAEAVR KRNDLLFIVV TDMQSLRYSH PEAQRIGQPF
KGDDILKALN GEENVAINRG FLAQALRVFT PIYDENHKQI GVVAIGLELS RVTQQINDSR
WSIIWSVLFG MLVGLIGTCI LVKVLKKILF GLEPYEISTL FEQRQAMLQS IKEGVVAVDD
RGEVTLINDA AQELLNYRKS QDDEKLSTLS HSWSQVVDVS EVLRDGTPRR DEEITIKDRL
LLINTVPVRS NGVIIGAIST FRDKTEVRKL MQRLDGLVNY ADALRERSHE FMNKLHVILG
LLHLKSYKQL EDYILKTANN YQEEIGSLLG KIKSPVIAGF LISKINRATD LGHTLILNSE
SQLPDSGSED QVATLITTLG NLIENALEAL GPEPGGEISV TLHYRHGWLH CEVNDDGPGI
APDKIDHIFD KGVSTKGSER GVGLALVKQQ VENLGGSIAV ESEPGIFTQF FVQIPWDGER
SNR