ID DCUS_ECOL6 Reviewed; 543 AA.
AC P59340;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2003, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=Sensor histidine kinase DcuS {ECO:0000250|UniProtKB:P0AEC8};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:P0AEC8};
GN Name=dcuS; OrderedLocusNames=c5131;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; sdhCDAB; etc.). Weakly regulates the aerobic C4-dicarboxylate
CC transporter dctA. Activates DcuR by phosphorylation.
CC {ECO:0000250|UniProtKB:P0AEC8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P0AEC8};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0AEC8}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AEC8}; Multi-pass membrane protein
CC {ECO:0000255}.
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. {ECO:0000250|UniProtKB:P0AEC8}.
CC -!- PTM: Autophosphorylated. The phosphoryl group is rapidly transferred to
CC DcuR. {ECO:0000250|UniProtKB:P0AEC8}.
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DR EMBL; AE014075; AAN83553.1; -; Genomic_DNA.
DR RefSeq; WP_001216466.1; NZ_CP051263.1.
DR AlphaFoldDB; P59340; -.
DR BMRB; P59340; -.
DR SMR; P59340; -.
DR STRING; 199310.c5131; -.
DR KEGG; ecc:c5131; -.
DR eggNOG; COG3290; Bacteria.
DR HOGENOM; CLU_020211_11_2_6; -.
DR BioCyc; ECOL199310:C5131-MONOMER; -.
DR BRENDA; 2.7.13.3; 2026.
DR Proteomes; UP000001410; Chromosome.
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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16915; HATPase_DpiB-CitA-like; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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 PANTHER; PTHR43547:SF10; SENSOR HISTIDINE KINASE DCUS; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 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_0000074752"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AEC8"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..181
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AEC8"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AEC8"
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; 60546 MW; 201AB6FA1FF2B5CD CRC64;
MRHSLPYRML RKRPMKLSTT VILMVSAVLF SVLLVVHLIY FSQISDMTRD GLANKALAVA
RTLADSPEIR QGLQKKPQES GIQAIAEAVR KRNDLLFIVV TDMHSLRYSH PEAQRIGQPF
KGDDILKALN GEENVAINRG FLAQALRVFT PIYDENHKQI GVVAIGLELS RVTQQINDSR
WSIIWSVLFG MLVGLIGTCI LVNVLKKILF 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
//
