ID DCUS_SHIFL Reviewed; 543 AA. AC P59341; DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 22-FEB-2003, sequence version 1. DT 04-NOV-2026, entry version 157. 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=SF4098, S3632; OS Shigella flexneri. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE005674; AAN45523.1; -; Genomic_DNA. DR EMBL; AE014073; AAP18676.1; -; Genomic_DNA. DR RefSeq; WP_001216446.1; NZ_AP040250.1. DR AlphaFoldDB; P59341; -. DR BMRB; P59341; -. DR SMR; P59341; -. DR STRING; 198214.SF4098; -. DR PaxDb; 198214-SF4098; -. DR KEGG; sfl:SF4098; -. DR KEGG; sfx:S3632; -. DR PATRIC; fig|198214.7.peg.4832; -. DR HOGENOM; CLU_020211_11_2_6; -. DR OMA; AANRMHT; -. DR BRENDA; 2.7.13.3; 5712. DR Proteomes; UP000001006; Chromosome. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0004673; F:protein histidine kinase activity; ISS:UniProtKB. 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 FunFam; 1.10.287.130:FF:000011; Sensor histidine kinase DcuS; 1. DR FunFam; 3.30.450.20:FF:000018; Sensor histidine kinase DcuS; 1. DR FunFam; 3.30.450.20:FF:000045; Sensor histidine kinase DcuS; 1. DR FunFam; 3.30.565.10:FF:000041; Sensor histidine kinase DcuS; 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; IPR036890; HATPase_C_sf. DR InterPro; IPR003594; HATPase_dom. 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 NCBIfam; NF008298; dcuS; 1. 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_0000074753" 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; 60500 MW; 47705513D1206728 CRC64; MRHSLPYHIL RKRPMKLSTT VILMVSAVLF SVLLVVHLIY FSQISDMTRD GLANKALAVA RTLADSPEIR QGLQKKPQES GIQAIAEAVR KRNDLLFIVV TDMQSLRYSH PEAQRIGQPF KGDDILNALN 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 //