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   03-AUG-2022, entry version 141.
DE   RecName: Full=Sensor histidine kinase DcuS;
DE            EC=2.7.13.3;
GN   Name=dcuS; OrderedLocusNames=SF4098, S3632;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   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; 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; AE005674; AAN45523.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18676.1; -; Genomic_DNA.
DR   RefSeq; NP_709816.1; NC_004337.2.
DR   RefSeq; WP_001216446.1; NZ_WPGW01000256.1.
DR   AlphaFoldDB; P59341; -.
DR   BMRB; P59341; -.
DR   SMR; P59341; -.
DR   STRING; 198214.SF4098; -.
DR   EnsemblBacteria; AAN45523; AAN45523; SF4098.
DR   EnsemblBacteria; AAP18676; AAP18676; S3632.
DR   GeneID; 1023514; -.
DR   KEGG; sfl:SF4098; -.
DR   KEGG; sfx:S3632; -.
DR   PATRIC; fig|198214.7.peg.4832; -.
DR   HOGENOM; CLU_020211_11_2_6; -.
DR   OMA; HYQNGWL; -.
DR   OrthoDB; 1755994at2; -.
DR   BRENDA; 2.7.13.3; 5712.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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_0000074753"
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;  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