ID QSEC_SALTI Reviewed; 449 AA.
AC Q8Z3P2;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE RecName: Full=Sensor protein QseC;
DE EC=2.7.13.3;
GN Name=qseC; OrderedLocusNames=STY3355, t3099;
OS Salmonella typhi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Member of a two-component regulatory system QseB/QseC.
CC Activates the flagella regulon by activating transcription of FlhDC.
CC May activate QseB by phosphorylation (By 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 -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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DR EMBL; AL513382; CAD03010.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70643.1; -; Genomic_DNA.
DR RefSeq; NP_457571.1; NC_003198.1.
DR RefSeq; WP_000779337.1; NZ_WSUR01000003.1.
DR AlphaFoldDB; Q8Z3P2; -.
DR SMR; Q8Z3P2; -.
DR STRING; 220341.gene:17587213; -.
DR KEGG; stt:t3099; -.
DR KEGG; sty:STY3355; -.
DR PATRIC; fig|220341.7.peg.3415; -.
DR eggNOG; COG0642; Bacteria.
DR HOGENOM; CLU_000445_89_37_6; -.
DR OMA; WRIFWLP; -.
DR OrthoDB; 9809766at2; -.
DR BRENDA; 2.7.13.3; 5557.
DR PHI-base; PHI:6883; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.5.1040; Sensor protein qsec; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR PANTHER; PTHR45436:SF14; SENSOR PROTEIN QSEC; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..449
FT /note="Sensor protein QseC"
FT /id="PRO_0000074706"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..161
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 183..235
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 243..449
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 246
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 449 AA; 50607 MW; 611E691DE36E9F6B CRC64;
MKLTQRLSLR VRLTLIFLIL VSITWAISSF VAWRKTTDNV DELFDTQLML FARRLSTLDL
NELNAPQRMA HTPKKLKHGH IDDDALAFAI FSADGKMLLH DGDNGQDIPY RYRREGFDNG
YLKDDNDLWR FLWLNSADGK YRIVVGQEWD YREDMALAIV AAQLTPWLIA LPFMLLILLL
LLHRELRPLK KLAQALRFRS PESETPLDAK GVPSEVRPLV EALNQLFSRI HSMMVRERRF
TSDAAHELRS PLAALKVQTE VAQLSGDDPL SRDKALTQLH AGIDRATRLV DQLLTLSRLD
SLNNLQDVAE ISLEELLQSA VMDIYHPAQQ ANIDVRLQLN AHDVIRTGQP LLLSLLVRNL
LDNAIRYSPQ GSVVDVTLHA RSFTVRDNGP GVAPEILTHI GERFYRPPGQ SVTGSGLGLS
IVRRIATLHG MTVSFGNAAE GGFEAVVRW
//
