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   25-MAY-2022, entry version 137.
DE   RecName: Full=Sensor protein QseC;
DE            EC=2.7.13.3;
GN   Name=qseC; OrderedLocusNames=STY3355, t3099;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; 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; 220341.16504256; -.
DR   EnsemblBacteria; AAO70643; AAO70643; t3099.
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; DKLFDTQ; -.
DR   BRENDA; 2.7.13.3; 5557.
DR   PHI-base; PHI:6883; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR013727; 2CSK_N.
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   Pfam; PF08521; 2CSK_N; 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; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 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