ID   QSEC_SALTY              Reviewed;         449 AA.
AC   Q8ZLZ9;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Sensor protein QseC;
DE            EC=2.7.13.3;
GN   Name=qseC; OrderedLocusNames=STM3178;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL22052.1; -; Genomic_DNA.
DR   RefSeq; NP_462093.1; NC_003197.2.
DR   RefSeq; WP_000779328.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZLZ9; -.
DR   SMR; Q8ZLZ9; -.
DR   STRING; 99287.STM3178; -.
DR   PaxDb; Q8ZLZ9; -.
DR   EnsemblBacteria; AAL22052; AAL22052; STM3178.
DR   GeneID; 1254701; -.
DR   KEGG; stm:STM3178; -.
DR   PATRIC; fig|99287.12.peg.3369; -.
DR   HOGENOM; CLU_000445_89_37_6; -.
DR   OMA; DKLFDTQ; -.
DR   PhylomeDB; Q8ZLZ9; -.
DR   BioCyc; SENT99287:STM3178-MON; -.
DR   BRENDA; 2.7.13.3; 5542.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
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; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..449
FT                   /note="Sensor protein QseC"
FT                   /id="PRO_0000074707"
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;  50538 MW;  97F93CDA054F9EAD CRC64;
     MKLTQRLSLR VRLTLIFLIL VSITWAISSF VAWRKTTDNV DELFDTQLML FARRLSTLDL
     NEINAPQRMA 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 GGFEAVVSW