ID   BTSS_ECOL6              Reviewed;         561 AA.
AC   P0AD15; P33357; P76434;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Sensor histidine kinase BtsS {ECO:0000250|UniProtKB:P0AD14};
DE            EC=2.7.13.3 {ECO:0000250|UniProtKB:P0AD14};
GN   Name=btsS {ECO:0000250|UniProtKB:P0AD14}; Synonyms=yehU;
GN   OrderedLocusNames=c2656;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Member of the two-component regulatory system BtsS/BtsR. BtsS
CC       is a high-affinity receptor for extracellular pyruvate that activates
CC       BtsR by phosphorylation. {ECO:0000250|UniProtKB:P0AD14}.
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:P0AD14};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0AD14}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P0AD14}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN81112.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN81112.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001295431.1; NC_004431.1.
DR   AlphaFoldDB; P0AD15; -.
DR   SMR; P0AD15; -.
DR   STRING; 199310.c2656; -.
DR   EnsemblBacteria; AAN81112; AAN81112; c2656.
DR   GeneID; 66673979; -.
DR   KEGG; ecc:c2656; -.
DR   eggNOG; COG3275; Bacteria.
DR   HOGENOM; CLU_020473_3_3_6; -.
DR   OMA; SHFFRSN; -.
DR   Proteomes; UP000001410; 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:0071555; P:cell wall organization; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF55874; SSF55874; 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..561
FT                   /note="Sensor histidine kinase BtsS"
FT                   /id="PRO_0000042843"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..43
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..108
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..140
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..170
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..561
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AD14"
FT   DOMAIN          354..559
FT                   /note="Histidine kinase"
SQ   SEQUENCE   561 AA;  62092 MW;  437B09A2010231C3 CRC64;
     MYDFNLVLLL LQQMCVFLVI AWLMSKTPLF IPLMQVTVRL PHKFLCYIVF SIFCIMGTWF
     GLHIDDSIAN TRAIGAVMGG LLGGPVVGGL VGLTGGLHRY SMGGMTALSC MISTIVEGLL
     GGLVHSILIR RGRTDKVFNP ITAGAVTFVA EMVQMLIILA IARPYEDAVR LVSNIAAPMM
     VTNTVGAALF MRILLDKRAM FEKYTSAFSA TALKVAASTE GILRQGFNEV NSMKVAQVLY
     QELDIGAVAI TDREKLLAFT GIGDDHHLPG KPISSTYTLK AIETGEVVYA DGNEVPYRCS
     LHPQCKLGST LVIPLRGENQ RVMGTIKLYE AKNRLFSSIN RTLGEGIAQL LSAQILAGQY
     ERQKAMLTQS EIKLLHAQVN PHFLFNALNT IKAVIRRDSE QASQLVQYLS TFFRKNLKRP
     SEFVTLADEI EHVNAYLQIE KARFQSRLQV NIAIPQELSQ QQLPAFTLQP IVENAIKHGT
     SQLLDTGRVA ISARREGQHL MLEIEDNAGL YQPVTNASGL GMNLVDKRLR ERFGDDYGIS
     VACEPDSYTR ITLRLPWRDE A