BTSS_SHIFL
ID BTSS_SHIFL Reviewed; 561 AA.
AC P0AD16; P33357; P76434;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 110.
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=SF2198, S2325;
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 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}.
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DR EMBL; AE005674; AAN43724.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP17542.1; -; Genomic_DNA.
DR RefSeq; NP_708017.2; NC_004337.2.
DR RefSeq; WP_001295431.1; NZ_WPGW01000249.1.
DR AlphaFoldDB; P0AD16; -.
DR SMR; P0AD16; -.
DR STRING; 198214.SF2198; -.
DR PRIDE; P0AD16; -.
DR EnsemblBacteria; AAN43724; AAN43724; SF2198.
DR EnsemblBacteria; AAP17542; AAP17542; S2325.
DR GeneID; 1027301; -.
DR GeneID; 66673979; -.
DR KEGG; sfl:SF2198; -.
DR KEGG; sfx:S2325; -.
DR PATRIC; fig|198214.7.peg.2626; -.
DR HOGENOM; CLU_020473_3_3_6; -.
DR OMA; SHFFRSN; -.
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: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; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..561
FT /note="Sensor histidine kinase BtsS"
FT /id="PRO_0000042844"
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
