BTSS_ECOLI
ID BTSS_ECOLI Reviewed; 561 AA.
AC P0AD14; P33357; P76434; Q2MAV4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Sensor histidine kinase BtsS {ECO:0000305};
DE EC=2.7.13.3;
GN Name=btsS {ECO:0000303|PubMed:28469239}; Synonyms=yehU;
GN OrderedLocusNames=b2126, JW5353;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND AUTOPHOSPHORYLATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15522865; DOI=10.1074/jbc.m410104200;
RA Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., Ishihama A.;
RT "Functional characterization in vitro of all two-component signal
RT transduction systems from Escherichia coli.";
RL J. Biol. Chem. 280:1448-1456(2005).
RN [5]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-382.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22685278; DOI=10.1128/jb.00409-12;
RA Kraxenberger T., Fried L., Behr S., Jung K.;
RT "First insights into the unexplored two-component system YehU/YehT in
RT Escherichia coli.";
RL J. Bacteriol. 194:4272-4284(2012).
RN [7]
RP FUNCTION, AND INTERACTION WITH BTST AND YHJX.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24659770; DOI=10.1128/jb.01554-14;
RA Behr S., Fried L., Jung K.;
RT "Identification of a novel nutrient-sensing histidine kinase/response
RT regulator network in Escherichia coli.";
RL J. Bacteriol. 196:2023-2029(2014).
RN [8]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=28469239; DOI=10.1038/s41598-017-01410-2;
RA Behr S., Kristoficova I., Witting M., Breland E.J., Eberly A.R., Sachs C.,
RA Schmitt-Kopplin P., Hadjifrangiskou M., Jung K.;
RT "Identification of a high-affinity pyruvate receptor in Escherichia coli.";
RL Sci. Rep. 7:1388-1388(2017).
CC -!- FUNCTION: Member of the two-component regulatory system BtsS/BtsR,
CC which is part of a nutrient-sensing regulatory network composed of
CC BtsS/BtsR, the low-affinity pyruvate signaling system YpdA/YpdB and
CC their respective target proteins, BtsT and YhjX. Responds to depletion
CC of nutrients, specifically serine, and the concomitant presence of
CC extracellular pyruvate. BtsS is a high-affinity receptor for
CC extracellular pyruvate that activates BtsR by phosphorylation.
CC Activation of the BtsS/BtsR signaling cascade also suppresses
CC YpdA/YpdB-mediated yhjX induction. {ECO:0000269|PubMed:15522865,
CC ECO:0000269|PubMed:22685278, ECO:0000269|PubMed:24659770,
CC ECO:0000269|PubMed:28469239}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with BtsT and YhjX. {ECO:0000269|PubMed:24659770}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:15522865}.
CC -!- DISRUPTION PHENOTYPE: Deletion of btsSR has no obvious phenotypic
CC effect under the conditions tested. {ECO:0000269|PubMed:22685278}.
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DR EMBL; U00007; AAA60489.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75187.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76602.1; -; Genomic_DNA.
DR PIR; E64980; E64980.
DR RefSeq; NP_416630.1; NC_000913.3.
DR RefSeq; WP_001295431.1; NZ_STEB01000002.1.
DR AlphaFoldDB; P0AD14; -.
DR SMR; P0AD14; -.
DR BioGRID; 4260444; 256.
DR DIP; DIP-11909N; -.
DR STRING; 511145.b2126; -.
DR jPOST; P0AD14; -.
DR PaxDb; P0AD14; -.
DR PRIDE; P0AD14; -.
DR EnsemblBacteria; AAC75187; AAC75187; b2126.
DR EnsemblBacteria; BAE76602; BAE76602; BAE76602.
DR GeneID; 66673979; -.
DR GeneID; 949027; -.
DR KEGG; ecj:JW5353; -.
DR KEGG; eco:b2126; -.
DR PATRIC; fig|1411691.4.peg.119; -.
DR EchoBASE; EB1945; -.
DR eggNOG; COG3275; Bacteria.
DR HOGENOM; CLU_020473_3_3_6; -.
DR InParanoid; P0AD14; -.
DR OMA; SHFFRSN; -.
DR PhylomeDB; P0AD14; -.
DR BioCyc; EcoCyc:EG12007-MON; -.
DR BioCyc; MetaCyc:EG12007-MON; -.
DR PRO; PR:P0AD14; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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 GO; GO:0018106; P:peptidyl-histidine phosphorylation; IMP:EcoCyc.
DR GO; GO:0031667; P:response to nutrient levels; IDA:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IMP:EcoCyc.
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 1: Evidence at protein level;
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_0000013870"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..43
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..108
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..170
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..561
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 354..559
FT /note="Histidine kinase"
FT MUTAGEN 382
FT /note="H->Q: Lack of activity."
FT /evidence="ECO:0000269|PubMed:22685278"
FT CONFLICT 175..176
FT /note="IA -> MP (in Ref. 1; AAA60489)"
FT /evidence="ECO:0000305"
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
