ID   RSTB_ECOLI              Reviewed;         433 AA.
AC   P18392;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Sensor protein RstB;
DE            EC=2.7.13.3;
GN   Name=rstB; Synonyms=uspT; OrderedLocusNames=b1609, JW1601;
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;
RA   Kuempel P.L.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-433.
RX   PubMed=2646639; DOI=10.1073/pnas.86.5.1593;
RA   Hill T.M., Tecklenburg M.L., Pelletier A.J., Kuempel P.L.;
RT   "tus, the trans-acting gene required for termination of DNA replication in
RT   Escherichia coli, encodes a DNA-binding protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:1593-1597(1989).
RN   [6]
RP   SIMILARITY TO SENSORY TRANSDUCTION PROTEINS.
RX   PubMed=1925016; DOI=10.1016/0923-2508(91)90026-7;
RA   Roecklein B., Pelletier A.J., Kuempel P.L.;
RT   "The tus gene of Escherichia coli: autoregulation, analysis of flanking
RT   sequences and identification of a complementary system in Salmonella
RT   typhimurium.";
RL   Res. Microbiol. 142:169-175(1991).
RN   [7]
RP   MAPPING.
RX   PubMed=1495392; DOI=10.1111/j.1365-2958.1992.tb00890.x;
RA   Roecklein B.A., Kuempel P.L.;
RT   "In vivo characterization of tus gene expression in Escherichia coli.";
RL   Mol. Microbiol. 6:1655-1661(1992).
RN   [8]
RP   INDUCTION.
RC   STRAIN=K12;
RX   PubMed=12813061; DOI=10.1128/jb.185.13.3696-3702.2003;
RA   Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T.,
RA   Mori H., Ishihama A., Utsumi R.;
RT   "Identification and molecular characterization of the Mg2+ stimulon of
RT   Escherichia coli.";
RL   J. Bacteriol. 185:3696-3702(2003).
RN   [9]
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   [10]
RP   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).
CC   -!- FUNCTION: Member of the two-component regulatory system RstB/RstA. RstB
CC       functions as a membrane-associated protein kinase that phosphorylates
CC       RstA (Probable). {ECO:0000305|PubMed:15522865}.
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; Multi-pass membrane protein.
CC   -!- INDUCTION: Induced by low extracellular levels of magnesium via the
CC       PhoQ/PhoP two-component regulatory system.
CC       {ECO:0000269|PubMed:12813061}.
CC   -!- PTM: Autophosphorylated.
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DR   EMBL; U41101; AAA82082.1; -; Genomic_DNA.
DR   EMBL; X75466; CAA53208.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74681.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15347.1; -; Genomic_DNA.
DR   PIR; C64917; C64917.
DR   RefSeq; NP_416126.1; NC_000913.3.
DR   RefSeq; WP_000732512.1; NZ_SSZK01000001.1.
DR   AlphaFoldDB; P18392; -.
DR   SMR; P18392; -.
DR   BioGRID; 4261764; 18.
DR   DIP; DIP-10808N; -.
DR   IntAct; P18392; 3.
DR   STRING; 511145.b1609; -.
DR   jPOST; P18392; -.
DR   PaxDb; P18392; -.
DR   PRIDE; P18392; -.
DR   EnsemblBacteria; AAC74681; AAC74681; b1609.
DR   EnsemblBacteria; BAA15347; BAA15347; BAA15347.
DR   GeneID; 948870; -.
DR   KEGG; ecj:JW1601; -.
DR   KEGG; eco:b1609; -.
DR   PATRIC; fig|1411691.4.peg.653; -.
DR   EchoBASE; EB1215; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_89_27_6; -.
DR   InParanoid; P18392; -.
DR   OMA; IDNIAHE; -.
DR   PhylomeDB; P18392; -.
DR   BioCyc; EcoCyc:RSTB-MON; -.
DR   BioCyc; MetaCyc:RSTB-MON; -.
DR   BRENDA; 2.7.13.3; 2026.
DR   PRO; PR:P18392; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0018106; P:peptidyl-histidine phosphorylation; IDA:EcoCyc.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR   GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
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; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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   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..433
FT                   /note="Sensor protein RstB"
FT                   /id="PRO_0000074866"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..135
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..433
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          158..210
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          218..425
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         276
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   433 AA;  49283 MW;  62003BE4E48C7DDA CRC64;
     MKKLFIQFYL LLFVCFLVMS LLVGLVYKFT AERAGKQSLD DLMNSSLYLM RSELREIPPH
     DWGKTLKEMD LNLSFDLRVE PLSKYHLDDI SMHRLRGGEI VALDDQYTFL QRIPRSHYVL
     AVGPVPYLYY LHQMRLLDIA LIAFIAISLA FPVFIWMRPH WQDMLKLEAA AQRFGDGHLN
     ERIHFDEGSS FERLGVAFNQ MADNINALIA SKKQLIDGIA HELRTPLVRL RYRLEMSDNL
     SAAESQALNR DISQLEALIE ELLTYARLDR PQNELHLSEP DLPLWLSTHL ADIQAVTPDK
     TVRIKTLVQG HYAALDMRLM ERVLDNLLNN ALRYCHSTVE TSLLLSGNRA TLIVEDDGPG
     IAPENREHIF EPFVRLDPSR DRSTGGCGLG LAIVHSIALA MGGTVNCDTS ELGGARFSFS
     WPLWHNIPQF TSA