BARA_ECOLI
ID BARA_ECOLI Reviewed; 918 AA.
AC P0AEC5; P26607; P77032;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Signal transduction histidine-protein kinase BarA;
DE EC=2.7.13.3 {ECO:0000305|PubMed:11022030};
GN Name=barA {ECO:0000303|PubMed:1574005}; OrderedLocusNames=b2786, JW2757;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND AUTOPHOSPHORYLATION.
RC STRAIN=K12;
RX PubMed=1574005; DOI=10.1111/j.1365-2958.1992.tb01530.x;
RA Nagasawa S., Tokishita S., Aiba H., Mizuno T.;
RT "A novel sensor-regulator protein that belongs to the homologous family of
RT signal-transduction proteins involved in adaptive responses in Escherichia
RT coli.";
RL Mol. Microbiol. 6:799-807(1992).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 106-918.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11022030; DOI=10.1074/jbc.m001550200;
RA Pernestig A.-K., Melefors O., Georgellis D.;
RT "Identification of UvrY as the cognate response regulator for the BarA
RT sensor kinase in Escherichia coli.";
RL J. Biol. Chem. 276:225-231(2001).
RN [6]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12193630; DOI=10.1128/jb.184.18.5130-5140.2002;
RA Suzuki K., Wang X., Weilbacher T., Pernestig A.-K., Melefors O.,
RA Georgellis D., Babitzke P., Romeo T.;
RT "Regulatory circuitry of the CsrA/CsrB and BarA/UvrY systems of Escherichia
RT coli.";
RL J. Bacteriol. 184:5130-5140(2002).
RN [7]
RP FUNCTION.
RX PubMed=12533459; DOI=10.1128/jb.185.3.843-853.2003;
RA Pernestig A.-K., Georgellis D., Romeo T., Suzuki K., Tomenius H.,
RA Normark S., Melefors O.;
RT "The Escherichia coli BarA-UvrY two-component system is needed for
RT efficient switching between glycolytic and gluconeogenic carbon sources.";
RL J. Bacteriol. 185:843-853(2003).
RN [8]
RP SUBCELLULAR LOCATION.
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 UvrY/BarA
CC involved in the regulation of carbon metabolism via the CsrA/CsrB
CC regulatory system (PubMed:12193630, PubMed:12533459). Phosphorylates
CC UvrY, probably via a four-step phosphorelay (PubMed:11022030).
CC {ECO:0000269|PubMed:11022030, ECO:0000269|PubMed:12193630,
CC ECO:0000269|PubMed:12533459}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000305|PubMed:11022030};
CC -!- INTERACTION:
CC P0AEC5; P0ABH9: clpA; NbExp=3; IntAct=EBI-546740, EBI-546140;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Autophosphorylated (PubMed:1574005, PubMed:11022030). Activation
CC requires a sequential transfer of a phosphate group from a His in the
CC primary transmitter domain, to an Asp in the receiver domain and to a
CC His in the secondary transmitter domain (Probable).
CC {ECO:0000269|PubMed:11022030, ECO:0000269|PubMed:1574005, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene leads to hydrogen
CC peroxide hypersensitivity. {ECO:0000269|PubMed:11022030}.
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DR EMBL; D10888; BAA01710.1; -; Genomic_DNA.
DR EMBL; U29580; AAA69296.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75828.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16571.2; -; Genomic_DNA.
DR PIR; S20550; S20550.
DR RefSeq; NP_417266.1; NC_000913.3.
DR RefSeq; WP_000186450.1; NZ_SSZK01000003.1.
DR AlphaFoldDB; P0AEC5; -.
DR SMR; P0AEC5; -.
DR BioGRID; 4262286; 24.
DR BioGRID; 851585; 1.
DR DIP; DIP-47932N; -.
DR IntAct; P0AEC5; 4.
DR STRING; 511145.b2786; -.
DR iPTMnet; P0AEC5; -.
DR jPOST; P0AEC5; -.
DR PaxDb; P0AEC5; -.
DR PRIDE; P0AEC5; -.
DR EnsemblBacteria; AAC75828; AAC75828; b2786.
DR EnsemblBacteria; BAA16571; BAA16571; BAA16571.
DR GeneID; 66673347; -.
DR GeneID; 947255; -.
DR KEGG; ecj:JW2757; -.
DR KEGG; eco:b2786; -.
DR PATRIC; fig|1411691.4.peg.3949; -.
DR EchoBASE; EB1341; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR eggNOG; COG3850; Bacteria.
DR eggNOG; COG4999; Bacteria.
DR HOGENOM; CLU_000445_104_1_6; -.
DR InParanoid; P0AEC5; -.
DR OMA; NGINAMA; -.
DR PhylomeDB; P0AEC5; -.
DR BioCyc; EcoCyc:BARA-MON; -.
DR BioCyc; MetaCyc:BARA-MON; -.
DR PRO; PR:P0AEC5; -.
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:0009927; F:histidine phosphotransfer kinase activity; IDA:EcoliWiki.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:EcoCyc.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoliWiki.
DR GO; GO:0006468; P:protein phosphorylation; IDA:EcoliWiki.
DR GO; GO:0010034; P:response to acetate; IEP:EcoCyc.
DR GO; GO:1901425; P:response to formic acid; IEP:EcoCyc.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:EcoCyc.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR019247; Histidine_kinase_BarA_N.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF09984; sCache_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47226; SSF47226; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..918
FT /note="Signal transduction histidine-protein kinase BarA"
FT /id="PRO_0000074697"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..176
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..918
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 200..252
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 299..520
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 669..785
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 822..918
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT MOD_RES 302
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 718
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 861
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 918 AA; 102453 MW; EA31D6D732F023CD CRC64;
MTNYSLRARM MILILAPTVL IGLLLSIFFV VHRYNDLQRQ LEDAGASIIE PLAVSTEYGM
SLQNRESIGQ LISVLHRRHS DIVRAISVYD ENNRLFVTSN FHLDPSSMQL GSNVPFPRQL
TVTRDGDIMI LRTPIISESY SPDESPSSDA KNSQNMLGYI ALELDLKSVR LQQYKEIFIS
SVMMLFCIGI ALIFGWRLMR DVTGPIRNMV NTVDRIRRGQ LDSRVEGFML GELDMLKNGI
NSMAMSLAAY HEEMQHNIDQ ATSDLRETLE QMEIQNVELD LAKKRAQEAA RIKSEFLANM
SHELRTPLNG VIGFTRLTLK TELTPTQRDH LNTIERSANN LLAIINDVLD FSKLEAGKLI
LESIPFPLRS TLDEVVTLLA HSSHDKGLEL TLNIKSDVPD NVIGDPLRLQ QIITNLVGNA
IKFTENGNID ILVEKRALSN TKVQIEVQIR DTGIGIPERD QSRLFQAFRQ ADASISRRHG
GTGLGLVITQ KLVNEMGGDI SFHSQPNRGS TFWFHINLDL NPNIIIEGPS TQCLAGKRLA
YVEPNSAAAQ CTLDILSETP LEVVYSPTFS ALPPAHYDMM LLGIAVTFRE PLTMQHERLA
KAVSMTDFLM LALPCHAQVN AEKLKQDGIG ACLLKPLTPT RLLPALTEFC HHKQNTLLPV
TDESKLAMTV MAVDDNPANL KLIGALLEDM VQHVELCDSG HQAVERAKQM PFDLILMDIQ
MPDMDGIRAC ELIHQLPHQQ QTPVIAVTAH AMAGQKEKLL GAGMSDYLAK PIEEERLHNL
LLRYKPGSGI SSRVVTPEVN EIVVNPNATL DWQLALRQAA GKTDLARDML QMLLDFLPEV
RNKVEEQLVG ENPEGLVDLI HKLHGSCGYS GVPRMKNLCQ LIEQQLRSGT KEEDLEPELL
ELLDEMDNVA REASKILG
