ID   BARA_ECOL6              Reviewed;         918 AA.
AC   P0AEC6; P26607; P77032;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   02-SEP-2026, entry version 129.
DE   RecName: Full=Signal transduction histidine-protein kinase BarA;
DE            EC=2.7.13.3;
GN   Name=barA; OrderedLocusNames=c3349;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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 UvrY/BarA
CC       involved in the regulation of carbon metabolism via the CsrA/CsrB
CC       regulatory system. Phosphorylates UvrY, probably via a four-step
CC       phosphorelay (By similarity). {ECO:0000250}.
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 {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: Activation requires a sequential transfer of a phosphate group
CC       from a His in the primary transmitter domain, to an Asp in the receiver
CC       domain and to a His in the secondary transmitter domain. {ECO:0000250}.
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DR   EMBL; AE014075; AAN81797.1; -; Genomic_DNA.
DR   RefSeq; WP_000186450.1; NC_004431.1.
DR   PDB; 3IQT; X-ray; 1.40 A; A=799-918.
DR   AlphaFoldDB; P0AEC6; -.
DR   SMR; P0AEC6; -.
DR   STRING; 199310.c3349; -.
DR   DNASU; 1039190; -.
DR   GeneID; 75172870; -.
DR   GeneID; 75203823; -.
DR   KEGG; ecc:c3349; -.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG3437; Bacteria.
DR   eggNOG; COG3850; Bacteria.
DR   eggNOG; COG4999; Bacteria.
DR   HOGENOM; CLU_000445_104_1_6; -.
DR   BioCyc; ECOL199310:C3349-MONOMER; -.
DR   EvolutionaryTrace; P0AEC6; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00088; HPT; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   FunFam; 1.10.287.130:FF:000003; Histidine kinase; 1.
DR   FunFam; 1.20.120.160:FF:000002; Histidine kinase; 1.
DR   FunFam; 3.30.565.10:FF:000020; Histidine kinase; 1.
DR   FunFam; 3.40.50.2300:FF:000109; Histidine kinase; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR003594; HATPase_dom.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P_dom.
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   NCBIfam; NF008318; PRK11107.1; 1.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PDBsum; 3IQT; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..918
FT                   /note="Signal transduction histidine-protein kinase BarA"
FT                   /id="PRO_0000074699"
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"
FT   HELIX           806..808
FT                   /evidence="ECO:0007829|PDB:3IQT"
FT   HELIX           812..818
FT                   /evidence="ECO:0007829|PDB:3IQT"
FT   TURN            819..821
FT                   /evidence="ECO:0007829|PDB:3IQT"
FT   HELIX           823..848
FT                   /evidence="ECO:0007829|PDB:3IQT"
FT   HELIX           856..867
FT                   /evidence="ECO:0007829|PDB:3IQT"
FT   HELIX           873..887
FT                   /evidence="ECO:0007829|PDB:3IQT"
FT   HELIX           892..895
FT                   /evidence="ECO:0007829|PDB:3IQT"
FT   HELIX           896..916
FT                   /evidence="ECO:0007829|PDB:3IQT"
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
//