BARA_ECOL6
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 03-AUG-2022, entry version 113.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 PDBsum; 3IQT; -.
DR AlphaFoldDB; P0AEC6; -.
DR SMR; P0AEC6; -.
DR STRING; 199310.c3349; -.
DR DNASU; 1039190; -.
DR EnsemblBacteria; AAN81797; AAN81797; c3349.
DR GeneID; 66673347; -.
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 OMA; NGINAMA; -.
DR BioCyc; ECOL199310:C3349-MON; -.
DR EvolutionaryTrace; P0AEC6; -.
DR Proteomes; UP000001410; 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 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 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; 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_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
