BARA_SHIFL
ID BARA_SHIFL Reviewed; 918 AA.
AC P59342;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2003, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Signal transduction histidine-protein kinase BarA;
DE EC=2.7.13.3;
GN Name=barA; OrderedLocusNames=SF2799, S2993;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005674; AAN44287.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18112.1; -; Genomic_DNA.
DR RefSeq; NP_708580.1; NC_004337.2.
DR RefSeq; WP_000186422.1; NZ_WPGW01000063.1.
DR AlphaFoldDB; P59342; -.
DR SMR; P59342; -.
DR STRING; 198214.SF2799; -.
DR EnsemblBacteria; AAN44287; AAN44287; SF2799.
DR EnsemblBacteria; AAP18112; AAP18112; S2993.
DR GeneID; 1026816; -.
DR KEGG; sfl:SF2799; -.
DR KEGG; sft:NCTC1_03078; -.
DR KEGG; sfx:S2993; -.
DR PATRIC; fig|198214.7.peg.3332; -.
DR HOGENOM; CLU_000445_104_1_6; -.
DR OMA; NGINAMA; -.
DR OrthoDB; 1755994at2; -.
DR BRENDA; 2.7.13.3; 5712.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 3: Inferred from homology;
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_0000074700"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..175
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..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; 102481 MW; 2E95844A64D3A842 CRC64;
MTNYSLRARM MILILAPTVL IGLLLSIFFV VHRYNDLQRQ LEDAGASIIE PLAVSTEYGM
SLQNRESIGQ LISVLHRRHS DIVRAISVYD ENNRLFVTSN FHLDPSSMQL GSNVPFPRQL
TVTRDGDIMI LRTPIISESY SPDESPSSDA KNSQNMLGYI ALELDLKSVR LQQYKEIFIS
CVMMLFCIGI 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 IQCLAGKRLA
YVEPNSAAAQ CTLDILSETP LEVVYSPTFS ALPPAHYDMM LLGIAVTFRE PLTMQHERLA
KAVSMTDFLM LALPCHAQVN AEKLKQDGIG ACLLKPLTPT RLLPALTEFC HHKQNTLLPV
TDESKLAMTV MAVDDNPANL KLIGALLEDM VQHVELCDSG HQAVERAKQM PFDLILMDIQ
MPDMDGIRAC ELIHQLPHQR QTPVIAVTAH AMAGQKEKLL GAGMSDYLAK PIEEERLHNL
LLRYKPGSGI SSRVVTPEVN EIVVNPNATL DWQLALRQAA GKTDLARDML QMLLDFLPEV
RNKVEEQLAG ENPEGLVDLI HKLHGSCGYS GVPRMKNLCQ LIEQQLRSGT KEEDLEPELL
ELLDEMDNVA REASKILG
