ID F5Y3R1_RAMTT Unreviewed; 918 AA.
AC F5Y3R1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Rta_26170 {ECO:0000313|EMBL:AEG93718.1};
OS Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 /
OS TTB310).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG93718.1, ECO:0000313|Proteomes:UP000008385};
RN [1] {ECO:0000313|Proteomes:UP000008385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC {ECO:0000313|Proteomes:UP000008385};
RA Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., Py B.,
RA Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., Marechal E.,
RA Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., DuBow M.,
RA Barras F., Heulin T.;
RT "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG93718.1, ECO:0000313|Proteomes:UP000008385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC {ECO:0000313|Proteomes:UP000008385};
RX PubMed=21912644; DOI=10.1371/journal.pone.0023784;
RA De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C.,
RA Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O.,
RA Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V.,
RA Dubow M.S., Barras F., Barbe V., Weissenbach J., Mihalcescu I.,
RA Vermeglio A., Achouak W., Heulin T.;
RT "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome
RT Reveals a Well-Stocked Toolbox for Adaptation to a Desert Environment.";
RL PLoS ONE 6:E23784-E23784(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; CP000245; AEG93718.1; -; Genomic_DNA.
DR AlphaFoldDB; F5Y3R1; -.
DR STRING; 365046.Rta_26170; -.
DR KEGG; rta:Rta_26170; -.
DR PATRIC; fig|365046.3.peg.2675; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR HOGENOM; CLU_000445_114_51_4; -.
DR Proteomes; UP000008385; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AEG93718.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008385};
KW Transferase {ECO:0000313|EMBL:AEG93718.1}.
FT DOMAIN 38..84
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 105..157
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 365..417
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 562..780
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 800..916
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 849
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 918 AA; 100896 MW; B9B78BD3B2469466 CRC64;
MEGGKTSIRR QPDGGENRRP MEAPTFAFDD PRLLAGLLVE ASADVIFTKD LQGRYRYANP
ALLQAVGLQA HEVLGRTAEQ VLPDAAAARQ LMDNDRQVLA HGQPVEVEEA VPSADGGWRH
WLTRKTPLRD ERGRIIGLLA VAREITERKL AQAQRDLIRL KLEMGVQAAG LVMAEIDYRS
NQNHISAELA RLFEMGEAAM TVPRQAIFDR IHPEDRPRYL QGIARAIDPA GNGHLAIQVR
ALLPSGTVKW LDIRLQVTFA PAADGQLQPD RGMCAARDVT SEVLADAALR VSEARFRVAA
EAASDILWTN DPSGRMRGPQ PGWAAFTGQR QEEYQDYGWA RAVHPDDAQP TIAAWNAAVA
RGSKFVFQHR VRRHDGVWRT FSVRALPVQD ADGQVREWVG VHTDITDLLA AGRARSEAER
RYRQLFENMT EEVHFWRLER EPDGRIRSWR LLDANGPALA TWQRRLDDIR GLTTDEIFGA
GATGHYRPVV EQVMREQRPV SYDDFFQPLG RHFRFATVPL GSEEFMTTGA DVTAMRTAQQ
TIERQNLELR DADARKDRFL ATLSHELRNP LAPIRTAAEL LARPTLAADQ LALARQVIQR
QVGHMALLLD DLLDVARITQ GKLELRRERV ALAAIVDSAV EAVRPLIERK QHRLRIELPA
RALELEADPL RLSQVLANLL TNAAKYTDAG GCITLAAAAE GGLLRLEVRD TGIGLAPEAL
PGLFRMFSQV REASDRSEGG LGLGLALVRA LVELHGGSVA AGSAGPGQGS TFTVRVPLPA
ATGPSRPDSP ATALEQAGRK VLVADDNRDA ADTLALLLEA DGHQVRVAYD GRTAVSLARA
FQPDAALLDI GMPELNGHEV ARALRQEPWA QGLVLVAVTG WGQAEDRRIA REAGFDHHVT
KPVEPAALDR LLAPARPA
//
