ID Q0BQN2_GRABC Unreviewed; 561 AA.
AC Q0BQN2;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 18-JUN-2025, entry version 114.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=GbCGDNIH1_1972 {ECO:0000313|EMBL:ABI62870.1};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Acetobacterales; Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI62870.1, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI62870.1, ECO:0000313|Proteomes:UP000001963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR EMBL; CP000394; ABI62870.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0BQN2; -.
DR STRING; 391165.GbCGDNIH1_1972; -.
DR KEGG; gbe:GbCGDNIH1_1972; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_6_5; -.
DR Proteomes; UP000001963; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR025908; Sensor_TM1.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR025919; Stimulus_sens_dom.
DR InterPro; IPR050428; TCS_sensor_his_kinase.
DR PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13755; Sensor_TM1; 1.
DR Pfam; PF13756; Stimulus_sens_1; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001963};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABI62870.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 24..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 275..331
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 339..561
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 561 AA; 61541 MW; 0FCB4E847500B990 CRC64;
MAGLMTHNRP PSATNRRYRL ISPLLRRILV VNVMPLVLLV AALLYLDQYQ NGLLSAEVLT
LREQARIFAG ALGEVAIDPP GKTPPHLSAG IARPLLRRLT EPTPNARARL YGPDGSLVAD
SQAMRHDPGE DIGTEPVANP HERSMLTDMV STFYDWVQTH FPHAGHSPIM NTDRDEALET
RPRWQSDTGK GQSAAFTPAD SALEMPAYIR RTADSRLLVT VAEPVQHDNH TIGIIQVTRE
AREVDASLFA IRVSILALFG LALGLTVIMS GYLARTIARP MRSLAVAAGQ MREERVRGSY
LPPALLRRGD EIGELAEALS ESAVALWARM DAIERFAADV AHEIKNPLSS INSAIETLRR
VEDPAQHKRL MSIIAQDVGR LDRLITDISD ASRVDAELSR QPTEEVDVAP ILSTLAEIHE
ATRDEEDGDP VLTVHISDQP LVVRAVETRL VQVLHNLIGN AVSFSPPDGV ITLSAGRNGP
FIQITVEDEG PGIPDSKLEH IFDRFYSERP EREQFGKHSG LGLSISRQII EALSGEINAD
NRRDAEGKII GARFSIKLPG T
//