ID B3Q996_RHOPT Unreviewed; 581 AA.
AC B3Q996;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Rpal_0360 {ECO:0000313|EMBL:ACE98920.1};
OS Rhodopseudomonas palustris (strain TIE-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=395960 {ECO:0000313|EMBL:ACE98920.1, ECO:0000313|Proteomes:UP000001725};
RN [1] {ECO:0000313|EMBL:ACE98920.1, ECO:0000313|Proteomes:UP000001725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIE-1 {ECO:0000313|EMBL:ACE98920.1,
RC ECO:0000313|Proteomes:UP000001725};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA Newman D.K., Roden E., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001096; ACE98920.1; -; Genomic_DNA.
DR RefSeq; WP_011155925.1; NC_011004.1.
DR AlphaFoldDB; B3Q996; -.
DR GeneID; 66891368; -.
DR KEGG; rpt:Rpal_0360; -.
DR HOGENOM; CLU_000445_89_6_5; -.
DR OrthoDB; 9805942at2; -.
DR Proteomes; UP000001725; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
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; 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; IPR025908; Sensor_TM1.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR025919; Stimulus_sens_dom.
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; SSF158472; HAMP domain-like; 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, ECO:0000313|EMBL:ACE98920.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 38..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 291..346
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 354..581
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 581 AA; 64625 MW; 6282521FBFB7EF2F CRC64;
MRDETPVHGR RWPRPLDWVR RTGQFFFTLS FSSLTRRILS LNLAGLMALS ASILYLSQFR
AGLIDARAQS LLVQAEIIAG AIAASATVET NTITIDPDRL LDLKPGESYG PPDEYAVLDF
PINPERVAPV LRRLISPTKT RARIYDRDGV LILDSRSLYG RGDVMRFELP PPTAEKPGIV
ERAMIAIRTW FNRGDLPLYR ELGPENGNGY QEVAQSLKGQ KSSMVRINDR GEVIVSVSVP
VQRFRAIYGS LMLSTQGDDI DQMVTAERLA ILKVFGVAAV VMFVLSVLLA STIAGPVRRL
ADAAERVRRR IRARVEIPDF TRRRDEIGHL SGALRDMTDS LYNRIEAIER FAADVSHELK
NPLTSLRSAV ETLPLAKTDN SRARLLSVIE HDVKRLDRLI SDISDASRLD AELQRQDAAQ
VDLRRLLTTL TLVANETRLG HNALVEVKFD GPAADQFPVP GHDSRLGQVI SNLLSNAQSF
SREGGKVRIL CRRRKAEIEI IVEDEGPGIR DDALEKIFER FYTDRPHQGF GQNSGLGLSI
SKQIVEAHGG KIWAENRVGP RGEDGEPTIA GARFIVRLPA T
//
