ID Q88DK1_PSEPK Unreviewed; 923 AA.
AC Q88DK1;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=PP_4824 {ECO:0000313|EMBL:AAN70393.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN70393.1, ECO:0000313|Proteomes:UP000000556};
RN [1] {ECO:0000313|EMBL:AAN70393.1, ECO:0000313|Proteomes:UP000000556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC {ECO:0000313|Proteomes:UP000000556};
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., Madupu R.,
RA Nelson W., White O., Peterson J., Khouri H., Hance I., Chris Lee P.,
RA Holtzapple E., Scanlan D., Tran K., Moazzez A., Utterback T., Rizzo M.,
RA Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D.,
RA Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N.,
RA Dusterhoft A., Tummler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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 ---------------------------------------------------------------------------
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; AE015451; AAN70393.1; -; Genomic_DNA.
DR RefSeq; NP_746929.1; NC_002947.4.
DR RefSeq; WP_010955433.1; NC_002947.4.
DR AlphaFoldDB; Q88DK1; -.
DR STRING; 160488.PP_4824; -.
DR PaxDb; 160488-PP_4824; -.
DR KEGG; ppu:PP_4824; -.
DR PATRIC; fig|160488.4.peg.5149; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_105_0_6; -.
DR OrthoDB; 9797243at2; -.
DR PhylomeDB; Q88DK1; -.
DR BioCyc; PPUT160488:G1G01-5161-MONOMER; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AAN70393.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000556};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:AAN70393.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..923
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004302000"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 404..624
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 642..764
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 791..910
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 696
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 840
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 923 AA; 101588 MW; CD9EE85ABC7433EE CRC64;
MRRLRIASAL IVSLLTLLCM FPAAAEHDGG WTVLLDEQAN LQLSDVRSER YRNQFSPLPL
ADLDAAPAGQ ALWLHYRLAP GDQEQLLRVF APDLSGLDLY ALEGEQLLRQ LHHGRQAGNA
SPTLRGSDHV LPLPNSRQPL DIYLRLVSEH QLRPAISLEP AAEAASDQRQ PLLFGMLFGG
LIMLIMHNLI RFLYTRSSTT LILALYHGLM LLSGLILLNL SGPWWHVWHS AQTPAAYLTL
VLAGLSGLYF TQHFFSPCNS PRLNRLLQGE MLIVGLSGLV LLFVDTLPLN LMTYALMALG
SVSMLLVSSY HWYKGYAPGR LFSLAMVVFN LGGLVLLPAL LGLTRTSTPW LLCILLGLTV
VSGLLLNLAV SERLRRISEE RFSASRALAA SDAEINAKAE FLAKISHEIR TPMNGVLGMT
ELLLGTPLSV KQRDYVQTIH SAGNELLTLI NEILDISKLE SRQIELDDVQ FDLNALIEDC
LNIFRAKAEQ QNIELISFTQ PQVPRVISGD PTRLRQALSS LLENALKNTD QGEILLVVAL
DQRGEVPRLR IAVQDSGEPL PAADREALLQ AELHSHHFLS SNKLGGHLGL VIAKQLIGLM
QGEFGIKSST GMGNTLWLTL PLDPSRLEQP PADLDSPLRD ARVLVVDDND TCRKVLVQQC
SAWGMNVSAV PSGKEALALL RTKAHLRDYF DAVLLDQNMP GMTGMQLAAK IKEDPSLNHD
ILVVMLTGIS NAPSKVIARN AGVKRILAKP VAGYTLKTTL AEELAQRGRE QAMPASLPGI
PQALDLPGDF RVLVAEDNSI STKVIRSMLG KLNLKPDTAC NGEEALQAMK AQHYDLVLMD
CEMPILDGFS ATQQLRAWEA ENQRQRTPVV ALTAHILAEH KERARLAGMD GHMAKPVELS
QLRELIQYWA NHREAKVDPA HTS
//
