ID Q3KF49_PSEPF Unreviewed; 1069 AA.
AC Q3KF49;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Pfl01_1864 {ECO:0000313|EMBL:ABA73607.1};
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA73607.1, ECO:0000313|Proteomes:UP000002704};
RN [1] {ECO:0000313|EMBL:ABA73607.1, ECO:0000313|Proteomes:UP000002704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA73607.1,
RC ECO:0000313|Proteomes:UP000002704};
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA73607.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3KF49; -.
DR KEGG; pfo:Pfl01_1864; -.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_37_3_6; -.
DR Proteomes; UP000002704; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd13705; PBP2_BvgS_D1; 1.
DR CDD; cd13707; PBP2_BvgS_D2; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 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; 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 InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 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; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 2.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABA73607.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:ABA73607.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1069
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004227499"
FT DOMAIN 588..810
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 831..950
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 974..1069
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 880
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1015
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1069 AA; 118408 MW; 292A07EBDABC2FBE CRC64;
MIWPLRFVLL SILMLASTVH ATEAQRLEIV SRTRLEGVQI QLDEQDRQWL RAHPVLRIGA
SWPDYPPFEL TRKRHELEGL TADYADAIAQ ILNIDVEVWC HANRASAMAA LKAGEVDLLG
TSNNFEIADP ELMLSRAYAE DQPMWVTRLN EALPDDLAGK RIAMVDDYLP ASTIEEAYPK
ASLQRYRSIL DALGAVAFGR DDLYLGDFIS ASYLINTHFQ NDLQLAGPSG LDANPFGFAL
ARSNIRLKRL VDKALLAIPM EQRLAMELRW SAGRADIAAQ SRVSLSDSEQ QWLDQHPVVR
VGAVDDFAPL TFFDTDGRFS GLVAQLLNLI SQRSGLTFEV VRGQSLDRQV EQLRNGELDL
LPVMTPSRER ETQMLFTRSY ANSPFVLITE SKAQAPRSLE EMAGKRLALY RGNPLRDYLL
EHVPQINLIE LPSPADGTRA LFDGRADATL SSLLVARYQI DHQYRERLRI ASTLGDQPAR
IAMATAPDAP QLQSILNKAL LGIAPQEIDG LVARWSRNVV LQDSYWQRHR EQILRGFAVA
AGLLLLALGW IAFQRRQIRQ RQQWLQQLQE AKDAADEANR AKSTFLATMS HEIRTPMNAL
IGMLELALKR ADEGVTDRQA IEVASSAGQQ LLALIGDILD IARIESGHLS LAPKRANLRE
VVASVCRIFE GLARQKQLLL HVELDERSDV EVMLDPLRFK QVVSNLLSNA IKFTEAGEVS
LCLRVFGEHG GLIEVGVAIE DSGRGISAED QQRLFSPFVQ VGDHRSVAHG GSGLGLVISR
NLCRLMGGDL WMNSELNRGT QVMLRLELPV LAPRVQKEEA APAVAMTNSL AVLVVDDHPV
NRLLLCRQLS ELGHRPVDTD GGERALALWR GQSFDALITD INMQGLNGYE LTRAVRQEEA
ATGRAPCLIL GFTANAQIEE RQRCRAAGMN DCLFKPVLLR ELSQALMAAG AETQVESLDE
SAVSEFDLSA LLQLAGADNP LIEQLREEVR NSLRIDLQRL EASGLDRDVL RDLAHHVTGG
AHMIGAERVV SACRVLEQAC RDDQPAAALT AAIDSLRVAM HDLAQQLQA
//
