ID A0A089YPL3_9PSED Unreviewed; 781 AA.
AC A0A089YPL3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LT40_09020 {ECO:0000313|EMBL:AIS17529.1};
OS Pseudomonas rhizosphaerae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS17529.1, ECO:0000313|Proteomes:UP000029499};
RN [1] {ECO:0000313|EMBL:AIS17529.1, ECO:0000313|Proteomes:UP000029499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS17529.1};
RX PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA Kwak Y., Jung B.K., Shin J.H.;
RT "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL J. Biotechnol. 193:137-138(2015).
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; CP009533; AIS17529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A089YPL3; -.
DR STRING; 216142.LT40_09020; -.
DR KEGG; prh:LT40_09020; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_6; -.
DR Proteomes; UP000029499; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
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; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
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; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000029499};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 260..331
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 336..389
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 427..647
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 668..778
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 384..418
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 718
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 781 AA; 84039 MW; 9718795FE6B63779 CRC64;
MLGNETIVIP DVRLDSRIPQ DAYALTFVRS LIMVPIGQPV AVAALGAYWS EAQPHSRDTV
ERLESLARLA TIAIENARLT QARNRAAAIG AAQNRILALA VEENTLDVTL ESVVREVEAL
STSRLLGSIV LLDEQGRQVQ HCVGPSLPAL YQDAVKAMVI DPDSSTCSAP MPHNGLMTVV
HISNDAWQEK LGNLAIEQGL QVCGSVPIRS AQGAVMGAFV LYDPELHECA PADVEILDFV
VQTIGLMVHR TRVDAAIRTS EARLRLAVDH ADVGFWDVDF VLNTLVWPPQ TKAMFGISAD
VAVTLQDFYE GLHPQDRKAT LEAFAAAMDP ERRALYEVDY RTVGREDGVV RWVAAKGRAV
FDEDGRCLRV TGTAMDITAR KTADENLREL NATLEARIAQ AVAEREEVQL ALRQSQKMEA
MGQLTGGVAH DFNNLLTPIV GTLDMLQRRG VGGEREQRLI SGAVQSADRA KTLVQRLLAF
ARRQPLQAVA VNVGKLVSDM GDLLASTTGP QIKVVVDAPE HLPAAIADVN QLEMALLNLS
VNARDAMLEG GTLRISACME SIAEGHRSRL PAGNYLCLSV ADTGTGMDPT TLARSVEPFF
STKGVGQGTG LGLSMVHGLA SQLNGALTIQ SSPGLGTNVE LWLPRSIALP AEALRLVDTP
ELSSSRGVAL LVDDEELVRA STSYMLAELG YCVIEAASGE EALELMDTGE TFDLLITDHL
MPGISGTDLA KRVRRARPGT AILLVSGYAE REGLDPDLPR LSKPFRKNEL ATSLAHLGRG
A
//
