ID A0A0U3K305_9BURK Unreviewed; 1177 AA.
AC A0A0U3K305;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Hrubri_3398 {ECO:0000313|EMBL:ALU90558.1};
OS Herbaspirillum rubrisubalbicans M1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1078773 {ECO:0000313|EMBL:ALU90558.1, ECO:0000313|Proteomes:UP000069903};
RN [1] {ECO:0000313|EMBL:ALU90558.1, ECO:0000313|Proteomes:UP000069903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ALU90558.1,
RC ECO:0000313|Proteomes:UP000069903};
RA Balsanelli E., Cardoso R.L.A., Cruz L.M., Faoro H., Chubatsu L.S.,
RA Muller-Santos M., Baura V.A., Huergo L.F., Wassem R., Broughton W.,
RA Monteiro R.A., Souza E.M., Pedrosa F.O.;
RT "Herbaspirillum rubrisubalbicans M1 complete genome.";
RL Submitted (DEC-2015) 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; CP013737; ALU90558.1; -; Genomic_DNA.
DR RefSeq; WP_058897616.1; NZ_CP013737.1.
DR AlphaFoldDB; A0A0U3K305; -.
DR STRING; 1078773.Hrubri_3398; -.
DR KEGG; hrb:Hrubri_3398; -.
DR OrthoDB; 5468482at2; -.
DR Proteomes; UP000069903; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd19410; HK9-like_sensor; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ALU90558.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 500..720
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 785..898
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 907..1023
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1053..1175
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 393..476
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 834
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 956
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1108
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1177 AA; 130267 MW; 0CB079585DC6B052 CRC64;
MRVYSSQAEE RIAILKRQGK GAFSGLPLPP GPLIGFAVAI LAVLLIALFT YEASVSRGEA
ASAVSHTMKV REQLQAVVST LKDAETSQRG FLLTGTESYL SPYNQARAAL PGEIAKLREL
LADNPDQLQR LAQVERVVGD KLDELGETIS RRRNGDTVGA LAVVQSDRGK MFMDRVRVLT
RDMEEQERDL LASRQSDWRG AVAFSSAVAW GGSGLLLVLI AAAAVTTSRD YRAREKQAWI
RAGQMGLAER LQGEQRLSTL GENTLDFLTG YLNAQVGAIY LRNERGEFQR FAGYALEQVD
EPSHAAQALH LRDGQGLLGQ AAKLNRPMHV KEVPAHYLDI SSALGQHAPR ELLIVPAATD
GTVQAVFELG FLRQVRAEEE ELLARLADQI AIAVRSSKDR TRLEELLEET QRQSEELQAQ
QEELRVNNEE LEEQGQALKA SQLRLETQQA ELEETNAQLE EQTQLLELQK EDLAKTQVVL
VEKATELERA NQYKSEFLAN MSHELRTPLN STLILAKLLA DNKQGNLSDE QVRFAQTISS
AGNDLLALIN DILDLSKMEA GKLDIVSESF VVSKLAEELK ASFVVMAQQK SLGFKVEVEP
GVPLRMETDM QRLGQILKNL LSNAIKFTEK GEVSLRISLD AGGRIVFAVR DTGIGIGAEQ
HQFIFEAFRQ ADGSTHRKYG GTGLGLSISR DLAHLLGGDI EVQSRLGEGS IFTLSLPQVY
RPEQAVMRTA LPVPAAAAAT LQAAQVATAP DVRIPGPQVM PTPQKRLQDI AIDDDRDRIE
AASRLILVIE DDAAFAMILR DLAHEMGFQC VVTLSANEGV AAAEMYRPSA ILMDMNLPDF
SGLGVLDQIK RNPRTRHIPV HVVSVADYSQ EALERGAIGY ALKPVQREEL VGAIRKLEAK
FLQGLRHVLV VEDDARQLDS IRQLLAGENI NLVGVRTAAD ALARLRETTF DCMVMDLNLP
DLSGYQLLEK MAEQEHVAFP PVIVYTGRSL SAEEEQNLRR FSRSIIIKDA RSPERLLDEV
TLFLHQIETT LPPESQRLLK VARDRETVFE GRRILVVEDD VRNIFALSSV LEPKGMKVDI
ARNGREALQA LQRSQEQPGA PIDLVLMDIM MPEMDGLTAM REIRKQAIWK RLPIIALTAK
AMKDDQEKCL AAGANDYIAK PLDVEKLLSL VRVWMPK
//
