ID A0A1P8FN64_9PROT Unreviewed; 1137 AA.
AC A0A1P8FN64;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BWI17_18650 {ECO:0000313|EMBL:APV51531.1};
OS Betaproteobacteria bacterium GR16-43.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1904640 {ECO:0000313|EMBL:APV51531.1, ECO:0000313|Proteomes:UP000185830};
RN [1] {ECO:0000313|EMBL:APV51531.1, ECO:0000313|Proteomes:UP000185830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GR16-43 {ECO:0000313|EMBL:APV51531.1,
RC ECO:0000313|Proteomes:UP000185830};
RA Choi A.;
RT "Complete genome sequence of betaproteobacterium GR16-43, isolated from a
RT freshwater pond in South Korea.";
RL Submitted (DEC-2016) 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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP019169; APV51531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8FN64; -.
DR STRING; 1904640.BWI17_18650; -.
DR KEGG; beba:BWI17_18650; -.
DR OrthoDB; 5519028at2; -.
DR Proteomes; UP000185830; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 6.10.340.10; -; 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; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR033417; CHASE8.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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 PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF17152; CHASE8; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; 3.
DR SUPFAM; SSF158472; HAMP domain-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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 190..243
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 385..603
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 748..866
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 904..996
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1014..1130
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 797
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 943
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1063
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1137 AA; 120950 MW; 5FAFD640C1E049CB CRC64;
MKAPVAAFRA RMRDASIQAK LTGIALATVF AAIVVLGLVL AAGDFLRYRQ DTEDVLRSHA
QITATNASAA VAFRDAVSAR QTLAALHVSP AIERALIFDD KGRFFAEYFR GGTWRAPPEV
ASQLEAPRVT TTGVTLDHPI EFSDDTIGFV RVEGSFRGYV DSLGRFLLAL LVAAAAALAA
ALMLVLPLRA AVARPIQGLA QLMARVRRDG DYSLRVATPA RDELGSLAES FNAMLDVIEQ
RDTHLARERD LVHTILDTMD AAVLVVDAQG TIVEANGAFL RAVDKFETDC TGEPVWEAAG
VDDAQSFLAH LAHGERFEAA LRPTRGEPRP FAWRSSRTLD AGSRSALTVV TAIDIADHKR
VEATLRRAKE AAEAASLSKS RFVANMSHEI RTPMNGILGM AHVMHAASAD DAQRHSLETI
IASGEALLRI LNDILDFSKI EAGRLDIVGA PFAVHEYVED SVQVFAAEAR GKGLALRLTF
SDDVPDSAWG DSLRLRQVLS NLIGNAIKFT QSGSIGVHVD LAPGDGELRF AVTDTGVGLS
PEAHERIFEA FTQADSTTQR EYGGTGLGLS ISRQLVTLMG GRMGMESRPG EGSTFWFAVP
LPREVSAVPP RLPARLGVHV LLADGESGDR SFERQRMLSW GASVDIVASA AEARDKLGDG
TAYHAVLLDD ALPGGWRSVV SHLEATPELA SVPVALMGMG APADPLPARV TLEIPKPVKS
STLYNFLFPQ SPMSARVTGG TGRRIEASVL LVEDNPVNID VACAMLSQAG CTVSVARDGR
EALAVLETRT FDLVLMDCQL PGMDGYTATR LLREREAGTG RHQRIVAVTA HALSGDREAC
LAAGMDDYLP KPFSPVQLQS ALEANVGSVP GAGAAAPAAA AAPEEPVQCA EAIAQLRALE
AEGHSGLIER MVGHFEKQSA ASSAALRAAL EGGSREDAAQ AVHCLRSTVA HLGGRRLAAA
CQAAELASED PAADLGAAAR RYEEEVAVFR AVLSAAGPAG ETRIEATAER PRRQALVVDD
DENDRMFLGR ALQSVGFDVL EAATIVGGLE LVSQHAFDVL MLDRHIGVES GIANAPEFRR
LSRKRPLPII LVTGLVSPRV EGDASAAGIP ALLQKPTNWG EFPARLAPVL ARLLDRA
//
