ID A0A1H3YU63_9BURK Unreviewed; 1380 AA.
AC A0A1H3YU63;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444680_101694 {ECO:0000313|EMBL:SEA15099.1};
OS Variovorax sp. YR216.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882828 {ECO:0000313|EMBL:SEA15099.1, ECO:0000313|Proteomes:UP000199122};
RN [1] {ECO:0000313|Proteomes:UP000199122}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR216 {ECO:0000313|Proteomes:UP000199122};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FNRO01000001; SEA15099.1; -; Genomic_DNA.
DR STRING; 1882828.SAMN05444680_101694; -.
DR Proteomes; UP000199122; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; 3.30.450.350; CHASE domain; 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; 3.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
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 NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 319..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..246
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 352..423
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 426..478
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 497..542
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 585..637
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 706..762
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 787..1008
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1031..1149
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 750..780
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1082
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1380 AA; 150342 MW; 761CED518313ABB6 CRC64;
MGIRESARSL VWLIVGLCGA VGAALLQLQY NESLAQERFD ALARRAVEQL DNRMHSYEVG
LRSTRGAVIA AGGEGGITRL RFAQFMASRD VEREFPGAGG FGYIRRVPAA QEAAFIAAAR
LDGKPDFHIH QLGPNDGERF VVQYFEPGDS SSPAIGLDIA SEPKRRAAAE RAMRSGQATI
TAPITLVQSE SESVRLRSVL MLLPIYRAEA QLGKLQQRQR RSSAAHGTPD DVFGWAYTPL
RIDEVLKGFD FQGGDFAMSL VDATPGGRPE RFFTSPRQLG GQETELQTMR PLQLYGRTWQ
VDIKAQPRFI NQLNLRSPWA IFAIGLVLAL LLALLSFVEE IIQRRKEREG EQRSRLAAIV
TSSNDAVIGC RLDGSITDWN AAAAKIFGYS AEEVQGQPLQ SLLLPPDYVQ EEVTLLRHIA
DGKSVAAFET FRRHRDGSPV AVSVAAAPIR AADGRVIGVA ETMRDITHEK ATKARILELN
ATLEQQVQER TAELAALSQR ERAILDGAAS AIIATDVRGV VTLFNPAAEA LLGYSAAEVV
DRMEMNSFHD AFEVHGRSMA LTTEMGRPLE AGEVFAPAPG TGRAQAREWT YVRKDGRRVP
VHLNVSPLRD AEGTVVGFIA IAADLSERKV AEHRLRSNER FMRIVTDNIP GVVAYWTPDL
RCTFANNAHE RWLGRKSAEM AGITMEELLG PVRLGENQPM IRAVLAGEDQ RVMRTREMAD
GSVVHYWLHF IPDRDDAGVV QGFITVAVDV TDMREAQAQL EQLNEALNER SAQAESASRA
KSEFLANMSH EIRSPLNTVL GVAYLLRQTE LDERQRELLK RIQTASTALL GVINDILDIS
KIEAGEMVID ETEFGVRELL EGVIEMAAVA AGNKDIALRL DADEDLPDRL RGDVTRIRQI
LVNLLSNAVK FTAKGSVRLG VHAMARDEHR VRLRLAVTDT GIGIEPELLD RLFTPFTQAD
SSTTRRFGGT GLGLSIVRQL AELMGGEIGV SSTPGVGSEF WVVLPLGLAA EDDAFPMPDD
PHPLWRLEGV RVLVVDDSPI NLDVCRHILE SEGARVSLAS DGVQAVAQLR AAPDAFDAVL
MDVHMPVLDG NEATRRIRGE LGLRDLPVIA LTASALISER DRALEAGMTD FISKPFEVEE
LIRTVRRCVE RVRGVASIPS VSAESALPRA EPPPDWPRIE GIDAADAFAR LVGDKALLLS
VLRGLLGEYT DLAASAPACG DDGTGDALRA RLHKLQGSAG VIGARDVRQA ALDGETALKA
GDRVAAGRAL QALVAALRAL EASARPWLDT AAGTQELQEA QEAPVLDPEG LALLVDALDR
QDLAAMPWFE ELAPALRATL GDERFAQLDG AVRALQFRRA VAMLREESPF NAAEAALRTP
//
