ID A0A1I5SSW8_9SPHN Unreviewed; 665 AA.
AC A0A1I5SSW8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04488241_106118 {ECO:0000313|EMBL:SFP73833.1};
OS Sphingomonas rubra.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=634430 {ECO:0000313|EMBL:SFP73833.1, ECO:0000313|Proteomes:UP000199586};
RN [1] {ECO:0000313|EMBL:SFP73833.1, ECO:0000313|Proteomes:UP000199586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9113 {ECO:0000313|EMBL:SFP73833.1,
RC ECO:0000313|Proteomes:UP000199586};
RA de Groot N.N.;
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};
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DR EMBL; FOXP01000006; SFP73833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5SSW8; -.
DR STRING; 634430.SAMN04488241_106118; -.
DR Proteomes; UP000199586; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR014265; PrsK.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR02916; PEP_his_kin; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF13492; GAF_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SFP73833.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199586};
KW Transferase {ECO:0000313|EMBL:SFP73833.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 460..659
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 665 AA; 70657 MW; 9A7C4A956AAD6C2D CRC64;
MTAMLNLWTH ALVALLFGAM ALAGLRGGGR DWPRWSFITA ALLTALWALA VAGIDAHDIA
TRLAKTARDI AWLCFAAMLI RRERAGNRAI AMLYAVTIGV VAATAVVSLA MTGPLAPATM
AAADAVRQML IALASLAALM LLCHLAQNVR HDGRWMALAL VGSWSIDLIV ATVALIAGEW
PAWLGVVRGG VMLAVGSGIA VAAQRRGAGG PTLSRTAAIR LIGVAVGGCY LALTALAADR
AGGLDPAYAR PVQIAIVLGA TVALLTLAST PWLRAWMRVK LAKHLFAHRY DYRVEWQRFA
ATLGRPTDGE PLPRRLVKAL ADLTDSPAGL LLCRDDDQLV PLAHWAWPGT GEPVADPALA
GRLAGGHIVA LDEERRAGTL PSWLRVAHDA WVMVPLIHGD LLTGAIVLAR PPIDRQLDWE
DLDLLRVAGR QAASYLAENR AQAALADAAR FEEFNRRFAF LLHDIKNVAS QLTLVARNAE
RHADNPAFRV DMIETLRDGA GRMTALLGRL GQLDMGRAES VQPVDVTALV HRLAAARRAT
GPIVVEATAA LALAAPGRLE QAIGHLVQNA AEAGGVLPVR VVVGQGEKVT IDVIDEGVGM
SAEFVRDKLF RPFASTKPIG FGIGAYEARQ LIRAMNGTLD VDSREGAGTR FRIVLPLAPA
LEAAA
//