ID A0A165QPT2_9SPHN Unreviewed; 661 AA.
AC A0A165QPT2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A3736_08525 {ECO:0000313|EMBL:KZY56308.1};
OS Erythrobacter sp. HI0063.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1822240 {ECO:0000313|EMBL:KZY56308.1, ECO:0000313|Proteomes:UP000077326};
RN [1] {ECO:0000313|EMBL:KZY56308.1, ECO:0000313|Proteomes:UP000077326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI0063 {ECO:0000313|EMBL:KZY56308.1,
RC ECO:0000313|Proteomes:UP000077326};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZY56308.1}.
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DR EMBL; LWFF01000235; KZY56308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QPT2; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000077326; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 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; IPR007891; CHASE3.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KZY56308.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000077326};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 222..273
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 278..350
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 352..404
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 422..644
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 388..415
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 661 AA; 73032 MW; F5A505A78B6588D7 CRC64;
MPELRPSAAP LRFWADRPLA IKGLVFIAIP LAILFAALAS LYLSSTAEER AEADVRRAFA
IQRDTYQVHA LLSQAAAGVR GYALTGEDRF LEPYSVAERE LAPTIQRLDE AIEDPGVRNE
YATLTNLVDA KRQGLGEIVR VSRGGEDPAS SRAVLEAELS ASRDVLERLG SQVDVIQRRE
AVLLDQRRAR VDEVRSRFLL LTAISALLGL LGSIAAVYLF STGIVRRVRV LEGNAERLAK
GERLDELPDE ADEIGRLAQR LGRASALLRA REKELSESEE RFRLVVDRVR DYGIFALDTE
GRVATWNLGA ERIKGWQASE ILGRHFSSFY PPETRDFLPQ QIIDRAIHDG SAEDEGWRVR
RDGTRFWANV VITALRDGKG TLRGFAKVTR DMSERRRTEE ELRTAQDEAI AASRAKTALL
SRTSHELRTP MNAILGFGQL LEIDEENFAP HHRSAVTQIM KAGRHLLSLI NDLLDISSIE
AGVSELAIES FDLHELLAEV HSIGLPLVKQ SGLAFSLDLP EREVVVSADK RRALQVVLNL
IGNSAKYNRT GKAVRLSSRI EKHMAIVEVE DDGPGIDPPD VPRLFTAFDR LGEQNRSATE
GTGLGLALSR SLVESMKGKI GYEPASTGPG RLGARFWFSL PLAVDATTPT STLTPIEVPE
E
//
