ID A0A0Q4KWU8_9SPHN Unreviewed; 501 AA.
AC A0A0Q4KWU8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASE86_02360 {ECO:0000313|EMBL:KQN25122.1};
OS Sphingomonas sp. Leaf33.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736215 {ECO:0000313|EMBL:KQN25122.1, ECO:0000313|Proteomes:UP000051455};
RN [1] {ECO:0000313|EMBL:KQN25122.1, ECO:0000313|Proteomes:UP000051455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN25122.1,
RC ECO:0000313|Proteomes:UP000051455};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN25122.1, ECO:0000313|Proteomes:UP000051455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN25122.1,
RC ECO:0000313|Proteomes:UP000051455};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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};
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:KQN25122.1}.
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DR EMBL; LMLB01000001; KQN25122.1; -; Genomic_DNA.
DR RefSeq; WP_056421897.1; NZ_LMLB01000001.1.
DR AlphaFoldDB; A0A0Q4KWU8; -.
DR STRING; 1736215.ASE86_02360; -.
DR OrthoDB; 9808408at2; -.
DR Proteomes; UP000051455; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19410; HK9-like_sensor; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
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 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 PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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 PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KQN25122.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051455};
KW Transferase {ECO:0000313|EMBL:KQN25122.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 258..494
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 501 AA; 54833 MW; 7FCADB9665383FFC CRC64;
MGVSATIRDD DRALRRLLLW AMALGFAALL GAGIAAWSST ERTQRYAALV DHSYQVRDAI
GRFQVSLEQS ETARRGYLLT GNPLFRTLYQ DNAGRLVAEL DEIGGLTLDN PAQVDAVARV
RRLLQVVQKT REQSMALVAS GDRAFAVTLF AQDGSVTGMR AIRARLRVML AAEEALLDER
AADQRASVAT FLSVLAAAGF LVMLVAGVSF VTIFRFTRDL GASRARLQDM NDTLEDQVVE
RTTDLARANE EIQRFAYIVS HDLRSPLVNV MGFTAELEAG QKVLAELVDR AEEAAPDLVT
DEARFAARED LPEAIGFIRT STQKMDRLIN AILKLSREGR RTITPERVAM AALIGGIRDT
VQHRLDEIGG TVEVTGDLPT LVTDRLSIEQ VFANVIENAV KYRDPKRPVR IAVSGQKQGA
RAVFEITDNG RGIDPRDHAR VFDLFRRSGP QDQPGEGIGL AHVRALTYRL GGTIDVASEL
GQGATFRINL PLTIDTSGPL A
//
