ID H0F6E9_9BURK Unreviewed; 492 AA.
AC H0F6E9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=KYC_11713 {ECO:0000313|EMBL:EHK66121.1};
OS Achromobacter arsenitoxydans SY8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK66121.1, ECO:0000313|Proteomes:UP000003113};
RN [1] {ECO:0000313|EMBL:EHK66121.1, ECO:0000313|Proteomes:UP000003113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8 {ECO:0000313|EMBL:EHK66121.1,
RC ECO:0000313|Proteomes:UP000003113};
RX PubMed=22328747; DOI=10.1128/JB.06667-11;
RA Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.;
RT "Genome sequence of the highly efficient arsenite-oxidizing bacterium
RT Achromobacter arsenitoxydans SY8.";
RL J. Bacteriol. 194:1243-1244(2012).
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:EHK66121.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGUF01000043; EHK66121.1; -; Genomic_DNA.
DR RefSeq; WP_008162249.1; NZ_AGUF01000043.1.
DR AlphaFoldDB; H0F6E9; -.
DR STRING; 477184.KYC_11713; -.
DR PATRIC; fig|477184.5.peg.2326; -.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9804645at2; -.
DR Proteomes; UP000003113; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 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 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; 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; 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; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..492
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003532731"
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..259
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 274..490
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 492 AA; 53591 MW; 710C892F9361C149 CRC64;
MKRLTLTQRL SAVFALLLLA CCGASAWLQI AANSRYEQEV VQRLSSGLAQ HIAGSTELMD
AGGWKPDAVR SMFDMLMTVN PAVEVYLLSN DGRIVGDAAP PGQIKRDRVD LGPVKRLLAG
GMLPITGDDP RSADAQKVFS AAPVRVDGRE QGYVYVVLQG QAHDALAMDV SRSSVLRTTL
WSIALVALLG LVAGLAAFAL ITRPLRGLTR AVRAFEGDDG QALAALERPG DAAARNGDEI
AVLRRTFAQM GRRISEQWRE LTRQDQQRRD LVANISHDLR TPLTSLHGYL ETLRLKDETL
DPGERRRYLD IALAQSRKVG RLAQELFELA RLESGLVRLE PETFSLPELV QDVMQKFELA
AEARRQRLTT DFPQALPPVR ADLGLIERVL TNLLDNAIRH SPPGGRIELQ LGLASNRVQV
QVSDTGSGIP KELRAGLFTR ASALNRGPGD SGGLGLVIVQ RILQLHQSEI RLVEQAGAGA
VFQFDLAAAG QP
//
