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Database: UniProt
Entry: E3HW85_ACHXA
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Original site: E3HW85_ACHXA 
ID   E3HW85_ACHXA            Unreviewed;       397 AA.
AC   E3HW85;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=AXYL_04246 {ECO:0000313|EMBL:ADP17565.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP17565.1, ECO:0000313|Proteomes:UP000006876};
RN   [1] {ECO:0000313|EMBL:ADP17565.1, ECO:0000313|Proteomes:UP000006876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A8 {ECO:0000313|EMBL:ADP17565.1,
RC   ECO:0000313|Proteomes:UP000006876};
RX   PubMed=21097610; DOI=10.1128/JB.01299-10;
RA   Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT   "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT   Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(2011).
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; CP002287; ADP17565.1; -; Genomic_DNA.
DR   RefSeq; WP_013394875.1; NC_014640.1.
DR   AlphaFoldDB; E3HW85; -.
DR   STRING; 762376.AXYL_04246; -.
DR   KEGG; axy:AXYL_04246; -.
DR   PATRIC; fig|762376.5.peg.4254; -.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_51_4; -.
DR   OrthoDB; 9146564at2; -.
DR   Proteomes; UP000006876; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 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; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          23..80
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          98..150
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          170..390
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   397 AA;  42769 MW;  93852D5322B7E3F3 CRC64;
     MSLVEPPKEG TAAPFSSLAQ LDEPYRYQLL VEGVLDYAIF LLDANGFIAS WNAGAQRFKG
     YEAAEIIGQH FSRFYTDEDR AAGVPQRALA IASSEGRFEA EGWRVRKGGS RFWASVVIDP
     IRDGSGKLIG FAKVTRDITE KRHSQLELQA TQLALHRAQR MEALGRVTGG LAHDFNNFIS
     VIDGAAELLR NPELAPEKRV KYLNAIADTA QRATHLTQQM LAYARRQPLE PSQVDVGLCI
     EGMKPIFQAT LGAAVRVQYQ LPDDPCLICA DVSQLENALL NLVVNAADAM PFGGNVRIAV
     SCVDSRPDEQ GGLAAGPFVA VSVSDDGEGI APEILDHIFE PFFTTKPEGK GTGLGLSQVF
     GYVSQTGGHV DVASSAQEGT TFTLYFPKAS PGQGAAQ
//
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