ID D9QQI9_ACEAZ Unreviewed; 399 AA.
AC D9QQI9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Acear_1265 {ECO:0000313|EMBL:ADL12780.1};
OS Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Acetohalobium.
OX NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL12780.1, ECO:0000313|Proteomes:UP000001661};
RN [1] {ECO:0000313|EMBL:ADL12780.1, ECO:0000313|Proteomes:UP000001661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC {ECO:0000313|Proteomes:UP000001661};
RX PubMed=21304692;
RA Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT 7288).";
RL Stand. Genomic Sci. 3:57-65(2010).
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; CP002105; ADL12780.1; -; Genomic_DNA.
DR RefSeq; WP_013278226.1; NC_014378.1.
DR AlphaFoldDB; D9QQI9; -.
DR STRING; 574087.Acear_1265; -.
DR KEGG; aar:Acear_1265; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_20_9; -.
DR OrthoDB; 9813394at2; -.
DR Proteomes; UP000001661; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
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 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 Pfam; PF13426; PAS_9; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADL12780.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001661};
KW Transferase {ECO:0000313|EMBL:ADL12780.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 89..139
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 149..369
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 399 AA; 46482 MW; F6CD994BADA01F12 CRC64;
MELKELLKKN FEEEGVDIEE TLTNVLDNLH DIVIYQNLER EILWANETAI EEFNEPFDEI
KERHCYELVH DSSQLCEDCL VEKAEATGEI VEREKINPNG NLYLVRVYPV KNKEKEIKGI
IRISLNITKR RALKERLEQN RLRTELFANL SHELKTPLNL MFSGMQLLKL NLEKNEDEDK
YMEYLNTIKR NTNRLLKLVE NLVDINKLDS RSYDLSFQNC DIVSLVEKVF FSVKEYAENK
KRELEFDSEI EEKVIACDSF NMERVMLNLF SNAIKFTDKG DKISMYLSDE GDNISISVKD
TGIGIPKDKQ EIIFERFGQV DKSFTRNNEG SGIGLSLVNL IIERHDGEID LHSEYGSGSE
FIIKLPAQKL AQEDAERKKI EIHDSIINKI DMEFSDIYC
//
