ID   A0LS79_ACIC1            Unreviewed;       392 AA.
AC   A0LS79;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   SubName: Full=Putative signal transduction histidine kinase {ECO:0000313|EMBL:ABK52289.1};
GN   OrderedLocusNames=Acel_0516 {ECO:0000313|EMBL:ABK52289.1};
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Acidothermales;
OC   Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52289.1, ECO:0000313|Proteomes:UP000008221};
RN   [1] {ECO:0000313|EMBL:ABK52289.1, ECO:0000313|Proteomes:UP000008221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B
RC   {ECO:0000313|Proteomes:UP000008221};
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; CP000481; ABK52289.1; -; Genomic_DNA.
DR   RefSeq; WP_011719352.1; NC_008578.1.
DR   AlphaFoldDB; A0LS79; -.
DR   FunCoup; A0LS79; 27.
DR   STRING; 351607.Acel_0516; -.
DR   KEGG; ace:Acel_0516; -.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG4585; Bacteria.
DR   HOGENOM; CLU_000445_20_13_11; -.
DR   InParanoid; A0LS79; -.
DR   Proteomes; UP000008221; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0070025; F:carbon monoxide binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0070026; F:nitric oxide binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0019825; F:oxygen binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0019826; F:oxygen sensor activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0070483; P:detection of hypoxia; IEA:UniProtKB-ARBA.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   FunFam; 3.30.450.40:FF:000052; Oxygen sensor histidine kinase response regulator DevS/DosS; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR003594; HATPase_dom.
DR   InterPro; IPR050482; Sensor_HK_TwoCompSys.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF56; OXYGEN SENSOR HISTIDINE KINASE RESPONSE REGULATOR DOST; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABK52289.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008221};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          27..175
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
SQ   SEQUENCE   392 AA;  41585 MW;  A79A48CA72E5A264 CRC64;
     MPHRAIRDPE QLHALLDAVL LIEQDLDLRS TLQRIVGAAC ALTGARYGAL GVLDAAGTGL
     SEFVYTGLDA ETAARIGPPP KGIGVLGLLI RDPRPIRLAD LAAHPAAVGF PPGHPPMRSF
     LGVPVRVGDD VYGNLYLTEK RDAAEFTADD EALVVAFAKA AGLAIRNARL HARVEELALA
     ADRERIAREL HDTVIQRLFA TGLALQSVVP ITEVPAVRKQ ILETVADLDE TIRQIRTTIF
     SLEPPPETAP SLRARLLEIT SDAARGLGFE PEVRFAGPVD AVVPEPIGRE ILVVAREALA
     NVARHAHARH VEVRLAVDGG ESAAGGAPAA VILSVTDDGV GVDEAVIHGG RSRRGGHGLR
     NMRERAEALG GVFSIQPVDG GGTLLEWRVP LT
//