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Database: UniProt
Entry: A0LW35_ACIC1
LinkDB: A0LW35_ACIC1
Original site: A0LW35_ACIC1 
ID   A0LW35_ACIC1            Unreviewed;       839 AA.
AC   A0LW35;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Acel_1873 {ECO:0000313|EMBL:ABK53645.1};
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC   Acidothermus.
OX   NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK53645.1, ECO:0000313|Proteomes:UP000008221};
RN   [1] {ECO:0000313|EMBL:ABK53645.1, 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   -!- FUNCTION: Involved in the transmission of sensory signals from the
CC       chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC       can transfer its phosphate group to either CheB or CheY.
CC       {ECO:0000256|ARBA:ARBA00035100}.
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; CP000481; ABK53645.1; -; Genomic_DNA.
DR   RefSeq; WP_011720708.1; NC_008578.1.
DR   AlphaFoldDB; A0LW35; -.
DR   STRING; 351607.Acel_1873; -.
DR   KEGG; ace:Acel_1873; -.
DR   eggNOG; COG0643; Bacteria.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG2198; Bacteria.
DR   HOGENOM; CLU_000650_2_1_11; -.
DR   InParanoid; A0LW35; -.
DR   OMA; ACRMRPF; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000008221; Chromosome.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01584; CheW; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF50341; CheW-like; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABK53645.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008221};
KW   Transferase {ECO:0000313|EMBL:ABK53645.1}.
FT   DOMAIN          3..107
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          329..562
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          564..696
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   DOMAIN          720..836
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          131..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..164
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..208
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..233
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         50
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT   MOD_RES         769
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   839 AA;  87727 MW;  CBBDA8A84A43E9B2 CRC64;
     MGGWAEDPEL LATFRAEVEE RLASLSAGLL RLETGAASRQ VLSALFRDAH TVKGSARMMG
     LTAVLETAHA AEDLLAALRD GRFPVRRDLV DLLLATVDGI SRSLPGDPAP VGEEHLRALI
     AALRSALDGE EPVTVPRLPE PTVTVQSGPQ PLAVPPPPAR PGTTPSATET PAPAAQAAAP
     PFAVPPPPDG QAAGPPLAVP PPPAGPTGSP AGSTARPPRP AGSAPPPAGS APVGRPSTPT
     ATLSTPAAAA STLLESITPP AAVQIGGPTE PERGFDAIRV ASRRVYDLLD VVGEAELDAR
     RVERNAIELE TLLTEQQRWL RAVRAAATQP SEDLELALHR LVATSDQLVA SGHQLRERVE
     DARSRLAQVR DGAMGLAMVP VRRVLSGFPR LVRDVASAGG KDVGLRLVGE DVELDKKVLD
     AIADALRHLV TNAVDHGCET PAERVAAGKP PRATVTVEAR SAGGTVVLEV ADDGRGIDES
     AVRRQAIERG LLPPDSTVSG PALLQVLFAP AFSTAPTVTV TSGRGVGLDV VRTVVDELGG
     TIDIYTEPGR GTRFVLTLPI TLGVLRCLIA RVGAERYAVP VPNVIESISL RDVPVDNLAG
     APVVVRHGTS VPLLDLGAAL GVEGVRDPRA ALVVRQGGGD LVAWSVDRLE GELELVVKDL
     GSFIGRLPLV TGATIDGDGT VVCLLDLREM SARTGAASTA QPATAPPELE TPRPLGRRPR
     ILVVEDSVGV RELERVILEG AGYEVTTAVD GLDGLARLRT ELPDLVLADV EMPGMDGFTL
     TRTIRRTRGW EHLPVVIMTS RGDDGDRRAG MEAGANAYLL KSEFDQAQLV ETVGRLLGR
//
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