ID A0A3M8R882_9PROT Unreviewed; 739 AA.
AC A0A3M8R882;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EC580_05575 {ECO:0000313|EMBL:RNF64788.1};
OS Acidithiobacillus sulfuriphilus.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=1867749 {ECO:0000313|EMBL:RNF64788.1, ECO:0000313|Proteomes:UP000271650};
RN [1] {ECO:0000313|EMBL:RNF64788.1, ECO:0000313|Proteomes:UP000271650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ-2 {ECO:0000313|EMBL:RNF64788.1,
RC ECO:0000313|Proteomes:UP000271650};
RA Falagan C., Moya-Beltran A., Quatrini R., Johnson D.B.;
RT "Acidithiobacillus sulfuriphilus sp. nov.: an extremely acidophilic sulfur-
RT oxidizing chemolithotroph isolated from a neutral pH environment.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RNF64788.1}.
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DR EMBL; RIZI01000148; RNF64788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8R882; -.
DR OrthoDB; 5287283at2; -.
DR Proteomes; UP000271650; 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; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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 Gene3D; 3.30.450.20; PAS 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; IPR017232; NtrY.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000271650};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 324..376
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 517..736
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 739 AA; 80366 MW; 95FF865F1E154486 CRC64;
MDQQRRFTLR RWLRALSAGE IRDASRLAPR RSAILLLLAV AAFLAVDFFA STGGPLSTYF
VPLLLASAVT ALFLLILVLA SLGALWMRLR HGEVGSQLAA RLVLIIGLLS FTPAAIIFAF
SWQYLDQGVD SWFSSAVQSA LDQALDVART GVDRYRNNTL AAAENISQAL VGESDNSTVT
TVIQLRDQYH LASVTLFGSD NRIIATSSES LSITPRLPRR ELLSMAGGRP AAIIEPESGG
RLVVKALVPV LSPQLGQGNR ILYVEQPIPQ QLTSAADAVQ VAYTRYHQLL LMREPMKTAF
QLSLGVALLL TVLAAIWIGL HLARRLTAPI ARLAAGTQAV ARGEFVPVLS VPSNDEMGVL
LHSFNNMTRQ LARAKQQAAA AQEQAEQRRL YLETLVNQLS SGILTFDGQG GLLEANGAAA
QILQTPLPTG TDLDALRDGP LLAPFWETLG EWILHSRGEM QREIAIERPE GRQSLILHGA
RLHGEDGEGG GFVLVFDDVS TLVAAQRSAA WSEVARRLAH EIKNPLTPIQ LSAERLRRKY
LERLGTEGET LDRATRTIIH QVDALKVMVD AFSEYARQPQ LQLRPVDLNM VIAEAVDLYR
GQDTGVEIRA ELAADLPPLL ADANRLRQIL NNLLRNALDA LQGLGEGRGI IILRSRMAGD
VEPKLLELSV VDNGPGFPPE ILKRVFEPYV TSKVKGSGLG LAIVRRIVEE HGGTITADNE
GVQGGARILI HFPLTDGAA
//
