ID A0A1H8TGR4_9PROT Unreviewed; 796 AA.
AC A0A1H8TGR4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN02990966_03287 {ECO:0000313|EMBL:SEO89754.1};
OS Rhodospirillales bacterium URHD0017.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX NCBI_TaxID=1380357 {ECO:0000313|EMBL:SEO89754.1, ECO:0000313|Proteomes:UP000198826};
RN [1] {ECO:0000313|EMBL:SEO89754.1, ECO:0000313|Proteomes:UP000198826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URHD0017 {ECO:0000313|EMBL:SEO89754.1,
RC ECO:0000313|Proteomes:UP000198826};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FODP01000006; SEO89754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8TGR4; -.
DR STRING; 1380357.SAMN02990966_03287; -.
DR OrthoDB; 9795133at2; -.
DR Proteomes; UP000198826; 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; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 175..246
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 300..352
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 372..424
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 437..660
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 680..793
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 731
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 796 AA; 87447 MW; 9F6FE04BCDC29C97 CRC64;
MIARIRLRSL VILLGLLVAV GFALVVPAGY FAVFYAHLHH DLDFAARSKA SRLASFIADN
RESWQRPTDR LSQVIAQPEA GERATRQRVF DAGGRAILQS GEEKLTLPLA TVNVPVVVGG
SKVASVEMAA SLDKLLEEAA LVALASGLVG LSVFFLMRGV PLRAIDRTLG QLENAQERYR
RLFNVSPVLM VVLDRQTRRV LDANEATVRQ YGWSHEELLT MSSNDFYPPE DLPDVLAQRE
RFMADPNRVV PPLRHRKKDG TIIDVEQTIL PIDYDGKPAL LVTANDVTER NRAMRELRES
EQRYQALVET LPVGVLETTT DGRIVTANLA WRHMFGFGDD EDLGKLDVRD LYANPDDRGA
VVQLVQAEGA IPATESVFRR RDGTIFPVER YLRSVRDETG MVTSLRGIVI DITQRKSLEA
QLHQAQKMEA VGQLTGGVAH DFNNILMIVM AGVDALEEEK SLSQAARRRV DQISRAIDKA
SDLTRSLLAF SHKLPLLPQR VDLNALVLDV GRLLQRTLGT QVEIESMLGK DLWPVEVDRG
QLENALVNLC VNARDAMPDG GRVLIETRNV VLDGHGRGKD ADLPPGAYVR LSVTDTGEGI
AAEVLPRVFD PFFTTKEVGK GTGLGLSMVH GFIIQSHGHI AIQSERGRGT SITIHLPRAA
DLADEGDKPV ATDLPRGRER ILVVEDESHV GDAVVEQLQS LGYAVTQAAD GSAGLAAFET
AERPYDLLLT DIVMPGLNGK KLADEVAARW PGTSVLFMSG YRPDNESRLD PGARLLTKPF
HKSDLATAVR KALDTR
//