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Database: UniProt
Entry: A0A2D8RG80_9GAMM
LinkDB: A0A2D8RG80_9GAMM
Original site: A0A2D8RG80_9GAMM 
ID   A0A2D8RG80_9GAMM        Unreviewed;       833 AA.
AC   A0A2D8RG80;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-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=CME36_16535 {ECO:0000313|EMBL:MAM88912.1};
OS   Hahellaceae bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae.
OX   NCBI_TaxID=2048971 {ECO:0000313|EMBL:MAM88912.1, ECO:0000313|Proteomes:UP000225829};
RN   [1] {ECO:0000313|Proteomes:UP000225829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) 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:MAM88912.1}.
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DR   EMBL; NZNF01000040; MAM88912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D8RG80; -.
DR   Proteomes; UP000225829; 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; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.60.40.2380; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR   InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR   Pfam; PF07696; 7TMR-DISMED2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; 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        187..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        287..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        315..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        341..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          478..695
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          720..831
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          430..468
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         770
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   833 AA;  92833 MW;  1ABA20AA8610E801 CRC64;
     MLRLTLSCNR ISWIALFWLC SGLLFASEDL VLNEEASPGN LAASFVYISD RTVASRKQAL
     ALPPDRWQKL EHDIFNEGFV GSGFWLKATI RSDVSLEQGN WLLVLNNVLM EELSVYWQHD
     SEGLLLELVD FEAGQFAKLP LQGRHWLVPL TIQPGQSYTL LVHMKSFVVS QMPASILPVE
     RYLEHELLVG SLLNMAVAAL LVIAVVGLLL ALVYRDIGLF YHSVFVLGVA ILHASLQGLI
     FHWLWPHWPW LHKNIAFLAI VVALWAGVMF TREQMSSPES HPMFPKLLYF FAWLQPAVAL
     TSLLLPLHLR WQVNVLYLLS SVVTALVMGF VNSLRGQRVA IYYTAAMTIF FIGTFLLALN
     KLGFIPVNVY TDNLQLVGSL VGSVIFLLSV NERVNQKRLA KRAVKQQALD YERVAHETQV
     QLLRIERQTS EGLEQQVHAR TAELERALQE LKTAHSDLQL AKAAEEKAHL EKTRFLAAAS
     HDIRQPLHAL TLLVEDLLLS TPAQTAETVR TGLRVREAVD SLSALFDALF DLSKLDNKLV
     RPELELIDLA QLVSDYGERI QPLCQHANTV LQVDIPEKAV MVMSDRLMLE RILTILIDNA
     VNHSGSNRIG LVVSVSPSQL RLSVIDHGIG IAENDQVHIF EEFYQVDNEQ RNRSRGMGLG
     LALCRRLVGL IGCEITLHSA RGQGARFDIL MSRSPKDTAT ESSGRKAEGA QPTLCLQDKL
     VLVVDDDVLA REASAQLLQR WGMSVLPAAD GTEALAVLGE ARAPEFALLD YRLPGSNGLE
     LAKAIRARLG SKFPIIILTG DLRLSISEPD IRVLSKPIRP MRLRAAIQAI LQA
//
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