ID A0A2D8RHH5_9GAMM Unreviewed; 987 AA.
AC A0A2D8RHH5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CME36_19065 {ECO:0000313|EMBL:MAM89405.1};
OS Hahellaceae bacterium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae.
OX NCBI_TaxID=2048971 {ECO:0000313|EMBL:MAM89405.1, 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:MAM89405.1}.
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DR EMBL; NZNF01000041; MAM89405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D8RHH5; -.
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; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 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 InterPro; IPR011006; CheY-like_superfamily.
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; IPR019247; Histidine_kinase_BarA_N.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF09984; sCache_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF52172; CheY-like; 2.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:MAM89405.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 207..259
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 306..529
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 568..689
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 713..830
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 877..978
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 251..285
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 762
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 916
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 987 AA; 108712 MW; 63B4F27546C9C022 CRC64;
MIDTSGEQNF LSHFGAAGKH WSLRRKIFTY VMIPAALFAI VIGSVFITAR MMELEHIVTT
RSQETTDQLV NMSAVLLSRA DPTTLELIAG GTIQKEGVRS VVIYNQRGEI TAHAGAMPAA
RASQRNLLNA QGSRRRIGDY LQLVEPVWPT AQAAESTAGR AMPIGWVAVE FAYTPTQLAQ
SRAILLTVLG ILLTVFLSAV LASRLSRQLT RPLAHTVDVV SRIKRGDSGA RLDIEGSREI
ELLRDGINSM ADTLEHAHSE LQQNIDQATE DLRETLETIE IQNIELNIAR KEALQASKIK
SEFLANMSHE IRTPLNGIIG FARILLKSPL TQQQKDHATT IVKSSETLLS VINDILDFSR
IEAGKLLLDH SEFNVRDTID DAMTLLAPAA HEKNLDLAAM VYLDVPAILV GDPLRVKQII
LNLIGNAVKF TRHGEIVLRV MLEEQETNGH HVTIRISVSD TGVGMSKTQQ RALFHAFSQG
DASTARRFGG SGLGLVISRK LAEQMGGSIS VESTLGEGST FSVLLRLESL GQATGLRHLT
READDSLTPG DYENSRHYEA PPDLSGERLI YLEYQQRTAM VTQQILQHWS AEVVIAETLD
DLCDSIVKAQ KAGRGFSAAI LGITSYQLSS AVHLAAVERI EKQLDCRVVL LTPTIDSVRE
HAAILNACTA YALKPIPQRK LAAMMMLLLT KQHEGISPLR QPQSARLFRP KPRVMAVDDN
AANLRLIEAL LTDIGVEPVA VTSGYEALRL LKETSCDLVF MDVQMPGMDG METTRLIRSL
SGPVAHVPIL ALTAHALNEE REELLNNGFN EYVTKPISES QLLDLLSRYL QFAQPPKAAD
EVHQVYSNFS GTVRPSQKAA PEPCVDIESS IRLAAGKRDL AVELLSMLLE NLPEDEERFR
KLERANDVKG LEEAAHKLHG GTRYCGVPLL RAAVASLETM LKQKQPWTEH LKQTYAEIDR
LLYWADQTDW QPLMLGAPDG LSRSSAG
//
