ID A0A3N1M8V6_9PROT Unreviewed; 945 AA.
AC A0A3N1M8V6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EDC65_1939 {ECO:0000313|EMBL:ROQ00143.1};
OS Stella humosa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Stellaceae; Stella.
OX NCBI_TaxID=94 {ECO:0000313|EMBL:ROQ00143.1, ECO:0000313|Proteomes:UP000278222};
RN [1] {ECO:0000313|EMBL:ROQ00143.1, ECO:0000313|Proteomes:UP000278222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5900 {ECO:0000313|EMBL:ROQ00143.1,
RC ECO:0000313|Proteomes:UP000278222};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (NOV-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 -!- 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: 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:ROQ00143.1}.
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DR EMBL; RJKX01000013; ROQ00143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1M8V6; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000278222; 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; 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; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 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; 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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000278222};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 196..417
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 437..559
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 589..707
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 752..849
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 491
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 640
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 791
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 945 AA; 100483 MW; 9EF935A6FFAB9D09 CRC64;
MTNELDKVRH HFGQFLVVLF WLHVPILAAT AVAVDRSPVG AALASTVLAA AYHLAWWRRG
SAPSTRYLSA IALMGEPVLL VYLFSGKAWQ MDMHMYFFAT LALTIAWCDK RAVVVAATAI
AIHHLALSYL LPLAVFPSGG DLSRVLLHAG IVAFQTAVLV WLSDTLVEKF GQIGTMSAET
QEAENANRAK SMFLANMSHE IRTPMNAILG FAHLALRTDL TPRQRDYVTK IDRAGNSLLR
LINDILDFSK NEAGKLSLER HPFAVQAAID NQLHIAATAA EAKGVALRAV IDKTVPEVLI
GDELRFSQVV LNLVTNAVKF TGNGTVTVSA KVAKREADTV TLEVSVQDTG IGMTEQQLAS
LFRSFSQADS STTRRFGGTG LGLAICKQIV ELMGGTIRAE SSPGAGSTFV FTVVMEVGAA
AAMPTEPVPT PDIARLRVLV ADDNPASRKI LQQIFASWSM PVDLVASGPE VLGAIDMAAS
AATPYDLVLL DWKMPGLDGI ETIAAMRAST GAGRMPSVLL VTAYGDDEVR ADAEAMDVAA
VLTKPVDPRA LLAAITRLHA SQTGTATAAD DDRNAGAIPM VAPARRGLRV LLAEDNPINR
EIAIELLTGA GLKVDTAENG RIACDRMQAA GGRYAAVLMD VQMPEMDGIE ATMRIRQDWP
ADRLPIIAMT AHAYEVERQR CFAAGMNDHI AKPVDPALLI RTLDRWLVAR DATSLAEEAA
SAAPPAASPT DTLPDSLPPF DLPAALRRVN GKHALLRRLI VNFGANFADA APNLRAHVAR
AALGDARRLA HTLKGVAASL EIREVAAVAA GIETALADDD LDGMDAKLDA LDGLMAPAIV
AARSLLPGGP TSAAPTGAAV DAAAVARATV ALRTMLGRRS LGARAGFDRL AQALGMTAEA
AAQHPMKAAL DRLDYDRALQ LLDEIPHADD STVPRTETLW IGPRF
//
