ID A0A495XKI2_9PSEU Unreviewed; 887 AA.
AC A0A495XKI2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-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=DFJ66_7532 {ECO:0000313|EMBL:RKT74189.1};
OS Saccharothrix variisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT74189.1, ECO:0000313|Proteomes:UP000272729};
RN [1] {ECO:0000313|EMBL:RKT74189.1, ECO:0000313|Proteomes:UP000272729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT74189.1,
RC ECO:0000313|Proteomes:UP000272729};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
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:RKT74189.1}.
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DR EMBL; RBXR01000001; RKT74189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495XKI2; -.
DR Proteomes; UP000272729; 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 CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR InterPro; IPR006016; UspA.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RKT74189.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000272729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 415..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 654..883
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 887 AA; 95083 MW; 04FA3FFFA65D7B4C CRC64;
MAGARRWWKR EHEVKSRCGG LALSRARPAS TLGCVEGKRR RGELRIYLGA APGVGKTFAM
LGEAHRRRER GTDVVVGLVE THGREKTAEL LTGLEEVSRR VLRHKGVQFT EMDVDAVLAR
APEVAVVDEL AHTNIPGSRN AKRWQDVEEL LDAGIDVLST VNVQHLESLN DVVERITGVR
QQETVPDEVV RRAQQVELVD ITPEALRRRL AHGNVYAAHK IDAALGNYFR VGNLTALREL
ALLWVADQVD VALLRYRHEQ RITDTWEARE RVVVSVSGGP ESETLIRRAR RIATRAGAEL
VVVHVLRGDG LTGVSPQSLA RARKVTDDVG ATFHTVVGDD VPTALLEFAR GVNATQLVLG
TSRRSRLARV FDEGIGAAVI QASGPIDVHM VTHDEARRGP RWQLGRSPLT RTRVLLGWLL
AVLLPFAVTG VGVGSRAELT FSTDVIAFFL VTVVVALVGG LGPAVGAALL GAGLLNYFFT
PPYYSLAVAT PENLVTLVAM LLVAVLVALV VDRAARLGEQ GARARTEAAL LASYARTVLT
SPFPLARLLE KVRENFGLDS VALLERRDGG WERVACVGPR PCDEPDDADV DVPVTGDVHL
ALRGRTLPAS DQRALEAAAG QALMALRQQR MAAETADAQR RAATTELRTA LLSAVGHDLR
TPLTSIKASI GSLRAHDIEL SEEDTRELLE AIEVSADRLT GLVDNLLDSS RLATGAVAPL
LRAVTYDEVV ARALAGIDDR RAVEVEVSEG LPAVLADSGL LERVVANVID NALRHGRLSP
RRGVDVDGDG AISADEPEIA VRASAHGDRV ELRVVDHGRG LPKNTADAVF APFQRLGDRD
NTPGVGLGLS VAKGFVEAMG GSIAAEDTPG GGLTIVISLP AAEVAVA
//
