ID A0A0Q9ENZ0_9GAMM Unreviewed; 886 AA.
AC A0A0Q9ENZ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASE45_10785 {ECO:0000313|EMBL:KRD69596.1};
OS Lysobacter sp. Root96.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1736612 {ECO:0000313|EMBL:KRD69596.1, ECO:0000313|Proteomes:UP000050805};
RN [1] {ECO:0000313|EMBL:KRD69596.1, ECO:0000313|Proteomes:UP000050805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root96 {ECO:0000313|EMBL:KRD69596.1,
RC ECO:0000313|Proteomes:UP000050805};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD69596.1, ECO:0000313|Proteomes:UP000050805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root96 {ECO:0000313|EMBL:KRD69596.1,
RC ECO:0000313|Proteomes:UP000050805};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRD69596.1}.
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DR EMBL; LMJN01000002; KRD69596.1; -; Genomic_DNA.
DR RefSeq; WP_056305603.1; NZ_LMJN01000002.1.
DR AlphaFoldDB; A0A0Q9ENZ0; -.
DR STRING; 1736612.ASE45_10785; -.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000050805; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR029016; GAF-like_dom_sf.
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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRD69596.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000050805};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 658..879
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 886 AA; 96187 MW; 5E58CB97589B0D0F CRC64;
MTDARSAQAD ALIGELQRQG AGRLTVFLGA APGVGKTYAM LSRARELQRR GADVVIGIVE
THGRAETGAL VDGLELLPRK RIEYQGRTIE EMDLDALLAR RPKLALVDEL AHRNAPGSRH
ERRWQDVAEL LDAGIDVYST VNIQHLESLN DVVHRITGVR VGETVPDALF DRLRDIVLVD
LPPRELIERL QQGKVYVPDQ AAHALQAFFS PSNLTALREL AMQTAADRVD SDLREAQTAR
GLPGVPLRRG VLVAIDGRGQ SEYLVRIARR LAERRDAPWT VVTVQTGAAP ADAQQVELDR
AFALARRLGG DTAVLHGASI VDALLDHAAR AGISAIVLGR TRERPVARMF NRTLTQQLIQ
RGAHYELTIV STPEARAKAR RALRPLGGLL TRSDAGLAVI AAALATALAW IAERWIGLDD
LSLIFIVAVV VVAARTRMTA AVIAAVLCFF AYNFFFIEPR YTLLIGASQG VTTVVLFLVA
ALVAGRLASK LRMQVLALRA ANAHAIALQT LGRQLAAAAD LGQVTQAARD ALRRSLGADA
IVRFGDTGLH GADLPELTDK DRAAADWSLR HRRPAGRYTD TLAGSDWWFL PLAGGDGGVI
GLRFPQRGGR LGPEQQRLAE AMAEDIAQAA VRTRLVADLE NARVSGETER LRSALLSSVS
HDLRSPLAAI IGAASSLDNY AEAMSREDRH SLLETVRIEG ERLDRYIQNL LDMTRLGHGG
LTLNRDWIGV DELIGSAVTR LQRYEPGARF EIRLEPELGP IWVHPALVEQ ALFNVLENAA
KFSPAGEAVT VEARHVDGQL RIDVRDRGPG IPEDERKRIF DMFYSVERGD RGRQGTGLGL
AICQGMIGAH GGSVEALPGA PDEHDRRGTT IRITLPLIEP AAPATA
//