ID A0A0Q6M5M7_9BURK Unreviewed; 420 AA.
AC A0A0Q6M5M7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASC88_06895 {ECO:0000313|EMBL:KQU71461.1};
OS Rhizobacter sp. Root29.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736511 {ECO:0000313|EMBL:KQU71461.1, ECO:0000313|Proteomes:UP000051195};
RN [1] {ECO:0000313|EMBL:KQU71461.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU71461.1,
RC ECO:0000313|Proteomes:UP000051195};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU71461.1, ECO:0000313|Proteomes:UP000051195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root29 {ECO:0000313|EMBL:KQU71461.1,
RC ECO:0000313|Proteomes:UP000051195};
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:KQU71461.1}.
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DR EMBL; LMCN01000033; KQU71461.1; -; Genomic_DNA.
DR RefSeq; WP_056810763.1; NZ_LMCN01000033.1.
DR AlphaFoldDB; A0A0Q6M5M7; -.
DR STRING; 1736511.ASC88_06895; -.
DR Proteomes; UP000051195; Unassembled WGS sequence.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KQU71461.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051195};
KW Transferase {ECO:0000313|EMBL:KQU71461.1}.
FT DOMAIN 81..133
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 229..415
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 420 AA; 45505 MW; D10D362B6E51D58A CRC64;
MDVDDRDLLR ALLDNSPDHI YFKDRQSRFI KSSAAQALQF GMTTPDGLVG KSDFDVFSEA
HARPAFEDEQ QIIRTGLPMV GKVERETWMD GRPDTWALTT KMPLRNRDGE IIGTFGITKD
ISELKEAERR IGEVHRQLLE ASRLAGMAEI ATNVLHNVGN VLNSVNISAG LIGDRLRASK
LKGLERAVGL MDEHAGDLGA FLTQDTRGKL LPGYLRDLAQ VLLAEQAAIA EELALLAKSV
DHIKEVVATQ QSYAGASRVV EFLKFDELLD DALRMNAGAL TRHKVEVVKQ VPEFPELPLD
RHRLLQILVN LISNAKQAMS GTPAGQSPCI TLGAALLPAA DGRVLRITVA DNGEGIVPEN
LVHVFAHGFT TRSNGHGFGL HSCAMAAQEM GGTLSAHSQG AGCGATFVLE IPIGSQEDSR
//
