ID A0A0Q7PX53_9GAMM Unreviewed; 535 AA.
AC A0A0Q7PX53;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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=ASD14_06430 {ECO:0000313|EMBL:KQY52272.1};
OS Lysobacter sp. Root494.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1736549 {ECO:0000313|EMBL:KQY52272.1, ECO:0000313|Proteomes:UP000051738};
RN [1] {ECO:0000313|EMBL:KQY52272.1, ECO:0000313|Proteomes:UP000051738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root494 {ECO:0000313|EMBL:KQY52272.1,
RC ECO:0000313|Proteomes:UP000051738};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY52272.1, ECO:0000313|Proteomes:UP000051738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root494 {ECO:0000313|EMBL:KQY52272.1,
RC ECO:0000313|Proteomes:UP000051738};
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:KQY52272.1}.
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DR EMBL; LMFH01000005; KQY52272.1; -; Genomic_DNA.
DR RefSeq; WP_056130677.1; NZ_LMFH01000005.1.
DR AlphaFoldDB; A0A0Q7PX53; -.
DR STRING; 1736549.ASD14_06430; -.
DR OrthoDB; 9772100at2; -.
DR Proteomes; UP000051738; 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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR033424; MASE4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF00512; HisKA; 1.
DR Pfam; PF17158; MASE4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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 Kinase {ECO:0000313|EMBL:KQY52272.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051738};
KW Transferase {ECO:0000313|EMBL:KQY52272.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 314..529
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 535 AA; 58051 MW; 3376A44A64DF3F52 CRC64;
MQRLAVAESE EQQFILSNLP PSPAQKRLAL GIVIGLATAL YLVVGPFGGQ QLGASYSFVA
IYTTAMFVTD LITAILLFAQ FSILRSRAIL VIASGYLFTA LLIVPYVIAF PGALAPGGLA
GGLQTTAHLY LIWHCGFPLF IIGYALLKDD ESFGLTPQGK IGEEILFSVS MTAAAAGAVT
IWCMNGGALL PDIMLDQSRF VPNWLRVVGA PIAFLCIVAL VVLWRRRRSI LDLFLLVVLC
AYLIEIPPHY FPYPARFSTG WYAVRVTSLL SSSIVLVVLL YEITALYGAL LAAVLRQRHE
REARLMTGDA IAATVAHEVR QPLTAIVTSA DAGLRFLDRA LPNLDRAKEA FTRIASDGHR
AGAIIENIRT NLRPDESNRT NVELNALIRE ALDLESSDLR KHRTTVQLEL HAGLPDVRAN
QVQLRQVVLN LIVNAVDAMS SSDGPRVLSV KTALHDGNQV LVSVTDSGSG IRSMDGDRVF
DPLFTTKSDG MGMGLSICRS IVEAHNGRLW FTPNTPHGVV FQFTLHSSNS APAPA
//