ID A0A0Q8XL05_9SPHN Unreviewed; 769 AA.
AC A0A0Q8XL05;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASE13_15535 {ECO:0000313|EMBL:KRC78866.1};
OS Sphingomonas sp. Root241.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC78866.1, ECO:0000313|Proteomes:UP000051629};
RN [1] {ECO:0000313|EMBL:KRC78866.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC78866.1,
RC ECO:0000313|Proteomes:UP000051629};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC78866.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC78866.1,
RC ECO:0000313|Proteomes:UP000051629};
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:KRC78866.1}.
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DR EMBL; LMIV01000003; KRC78866.1; -; Genomic_DNA.
DR RefSeq; WP_056618053.1; NZ_LMIV01000003.1.
DR AlphaFoldDB; A0A0Q8XL05; -.
DR STRING; 1736501.ASE13_15535; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000051629; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
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; 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; IPR005330; MHYT_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF03707; MHYT; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50924; MHYT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KRC78866.1};
KW Membrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:KRC78866.1};
KW Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00244}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 43..68
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 80..99
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 106..130
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 174..195
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 215..236
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT DOMAIN 7..196
FT /note="MHYT"
FT /evidence="ECO:0000259|PROSITE:PS50924"
FT DOMAIN 254..324
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 327..379
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 392..612
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 635..745
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 684
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 769 AA; 82415 MW; CDB8E8DB02D29205 CRC64;
MVMTGSHDPV LVAISISIAV AASYTALDLA GRIRASEGWL RRVWLVTAAI AMGGGIWAMH
FVAMLAFSMP GMEVGYDVEL TIASLLVAIV VTGAGFVVMG RSRGALAPLL VAGVFMGLGI
VAMHYIGMAA MQMPTALSYD RLWLAISVLI AVGAATAALW LASRESHHFE RFGAAALMGA
AIAGMHFAGM RAAIFTMVPG SGMTRGTASV NQSTLAIGVS TAAFLILFLS LIAAMFDRRF
ALLVQREANA LRQSEERFRS LYKGTPLPLH ALDRFGLIEH VSDAWLDLMG YAREEVIGRP
FINFLTEASA RQFLQDWPEL LRQGSLGPCE YRAVTRDGAF LDLVSAAKVE RDSADELLHV
VGGLTDVTGR RRAEEALRQA QKLETMGQLT GGIAHDFNNL LAVILGNLEL LRKRLPEDPQ
ALRLLESAYQ GAERGASLTQ RLLAFARRQD LRPQPVDIPE LVRGMTNLLQ RSLGPRVQVE
THFPLGLPLA RVDAHQLEMA LLNLAVNARD AMPDGGDVDI SASEVLLADG EVDDLHAGRY
VRLTFADTGA GMDEETLARA ADPFFTTKEV GQGTGLGLSM VQGLAAQSGG WLALRSVVGQ
GTTAELYLPF AERPVRRKPE PARPEEAPTK LPAMTILVVD DDPLVLANTA AMLEDLGVTV
MMASSGGGAL AEVQRGGIDL VVADQLMPQM TGLELAGAIR KDYPELPLLL VTGFADLDRD
AIKDIHVLAK PFTQEALARA VRMVKVSASV IPINQPRTRA SAGDNDSGI
//
