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Database: UniProt
Entry: A0A0Q6JXY9_9SPHN
LinkDB: A0A0Q6JXY9_9SPHN
Original site: A0A0Q6JXY9_9SPHN 
ID   A0A0Q6JXY9_9SPHN        Unreviewed;       456 AA.
AC   A0A0Q6JXY9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASG67_12800 {ECO:0000313|EMBL:KQU48206.1};
OS   Sphingomonas sp. Leaf339.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU48206.1, ECO:0000313|Proteomes:UP000051371};
RN   [1] {ECO:0000313|EMBL:KQU48206.1, ECO:0000313|Proteomes:UP000051371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf339 {ECO:0000313|EMBL:KQU48206.1,
RC   ECO:0000313|Proteomes:UP000051371};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQU48206.1, ECO:0000313|Proteomes:UP000051371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf339 {ECO:0000313|EMBL:KQU48206.1,
RC   ECO:0000313|Proteomes:UP000051371};
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:KQU48206.1}.
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DR   EMBL; LMRS01000045; KQU48206.1; -; Genomic_DNA.
DR   RefSeq; WP_056531704.1; NZ_LMRS01000045.1.
DR   AlphaFoldDB; A0A0Q6JXY9; -.
DR   STRING; 1736343.ASG67_12800; -.
DR   OrthoDB; 9809567at2; -.
DR   Proteomes; UP000051371; 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; IPR013727; 2CSK_N.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF08521; 2CSK_N; 1.
DR   Pfam; PF02518; HATPase_c; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQU48206.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051371};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          198..249
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          257..456
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   456 AA;  50283 MW;  1C3A82BABB0D392E CRC64;
     MSEPLPEQRV RPKATGSLSR RMILIAAAWI VVLLAGGGFA LDRVLASAVT RNFDDQLEYV
     MTALIVSAEI DSGGEVMFTR EAADQRFLEP NSGLYWQVGA PGREAFPSRS LWDRRLAYGT
     PHSDRAVHSY DSAQFGTEEL RIVERDVKLP GSPVRWRFQV AQSREGLNSQ ITVLRRTLVR
     SFALLALGLI AMAALQTFYG LWPLRKVRAE IARMRAGHSA RVSDAMPLEV QPMVEELNAL
     IEHNERQAEE ARRHAGNLAH ALKTPLTVIM NAATAQADDL ADTVIREART MRRQVDHHLA
     RARAVGRRGS AHSRAEVWPS VESVERAVAR LYRHVRIDVA GPKDLSVHVE RQDLDEMLGN
     LIENAAKYGG GSVFVTVVAE AGFVELLVED DGTGIPEEDR IRIFDRGVRL DTGKPGTGLG
     LAIVRDVAEI YEGTVSLEES EDLGGLMVRL RLPAAG
//
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