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Database: UniProt
Entry: A0A0Q6M7C7_9BURK
LinkDB: A0A0Q6M7C7_9BURK
Original site: A0A0Q6M7C7_9BURK 
ID   A0A0Q6M7C7_9BURK        Unreviewed;       544 AA.
AC   A0A0Q6M7C7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ASC88_25230 {ECO:0000313|EMBL:KQU75662.1};
OS   Rhizobacter sp. Root29.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736511 {ECO:0000313|EMBL:KQU75662.1, ECO:0000313|Proteomes:UP000051195};
RN   [1] {ECO:0000313|EMBL:KQU75662.1, ECO:0000313|Proteomes:UP000051195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root29 {ECO:0000313|EMBL:KQU75662.1,
RC   ECO:0000313|Proteomes:UP000051195};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQU75662.1, ECO:0000313|Proteomes:UP000051195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root29 {ECO:0000313|EMBL:KQU75662.1,
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:KQU75662.1}.
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DR   EMBL; LMCN01000014; KQU75662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q6M7C7; -.
DR   STRING; 1736511.ASC88_25230; -.
DR   Proteomes; UP000051195; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17580; REC_2_DhkD-like; 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   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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051195}.
FT   DOMAIN          180..398
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          425..539
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         474
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   544 AA;  58456 MW;  7FA56A35252A4F1F CRC64;
     MQRDSSNRRR VLVLAPRGRD AAVIEQVLSG LDIAVEVCPN LAELTAGLGD ETTAAILTEE
     SLNEDGASSL QRWIESQPPW SDFPFVVLAT RQPARRSANA AAALARLGNA VLLERPLNAD
     TLVSAANSAM RSRRRQYDAR RQLEQYEAVA LENQRLFEAE RRARAEAEAA NRATDDFLAT
     LSHELRTPLS AILGWTYVLQ RRRGELGELA RGIDTIQRNA NSQARLIEDL LDMSRIVAGK
     VSLELQTVVP SQLLEQVVSS LLPSAQTKGI ELVTVLDPAL TPITGDPQRL LQVFRNLIVN
     ALKFTPGGGV VRVEAAVEGE ALVVRVVDNG VGISADFLPH VFERFRQADG STTRSQGGLG
     LGLAIVSRLV ELHGGSIAAQ SDGIGKGATF TVRLPPIEAA QPVHEAANDA VHGHPGGRGR
     ILNIRILLVE DDPDGREMVN QLLRDEGGEV VAVDSAARAL SALRDGVFDL IVSDIGMPDI
     DGYEFMKRIR DAGNPIPAIA LTAFARPEDK ARALEVGYSA HISKPVEPPA LIAAVAGVMG
     SGRR
//
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