ID A0A0Q5HS17_9BURK Unreviewed; 752 AA.
AC A0A0Q5HS17;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF77_01395 {ECO:0000313|EMBL:KQQ96682.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ96682.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ96682.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ96682.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ96682.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ96682.1,
RC ECO:0000313|Proteomes:UP000051760};
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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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:KQQ96682.1}.
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DR EMBL; LMOJ01000001; KQQ96682.1; -; Genomic_DNA.
DR RefSeq; WP_056333341.1; NZ_LMOJ01000001.1.
DR AlphaFoldDB; A0A0Q5HS17; -.
DR STRING; 1736272.ASF77_01395; -.
DR OrthoDB; 9808408at2; -.
DR Proteomes; UP000051760; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR PRINTS; PR01033; PHYTOCHROME.
DR SMART; SM00065; GAF; 1.
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; SSF55781; GAF domain-like; 2.
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; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Reference proteome {ECO:0000313|Proteomes:UP000051760};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606}.
FT DOMAIN 147..305
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 536..750
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 752 AA; 82769 MW; CE5F8CD08096595A CRC64;
MTPAPIATLD LSGCDREPIR TPGSIQPHGF LLTLSHEGVV LQASANLVRW LGIEAEAVCG
QPLAEVIGQA AAARVLPALT GDALGNRPFY LGTVTAANGC HFDALGHAWD GVLVLECEAV
ERAEAPDFRH LYPLLGDFLL NVDESQSVES LAALAARHVR MVTGYGRVMV YQFDRDGHGH
VMAESKEESY HSYMGQRFPA SDIPAQARDL YALSRIRLIQ DANYVPSPLV PAENPVSGRR
NDLSFAALRS VSPVHLQYMR NMGTLASMSV SLMVKGKLWG LISCHNETPC PVAFEKRTAC
EQLGQVLALC IESREDASEL QFRLEVRRMM VAMLGNLTKG ADVIDNMSVV FPELLRFARA
GGVAVVADER VLTYGDTPEV AAIRNLVSWL EQEGHGTEVF HTDALSNIYP RAAALKRNAS
GLLSMPISRL HKHYLLWFRP EVVHTIEWAG NPHEKAARSD ADVPGTLVQL TPRTSFATWR
ETIHGVSLPW HVAEIELTGE FRSALLGIAL ERAEQMAELA EELGRANKEL EAFSYSVSHD
LRAPLRHIVG FSDLLLESSG SEDATMRQRF LTNIKESARL AGKLVDDLLS FSQMGRAALR
PVDVDMSKLV ASCIDKLGLD IGKRNIEWHL APLPRITADP TFLHLAMMNL LSNAVKFTGQ
RDPAIINVRA DQDEHETVFH VADNGAGFNM DYVHKLFGVF QRLHRMEDFQ GTGIGLANVR
RIVERHGGRA WAESIQGQGA TFSFSIPRTL AL
//
