ID A0A0Q4GZX1_9BURK Unreviewed; 778 AA.
AC A0A0Q4GZX1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASE76_04195 {ECO:0000313|EMBL:KQM80343.1};
OS Xylophilus sp. Leaf220.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Xylophilus.
OX NCBI_TaxID=1735686 {ECO:0000313|EMBL:KQM80343.1, ECO:0000313|Proteomes:UP000051325};
RN [1] {ECO:0000313|EMBL:KQM80343.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM80343.1,
RC ECO:0000313|Proteomes:UP000051325};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM80343.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM80343.1,
RC ECO:0000313|Proteomes:UP000051325};
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:KQM80343.1}.
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DR EMBL; LMKO01000001; KQM80343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q4GZX1; -.
DR STRING; 1735686.ASE76_04195; -.
DR Proteomes; UP000051325; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00130; PAS; 2.
DR CDD; cd18161; REC_hyHK_blue-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
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; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
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:UP000051325}.
FT DOMAIN 1..67
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 69..121
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 193..247
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 248..323
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 326..378
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 416..640
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 662..776
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 712
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 778 AA; 85121 MW; BA3AD103A44B653E CRC64;
MVRSAVDFAV IATDVQGIVT DWNPGAEHVL HWTRAEMLGH TADRIFLPED RAVDRMGTEM
RCALRDGRAS DERWHMRQDG SRFWASGELM PLRAEDGTHI GYVKILRDFT AQREAADQQR
LESEFMRGVL ASSGDCIKVL DLDGRLVYMS EGGQSVMEVD DFAAVRGCPW PDFWEDEGNL
SAVAAIAAAR AGRAGHFQNF ANTLKGRRRF WDVQVTPILG RDGLPERLLA VSRDITSTKE
AERRLALSQE RLDLALGASD MVGIWDWDLA SNLLYADARF ARFYGVDPER GESGAPIEEY
LRAVHPDDLA RIRDEFRALF GNGGDYASDY RVVQPDGAVR WVSARGRLVR DAEGRPLRFP
GASVEITARK RAETTVREAN ELLETRIAEA LALRATAEDA LRQSQKMEAV GQLTGGLAHD
FNNLLASISG SFDLLRRRLA QGRHADLDRY IDIGRGATER AAALTHRLLA FSRRQTLDPK
PTSANRLVQG MEELIRRTVG PEIRTTLALE DGLWSTLVDP HQLENALLNL CINARDAMPF
GGHLLVKTCN RTLTDAVATE SGMVAGDYVA LDVTDSGSGM SPEVVQRVFE PFFTTKPLGM
GTGLGLSMVY GFAKQSGGEV RIASEPGLGT SVCIYLPRHA MDETPQAARL PLATPRGAQG
ETVLVVDDES AVRMLILDAL QDQGYTVLAA ADGDGAMSIL RSDVRVDLLV TDVGLPGGMN
GRQIADAARV DRPGLPVLFV TGYAEGAMSG EMPSGMHLLA KPFSMDLLSA RVRELIPL
//
