ID A0A0Q5DK86_9BURK Unreviewed; 651 AA.
AC A0A0Q5DK86;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF61_05785 {ECO:0000313|EMBL:KQQ40285.1};
OS Duganella sp. Leaf126.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ40285.1, ECO:0000313|Proteomes:UP000051032};
RN [1] {ECO:0000313|EMBL:KQQ40285.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ40285.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ40285.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ40285.1};
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:KQQ40285.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMNW01000012; KQQ40285.1; -; Genomic_DNA.
DR RefSeq; WP_056154687.1; NZ_LMNW01000012.1.
DR AlphaFoldDB; A0A0Q5DK86; -.
DR STRING; 1736266.ASF61_05785; -.
DR OrthoDB; 9768069at2; -.
DR Proteomes; UP000051032; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 6.10.250.690; -; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
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; 1.
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; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00448; REC; 2.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KQQ40285.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:KQQ40285.1}.
FT DOMAIN 7..124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 136..209
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 211..263
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 274..494
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 528..644
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 119..146
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 577
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 651 AA; 71394 MW; 1FA8B069B3346C6F CRC64;
MSNSDILILN VDDNDGARYV KTRILQGAGF EVIEAANGTD ALTMARRLRP TLVLLDVKLP
DINGIEVCRQ LKSDPATWTI LVLQTSAALT GRDDKIRGLE GGADNYLAAP IEADELIANV
NALLRLQRVQ ADLRNSEERF RQLTDNIEDV FWMFSLDGSA LLYVSNAYAG MWGRQPQALE
RTPGDWLEAI HAEDRAPVAA RWQLAGAGEP FDEEYRLTLA DGGVRWVRDR AFLVRDAANV
PYRLARITSD ITERRDMEDR LHAADDNKND FLATLAHELR NPLSPIRNAV ALMGEAAPDN
EALHRKARQI IVRQVAHLSR LVDDLLDVAR ISQGKLTLQL QRTELHAVVD VALETAQPML
ASRQHSLTVD VPPEPMWIHG DPVRLAQAIG NLLHNAAKFT NRGGQVRLQV KLLPDRRVSI
AVHDNGIGIT SYNLPRIFHM FAQGATAQDR AHDGLGIGLS LVSTLARMHN GSVHASSPGI
DLGSSFELVL PLLVDEQAAA APAPPPVEAG PEALAAALRP ARKPGVRRLL LVDDNVDSSE
VMGELLGILG HDVMLVHDAE RALDVARDYL PDTIILDIGM PKIDGYTLAR MLRADPLFAG
TRLIAHTGYG AEQDRRKTRD AGFDFHLVKP ANLDELGRSL GALPGHAHEK E
//
