ID A0A0T2ZG66_9BURK Unreviewed; 789 AA.
AC A0A0T2ZG66;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-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=ASE11_22225 {ECO:0000313|EMBL:KRC10068.1};
OS Hydrogenophaga sp. Root209.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1736490 {ECO:0000313|EMBL:KRC10068.1, ECO:0000313|Proteomes:UP000050889};
RN [1] {ECO:0000313|Proteomes:UP000050889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root209 {ECO:0000313|Proteomes:UP000050889};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC10068.1, ECO:0000313|Proteomes:UP000050889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root209 {ECO:0000313|EMBL:KRC10068.1,
RC ECO:0000313|Proteomes:UP000050889};
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:KRC10068.1}.
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DR EMBL; LMIE01000005; KRC10068.1; -; Genomic_DNA.
DR RefSeq; WP_056268070.1; NZ_LMIE01000005.1.
DR AlphaFoldDB; A0A0T2ZG66; -.
DR STRING; 1736490.ASE11_22225; -.
DR OrthoDB; 5389366at2; -.
DR Proteomes; UP000050889; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd00156; REC; 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 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; 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; 3.
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; 2.
DR Pfam; PF13426; PAS_9; 1.
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}.
FT DOMAIN 83..136
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 137..213
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 216..267
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 268..330
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 344..397
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 417..641
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 668..785
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 720
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 789 AA; 87032 MW; 140A02617949AC09 CRC64;
MTLAPSPPDG DFSTLFNFLP IGAYRSSPEG QMLRANQALV RLNGYASEAE LRDAVNDIAN
EWYVDPVRRR EFQAQLERDG YVRGFVSEIH RHKTRERVWI SENAHGVRDA SGVLLYYEGT
VEDITDRMRD QKALRDSEEQ LRLITAQMPG AVFSVFVRHD GEREYRFLSA GVRELYGFEA
EDLMRDPALL SRYFHPEDRV MLERDRQAIM SGVVSLDTEF RVVLPDGRIK WICNRSSAVS
ADEHGFLRVG VLFDITDRKE AEAALHASET LWKLALESAG DGVWDWNIRT GEEFFSTSIK
AMFGYADDDI ANLSAELDAR THPDDRAQME LDRATHFEGR SPMYRNEHRI RCKDGRWKWV
LSRGVVIARD GNGLPLRMVG THTDITELKE AESQQRALEA QLRESQKMEA IGTLAGGVAH
DFNNLLAAIL GNLVLAREDV GEDHPAQESL AEISRAAIRA RQLVQQILTF SRRQTQEMQR
QPLKPLVEEA LGLMRSLLPA GLKLVTRLPA SGLQVLADAT QMQQVLMNLC TNAWQSMEGG
SGDITVALRE VRLDAAQVLQ LGGLNPGAYA CLSVADNGPG MDIETQRRIF EPFFTTKAPG
AGTGLGLAVV HGIVKAHRGA ISVHSQPGEG TRFDVYLPLA AAADAGESSS MAVSAAPVPM
SSAVAGKHVV YIDDYEALVF LVGRLLRKHG HQATTFESGE AALAWMQANP GVHVDLVVSD
QNMPGLSGVE TATEIRRLRP GLKIAIISGH VNDRLLAEAN EAGVSDVMGK QDSMDALGEA
IRDLLDRNA
//
