ID A0A0S9NQK1_9BURK Unreviewed; 889 AA.
AC A0A0S9NQK1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF44_23090 {ECO:0000313|EMBL:KQP47570.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP47570.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP47570.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP47570.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP47570.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP47570.1,
RC ECO:0000313|Proteomes:UP000051759};
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:KQP47570.1}.
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DR EMBL; LMNA01000003; KQP47570.1; -; Genomic_DNA.
DR RefSeq; WP_056898538.1; NZ_LMNA01000003.1.
DR AlphaFoldDB; A0A0S9NQK1; -.
DR STRING; 1736318.ASF44_23090; -.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000051759; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF13492; GAF_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051759};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 423..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 672..883
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 889 AA; 94563 MW; C4034B2625C96898 CRC64;
MTATARPDPD ALLAQLQSDA ARDQRGRLRI YFGANAGVGK TWAMLTAAQR ALQAGRDVVI
GVVETHGRSE TAALVAGLPA LALRSAPHRG HVLAEFDLDA ALARRPAVLL VDELAHSNAP
GSRHAKRWQD VEELLAAGIE VWSALNVQHL ESLNGTVGAI TGIRVHETVP DSVLDGADEV
VLVDATPDEL AARLAAGKVY LPQQAERAAQ NFFRKGNLIA LREIALRRTA EHVEDDVRDW
RVEQSGAPPA WNTSGAVLAA VGPGMGAAQT VRAAARLAGQ LNVRWHAVYV ETPALARLPA
TQRDRILAVL RLADELGAET AVRTGQDIAA ELAAQARQLN CATLLFGRSA APAWWRRWRM
PLALQLARAA PGLDLLSVAR NDSARRLPHQ RLAAEPAVGA APWPGYAWAG AASVAVTLLA
TPLSGVLELT NIVMLFLLGV VGVAWRFGRG PAAFAAALNV LAFDFFFVQP AFSFAVSDVQ
YLLTFAVMLG VGLLVGQLTA GLRFAASVSA SRERRAHSLF ELTRELSAAL ESGQVAALGA
AAVQRHFGGE ALVLVADQAE RLRLPAQPPA GFDASVADWT WRQAQPAGLA TATLAAQPWH
YVPLQAPMRV RGVLALRPAQ PRWLLIPEQA QQLDTLARQI AIAIERVHYV EVAQQAQLDI
ESERLRNALL NALSHDVRTP LTALIGLAES LRSLPAAEQV QAAGAIVAQA HALHALVGNL
LDMARLENDM HLRRDWQSVE EAVGAAIRAA QPALQGLAVQ TALPADLPLV EFDAVLMERV
LVNLLENAAR YGAPPIVISA QALPQALQLA VRDHGPGLPP ALRGREQQLF DKFTRGQAES
ATPGVGLGLA ICKAIVQAHG GEIAASDAAG GGAEFRITLP RREPPDLPA
//
