ID A0A0T2ZIJ1_9BURK Unreviewed; 1259 AA.
AC A0A0T2ZIJ1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASE11_19620 {ECO:0000313|EMBL:KRC11089.1};
OS Hydrogenophaga sp. Root209.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1736490 {ECO:0000313|EMBL:KRC11089.1, 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:KRC11089.1, ECO:0000313|Proteomes:UP000050889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root209 {ECO:0000313|EMBL:KRC11089.1,
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:KRC11089.1}.
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DR EMBL; LMIE01000003; KRC11089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T2ZIJ1; -.
DR STRING; 1736490.ASE11_19620; -.
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; 6.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 7.
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 NCBIfam; TIGR00229; sensory_box; 6.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 4.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 7.
DR SMART; SM00091; PAS; 7.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 6.
DR PROSITE; PS50112; PAS; 4.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 63..134
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 136..188
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 258..314
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 415..467
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 540..591
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 599..670
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 673..725
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 726..796
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 868..943
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 945..997
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1026..1242
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 582..609
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 840..871
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1259 AA; 142098 MW; F0F69D48C3FD30CA CRC64;
MLEIETLKAE NQHLRQNYAQ HMGGSLHEDS SIDVSLRADL PLSLELALDA DKGSPVAAAH
LEYEALFAAL GSAFPIGIFR TDQAGVLTHV DARLQQIFAL GKHDFPNFGW LDRVHPDDLP
RVQEHWVRGI ATGESLSVEF RLIRPGDEVV HVLARNSPLR DEHGNVTSQL GFIQDITPMR
VLEAEARIKD ELNRQIIASS PDCTKVLDLD GRVVQMTAQG CRLLEVDDFE EVRMGAWADW
WPDDGVLLAL EAIESARSGE SSRFVAYGPT FKGTPKWWDT VVTPICDAHG QAVMLLAVSR
DITEQHLQHE SIQRFNAELE SAVQQRTEEL AVAKDRIHSA LREAQIAYNQ APCGYHSVDA
SGLYVLINQT ELNWLGYEDR NEVVGKKHFR DHVQPAYLDD VLERLQRLLR GETLEAAEIG
MLRRDGTGFI GLLNTTAVHD AQGRFLRTNN TLVDITERKA AEVALAAQRN FLQTVASSVP
VQLAFFDRDL ICRFANASYA RWLDGSPEKL AGLHLSRIAR SQDFEAARPR LDSALAGVAQ
RFEGERVFPD GTVFYASIDY TPYWHDGKVA GLFIQMLDIT ERKASEDLVN QTNRQLNQAL
SQAQALYNQA PCGYHSLDTR GVFVSVNDTE LGWLGYRRDE VVGKMVFREV LSAADLPLFE
SRMRKILKDD ALEGVEYQMR RRDGSTFYAL LSSSAVRDED GRFLRSNTTV VDITHRKAAE
MSLRDNQRFL QTITDHVPGL IAYLDAGLRF RFANAEHLRV YGMNPVDILG QHISQCVRPD
IWADIKPRME ATLAGQEQNF TTWRPTVDGK HIFVSSRYLP DVQDGKVRGL FVQMIDITES
KLIEERVSNL NEELEQRIRE RSAELLEAEQ RFRLMVDNLR DYCIFFMDAD GLITDWTDSA
QRMDGYSPTQ MLGRHYGVLF DPANPEHGRV RADQMLRLAA SRGQHELHNW HTRKDGTQYW
SHSVLIALRD DSGELRGFAK INRDMTDAKR LDDLMRNIND ELENRVVERT EQLLSANKDL
ESFSYSVSHD LRSPLRHISS FVSLLEEHMG GQCDEVSARY LNTIGNSARH MSQLIDGLLA
FSRLGRAAVN VTPVDFQLLV EAVVAQIGHD TEGRIVDWVV APDLPVVQGD ALLLREVWAN
LLGNAYKYSR PRERTRIEVG WSVDPVVGYT FFVRDNGVGF DTKYAQKLFG VFQRLHRASE
FEGTGIGLAL TRRIIERHSG SIWAESELGI GSVFYFSLPF EGPGFSDSIL DSMPAPLES
//
