ID A0A2P8KS85_9BURK Unreviewed; 361 AA.
AC A0A2P8KS85;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C7T35_04165 {ECO:0000313|EMBL:PSL85825.1}, GXN78_27755
GN {ECO:0000313|EMBL:NDZ16609.1};
OS Variovorax sp. WS11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1105204 {ECO:0000313|EMBL:PSL85825.1, ECO:0000313|Proteomes:UP000241151};
RN [1] {ECO:0000313|EMBL:PSL85825.1, ECO:0000313|Proteomes:UP000241151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:PSL85825.1,
RC ECO:0000313|Proteomes:UP000241151};
RA Crombie A.T., Mejia-Florez N.L., Murrell C.;
RT "Isoprene degraders from the Poplar phyllosphere.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NDZ16609.1, ECO:0000313|Proteomes:UP000479786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:NDZ16609.1,
RC ECO:0000313|Proteomes:UP000479786};
RA Dawson R.A., Larke-Mejia N.L., Crombie A.T., Ul-Haque M.F., Murrell J.C.;
RT "Isoprene oxidation by the Gram negative model bacterium Variovorax sp.
RT WS11.";
RL Submitted (FEB-2020) 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:PSL85825.1}.
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DR EMBL; JAAGOW010000003; NDZ16609.1; -; Genomic_DNA.
DR EMBL; PXZZ01000004; PSL85825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8KS85; -.
DR OrthoDB; 8864477at2; -.
DR Proteomes; UP000241151; Unassembled WGS sequence.
DR Proteomes; UP000479786; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF08447; PAS_3; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:PSL85825.1};
KW Transferase {ECO:0000313|EMBL:PSL85825.1}.
FT DOMAIN 69..141
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 149..201
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT COILED 24..72
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 361 AA; 39170 MW; 60A4D86D51DA41FC CRC64;
MSSSIATAAL LALALLAWLA VSAARRAARR RDAWNARLAQ LEQQVAEQHG AFERAEASRA
VAEAELRASE ERYAAALRGS QDGMWDWDLA SGRVQLSPRW KSMLGFEAHE LADDLQGWGS
RVHPEDRAAL DEALARPLAS GSAPADARFE HELRLVHKDG SVRWVLSRGV ALRRASGAAY
RVIGQDTDVT QLRRVSHVLQ AVADGTAGAV GEAFFPAMVR HFAQALGLDC AFVAECADQP
PTRVRTLAYW SDGTLKDNIE FALAGTPCEA VVHTEQAALH RCGLAQMFPR EAGWESYLGL
PIVASDGRML GHLAFRHRAP LGDEVLVDAV YRIFLARAAA ELERIQALAR LRVEASGAVA
S
//