ID A0A1N7SNQ7_9BURK Unreviewed; 626 AA.
AC A0A1N7SNQ7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=BN2476_670096 {ECO:0000313|EMBL:SIT49062.1};
OS Paraburkholderia piptadeniae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1701573 {ECO:0000313|EMBL:SIT49062.1, ECO:0000313|Proteomes:UP000195569};
RN [1] {ECO:0000313|EMBL:SIT49062.1, ECO:0000313|Proteomes:UP000195569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 7183 {ECO:0000313|EMBL:SIT49062.1,
RC ECO:0000313|Proteomes:UP000195569};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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};
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DR EMBL; CYGY02000067; SIT49062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7SNQ7; -.
DR OrthoDB; 344644at2; -.
DR Proteomes; UP000195569; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 262..314
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 315..390
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 393..445
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
SQ SEQUENCE 626 AA; 69211 MW; 9157FED890D3F545 CRC64;
MSVYLFATVL LGAVAALVIP RLGYSPGVND LLYVAIGLAG CLAVFLLAMS YGARRTAPRV
VRVVESPELS AFAANLSTPA VLLDNDALVF VNSAFLKHAR WEPYADEIVG MPFSNLVHPQ
SLLDLTALLT QSRDGEERTS GSLRIAYGDG SFRLHPVTAL RARGSRMTLL QFPAPYTSAD
AQRSELQILH HCQDAVLQLP QALFRVDREL RLIFSNPAWR SLVRAVGSDP EPKPFSAFFH
PEDAETLNAR LKSLLDGHLS ELVMEARLIR ADNTTAQVEL RGHAVTDHEG ILVGAVGLAT
DISNRRRNEE ALRASRRSLR TLLSNLRAMI YRGQNNRERS MAFVSEGCFD LTGYEAFELI
DESRMTFRSL IHPDDREFVW NEVQTRIVAR KPYELTYRIV DRSGQTKWVW DQGCGVYSAR
DELMGLEGFI VEVARRQMVE EDARRRLTFE NSTGLSSASI FVDRVEFSVA LSSRTSLPCA
IFAINVGELE RVATRFGQDY ADRVLIAIGR RLEVVQGQLN CAALLDSHVF AVLLVDFGAD
ALAWCSEAQH LAQRVAANMD AALDELQDNL RRLIEAPVKV EGHEFKLPTR VGCSSIGNGE
SDVKKVLDHV LSASGWEVGD AAGEAG
//
