ID A0A2N7W0F4_9BURK Unreviewed; 1248 AA.
AC A0A2N7W0F4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-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=C0Z19_16560 {ECO:0000313|EMBL:PMS22887.1};
OS Trinickia soli.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=380675 {ECO:0000313|EMBL:PMS22887.1, ECO:0000313|Proteomes:UP000235347};
RN [1] {ECO:0000313|EMBL:PMS22887.1, ECO:0000313|Proteomes:UP000235347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP25-8 {ECO:0000313|EMBL:PMS22887.1,
RC ECO:0000313|Proteomes:UP000235347};
RA Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA James E.K.;
RT "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT diazotrophy and nodulation in the Burkholderiaceae.";
RL Submitted (JAN-2018) 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:PMS22887.1}.
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DR EMBL; PNYB01000013; PMS22887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7W0F4; -.
DR Proteomes; UP000235347; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd12915; PDC2_DGC_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 5.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 1.
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; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000235347};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 468..538
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 586..650
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 723..951
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 995..1112
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1149..1246
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1044
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1188
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1248 AA; 135721 MW; E0A31C8E6B57CD70 CRC64;
MINVARLPRL LAHPSRAFRV NHATALGLIL ALWIALGAFA TWDARTELHS ERVQTDTLAD
ALAAHTSRVL REAAQVSSVV AWLVRRDGVG LPLQDYVHSG LLDMDVFIQV AVIDKHGILR
ASTMPDFRPI DLSDREHFRV HIDDANTRLF VGRPVIGRVS GQVSIQLSRR INDAQGRFVG
VVVVSMPPAY LTELYDALQI GHDGLVSVIG TRDFGIRARR SGDRENLDWQ RLPANAALRS
ALAHAPRGHF DETSPIDGVQ RTVSYKTLPD DPLVVEVGFS NADYLAAFRM RMLALLLAGV
ILTALIVAAE ANQGRLFRRL QAASEREREA LARTTDEATR ADALFTAIPD AALGLSADGQ
IDGHNPRLIE LLGWHGDEIG SSTPEQVARA FFRDDRSADR DEKSAHFAQM LRGIDLEHSA
SEVFHLETPY PCVYEMRVER RGANSNGVVA LIRDVSREHL SEQALMHSEA RYRQLIELSP
YAVFLIQEFT IAFANPKALE MLGAYSAAQI RGLSIIEFVH AEHREVVEER IGRLLLRYTA
APAREVKCLR LDGNAFIGEM TAVPYELDGV RGALVMLQDV TGRKEAETQR DRLFDLSLDL
TCLADPAGRF KRVNPAFTKV LGWSAEELLS RPFIDFVHPE DRASTVHKIE GRRPGEPIDQ
FENRYLCKDG GTRWLSWKAI QLEGLIYATA RDVTESRRAT QQLEQARADA EAASRAKSAF
LATMSHEIRT PMNGVIGMIE VLSQTPLSGD QGDMVTTVRE SANALLTLID DILDFSKIEA
GRLHIERVPL SIAHLVDGVC HSLKTVAERA GVRLQKSVSP DVPQVVLSDD TRLRQVLYNL
VGNAIKFSGG RPGKPGAVSV VVDCRPDPSD QKRAHVSFKV IDNGIGMSAD TLPKLFKPFT
QAEASTTRRF GGTGLGLAIC RRLCELMGGD VSAQSVQGEG STFTVSLPLE IGESVAEVGR
AHGHATAGAN GAQRIGSGSA GPALSVAQAR ELGRLILVAE DDAINQKVIL RQLGLLGHVA
EIAGDGREAL ALWRANRYAL LLTDLHMPEM DGYELVETIR REEAPGVRLP IVALTANAVQ
GEAARAKAVG MDGYLTKPLQ LARLQAVLDS HFPAHDAAAA STPAPAAPAP PQHEQAVDID
VLKGIVGDDP EIVRELLSDY QQSVGRLAAE LRSHCDAGRG REAGAIAHKL KSSSRSVGAL
MLGDLCAELE NAGKAGDLAL LANWAKQFDA ALAAVEDALE HLLAAEIK
//
