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Database: UniProt
Entry: B2TA90_PARPJ
LinkDB: B2TA90_PARPJ
Original site: B2TA90_PARPJ 
ID   B2TA90_PARPJ            Unreviewed;      1646 AA.
AC   B2TA90;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Bphyt_7104 {ECO:0000313|EMBL:ACD21392.1};
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD21392.1, ECO:0000313|Proteomes:UP000001739};
RN   [1] {ECO:0000313|EMBL:ACD21392.1, ECO:0000313|Proteomes:UP000001739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN
RC   {ECO:0000313|Proteomes:UP000001739};
RX   PubMed=21551308; DOI=10.1128/JB.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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; CP001053; ACD21392.1; -; Genomic_DNA.
DR   RefSeq; WP_012428888.1; NC_010676.1.
DR   STRING; 398527.Bphyt_7104; -.
DR   KEGG; bpy:Bphyt_7104; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_82_1_4; -.
DR   OMA; VDPFQVE; -.
DR   OrthoDB; 5389366at2; -.
DR   Proteomes; UP000001739; Chromosome 2.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16919; HATPase_CckA-like; 1.
DR   CDD; cd00082; HisKA; 2.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd18161; REC_hyHK_blue-like; 1.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 1.10.287.130; -; 2.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 3.40.50.2300; -; 3.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 2.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF00072; Response_reg; 3.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 2.
DR   SMART; SM00388; HisKA; 2.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   SUPFAM; SSF52172; CheY-like; 3.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 2.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 2.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACD21392.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          373..600
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          659..775
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          995..1062
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1133..1356
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1376..1492
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1531..1645
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         708
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1426
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1580
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1646 AA;  179585 MW;  E51737993980FA75 CRC64;
     MTRRVEEIAL KQPDRFMSDA PLVGSAAPSF LAGGGELGAL IRAYDWTQTA LGAPDTWPQG
     LKIAIRIMLT SRQPLWIGWG DELLYFYNDP YKSIIGGKHP VALGQPTRVV WREIWTDIEP
     LLDTALAGAE GIFVEQKLLI MERNGFPEET YYTFSYSPIP GEDGEPGGII CANSDNTAQV
     VGERQLALLK ELAAVSPNGR DWREACELSA RALQANPQDL PFALLYAAEP GSDTVTLVGA
     CGIEPGHPAA PQTMRVGESL WPIADVVKIQ APQMVRDLTQ RFGTALPRGP WHLAPEQAVI
     LPVSAGSEST QTVLLIAGLN PCRLVDDAYR SFLNLVAGQI GAAIGYAQAY EEERRRAEAL
     AEIDRAKTTF FSNISHEFRT PLTLMLGPLE ELLARPQPGP SGNNAQTRSD IDDRALIEIT
     HRNGLRLLKL VNALLDFSRI EAGRIEIHTQ PTDIAAFTAE LASLFQSAME AAGLRLEVEI
     PATPVVVQLD REMWEKVVMN LLSNAYKFTF FGTVRVAVRA VTGGVEVSVT DSGIGVAEEE
     VPRLFERFHR VAGAPGRSVE GSGIGLAMVQ ELVKLHGGTV RVDSVLGEGA CFTVSLPSGA
     VQSEREDAGV HATMSKHARS YVDAALRWSP ENEIVDGASI ETASADETSP EAAPAAAARL
     LVVDDNADLR EYMSRILRAA GHDVRLASDG QAALEAARAE APDLVLSDVM MPRLDGFGLL
     RALRADPHLR DTPVLMLSAR AGEEARVDGI EHGADDYLTK PFSARELLAR VSGNLQLARL
     RRETEMKLRE ESRTLEILNR VGSTVAAELD LNRAVQIVTD AATELTGAAF GSFFYNVLDQ
     KGGSYMLFTL SGVQKEAFER LPMPRNTAVF APTFQGDGIV RVDDITQDPR YGHNAPHRGM
     PDGHVKVRSY LAAPVQSRGG EVVGGLFFGH PEPGVFTERA ERIVAGIAAQ AAIAIDNARL
     YQAAQIEIAE RTKAQSALRD LNETLERRVI ETVADRDRLW ELSEDLLVVA DIEGRLQRVS
     PSWSTALGHN VHWLMSRSYV DLVHPDDVET VRTHLAELRR TGVPVRYENR FKRIDGTWRW
     VAWTLALDPD TTRIHGVGRD VTADKETTEA LRHAEEALRM AQKMEAIGKL TGGVAHDFNN
     LLQVIGGNLQ LLAKDVAGSE KPEQRVRNAL AGVARGANLA SQLLAFGRRQ PLAPKVVNLG
     RFVRGLDDML RRALGDGVEI ETIVSGGLWN TLVDPFQVEN ALLNLAINAR DAMSGHGKLT
     IEAGNAALDD AYAKRNAEVT PGQYVMLAVT DTGAGMSPEV RERVFEPFFT TKAEGQGTGL
     GLSMVYGFVK QSGGHVKIYS EEGHGTTIRI YLPRVRQEED LETNIEAGPA KGGTETILAV
     EDDEEVRTTV VEMLSDLGYR VLKAKDAQSA LAIVESGVPI DMLFTDVVMP GPLRSTELAR
     KARERLPAIA VLFTSGYTDN AIVHSGRLDE GIELLSKPYT HEALARKVRY VLQAQNPQAA
     EIAEAEQHLL EIDPPVTPDG ADSFVTQTRL RILLVEDDEL IRVSTAELLR TFDFDILEAE
     GEHDAKQILS EHAISVMLTD VGLAGKSGVD LALDVCRERP DLRVIFLTGY DLVLTPAQRA
     VLPHAMLMRK PYDPLDLIDA LKTPLR
//
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