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
//