ID U5NBX6_9BURK Unreviewed; 692 AA.
AC U5NBX6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cenrod_1599 {ECO:0000313|EMBL:AGX87684.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX87684.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX87684.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX87684.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(2013).
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; CP004885; AGX87684.1; -; Genomic_DNA.
DR AlphaFoldDB; U5NBX6; -.
DR STRING; 946483.Cenrod_1599; -.
DR KEGG; cbx:Cenrod_1599; -.
DR PATRIC; fig|946483.4.peg.1618; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_000445_114_51_4; -.
DR OrthoDB; 5389366at2; -.
DR Proteomes; UP000017184; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 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; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13188; PAS_8; 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; 2.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AGX87684.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000017184};
KW Transferase {ECO:0000313|EMBL:AGX87684.1}.
FT DOMAIN 203..273
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 339..552
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 574..690
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 625
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 692 AA; 74933 MW; 8ED4DB2AD23794A1 CRC64;
MLCLGANAVT RRSPARPQPL RRARSAASAT PVRPGRLVDE LRRYQAELRI QNQALRFSQA
DAEAASERFA TLFAHVPLAL MVVDERTQVL QHNARALALF RPLESDPPLV FLLPFVEPGM
ASQVEQGIEC ACREGASVLH ELTFLSGIDG RFTGDLHIAC FDDAEQPSLV CAIIDQSPLL
EQRRALQANQ RMLTERNEAL GQSQAQMAAI IDSSLDAIVS VDERLCISVC NPAAQSLFDC
GAAQAIGRGL DVFLPTAAQA LRQGEVEQTV RLGEMDARTL DGVQVPVEVS VSRQRNPDVA
TLFLRDLRMS KELERRRAVL EAQLLESQKM QAIGTLAGGI AHDFNNIIAA ILGNVALAMQ
DAGNEGPVGV SLAEIDRAAR RARDLVRQIL TFSRHEPPRR CSVMLARIVQ DAARLFHVTL
PPHIQLRQAI SSEPLWVMAD ATQIEQALLN LCTNAMHAIG DHAGYIAVEL EADHGASPPQ
ALLRVRDTGS GIDPETLQRI FEPFFTTKPV GQGTGLGLSV VHGIMQSHSG NIAVRSAPGE
GSEFVLRFPL CAQAPVAQAP AVATASAARR TGHRVMYVDD DEALVFLVQR ALRRRGYIVT
TYGDPKDALV ALGDDSNHVD LLVTDFNMPG YSGVELIRDA LRIRPALPVA LASGYVSPDI
ERDALAAGAR ALLHKPNDID ELCAAMQALL DG
//
