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Database: UniProt
Entry: A0A1S8FFH1_9BURK
LinkDB: A0A1S8FFH1_9BURK
Original site: A0A1S8FFH1_9BURK 
ID   A0A1S8FFH1_9BURK        Unreviewed;       925 AA.
AC   A0A1S8FFH1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=B0B52_15615 {ECO:0000313|EMBL:OOG39439.1};
OS   Polaromonas sp. A23.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1944133 {ECO:0000313|EMBL:OOG39439.1, ECO:0000313|Proteomes:UP000218978};
RN   [1] {ECO:0000313|EMBL:OOG39439.1, ECO:0000313|Proteomes:UP000218978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A23 {ECO:0000313|EMBL:OOG39439.1,
RC   ECO:0000313|Proteomes:UP000218978};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) 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   -!- 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:OOG39439.1}.
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DR   EMBL; MUNO01000027; OOG39439.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8FFH1; -.
DR   STRING; 1944133.B0B52_15615; -.
DR   Proteomes; UP000218978; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.60.40.2380; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR   InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43711:SF24; SENSOR HISTIDINE KINASE RPPB; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR   Pfam; PF07696; 7TMR-DISMED2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218978};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..925
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012616739"
FT   TRANSMEM        185..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        252..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        282..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          495..546
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          573..594
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          620..671
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          689..909
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          656..685
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   925 AA;  102312 MW;  AAD70E4BCD6B297C CRC64;
     MPFLVLFLLV LLPVSQAHAQ SGKLAIDAEG SYTLSRAFTV LEDSTGQLTL DDVLKPGQQE
     RFKPVSQSGS ATNFGLTLSA FWLRINLETQ IDSPAQWLFE VAYPALDQLE LFTPRPHGGY
     DRQIGGDLQA FETRKIPHRN HVLPVTLQPG AENVLYLRVQ SQGTLSAPAR LWQPSALWQH
     DQAEYAMLSL YFGLLIGLLL YNLLLYFSVR DRAYVIYAGF AGGMALSQAA LTGLGGQFLW
     PGLTWWNSVS PPVGMAVTAT FGILFARKFL DSATRMPWMN RVMLALTGGW LLALLAALLL
     PYTVSSWMVT VLAVVSVTVV VLAAVLSVLK KCPGARYFLT AWAVLLLGVA TLVLHNTGVL
     PSNLLTSNSL LIGSALEMVL LSFALADRIN MERAEKEQAQ AASQADQAMV EALSQSQERY
     RTVLQERETI LANSIVGIAF LTPEGRFRWA NQAMLEIFGA GDEPLNSMEP FYLSREQYLR
     VGGDVAACIR DGKTYETEIQ VRQYNGTLIW ISLSGKSVSP RDLTQGTVWV MMDITRRKEL
     EAELVRTSSE REAILNSALV GIVLSVARRH EWVNEKFAEM MGYPRTELIG RSSMHLHANV
     AAWEDFGRQA RDELQRHGTY ACERELRRRN GELFWVQMGG SCLQPNDPDA GVIWTFLDIT
     ERKKSEEDTR EALEQQKELN ELRSRFVAMT SHEFRTPLAT ILSSGEILKH YGERLSAPEK
     ADVLDSIAAS VQRMMRMLDR VLLIGKAEAQ MLEFDPRPTD LRRLCLDLLE EAQVQQPESA
     CELRLDYAGG DEPGLYDEKL LRHILGNLLS NAVKYSPQGG EVLFKVVKEP QAMVLEVSDN
     GIGIPEDEIA HLYESFHRAS NVGAIQGTGL GLAIARNAVN VHGGTIDVRS RVGAAASGTC
     FTVRLPLAAG VSSSGPSPFR TEVEP
//
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