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Database: UniProt
Entry: A0A328VJ39_9CHLR
LinkDB: A0A328VJ39_9CHLR
Original site: A0A328VJ39_9CHLR 
ID   A0A328VJ39_9CHLR        Unreviewed;       529 AA.
AC   A0A328VJ39;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A4R35_09120 {ECO:0000313|EMBL:RAQ95693.1};
OS   Thermogemmatispora tikiterensis.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Thermogemmatisporales;
OC   Thermogemmatisporaceae; Thermogemmatispora.
OX   NCBI_TaxID=1825093 {ECO:0000313|EMBL:RAQ95693.1, ECO:0000313|Proteomes:UP000248706};
RN   [1] {ECO:0000313|EMBL:RAQ95693.1, ECO:0000313|Proteomes:UP000248706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T81 {ECO:0000313|EMBL:RAQ95693.1,
RC   ECO:0000313|Proteomes:UP000248706};
RA   Tomazini A., Lal S., Stott M., Henrissat B., Polikarpov I., Sparling R.,
RA   Levin D.B.;
RT   "Analysis of Carbohydrate Active Enzymes in Thermogemmatispora T81 Reveals
RT   Carbohydrate Degradation Ability.";
RL   Submitted (AUG-2016) 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:RAQ95693.1}.
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DR   EMBL; MCIF01000002; RAQ95693.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328VJ39; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000248706; Unassembled WGS sequence.
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; 1.
DR   Gene3D; 1.10.287.130; -; 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; 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; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248706}.
FT   DOMAIN          95..147
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          148..218
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          221..273
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          277..510
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   529 AA;  60241 MW;  2F71EE475E8815A1 CRC64;
     MAGTFPEEGP PARDPSIEQL LQESHTREII DQSPDCIKLL DHEGHLLWLN QGGIRALEIE
     DVASCLNSEW VTFWSGEGRR LAEQALAEAR AGRVGHFEGF CPTMKGTPRW WQVTITPFLD
     HEGRIACLLA ISRDITERKQ AEAALKASEE RFRSLAEHAP IIIWQTDTTG SAVYFNTTWQ
     HFTGRPSAQC QGWQWTTAIH PSDRRRVLEH WHMALTNQQP YESQFRLLGA DGEYHDMLVR
     TTPYNDASLQ FAGYIGTMLD ISKQTALERQ RDAFLSLATH ELKTPLTALL GNIQLARRLL
     QRLARSTELD EETRLQLFEQ AQGLLERGEQ HLRRQNRLIN DLLEMSRNQD ETLELRLAHW
     DLVEIVRETV QDLQLAFPQR VIALNLPEKE SLFVYIDRDR IEQVVHNYLT NALKYSPPEQ
     PIEVGVERST MAARCWVRDA GPGLPDEARE HIWERFYQVP GIRPYQNAGA SLGLGLYISR
     RLIQQQGGEV GVESCEGVGS TFWFTLPLVA PTEEARGSIQ QAENKEGAA
//
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