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Database: UniProt
Entry: A0A1Q7HSI1_9CHLR
LinkDB: A0A1Q7HSI1_9CHLR
Original site: A0A1Q7HSI1_9CHLR 
ID   A0A1Q7HSI1_9CHLR        Unreviewed;       544 AA.
AC   A0A1Q7HSI1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AUH85_11820 {ECO:0000313|EMBL:OLC54369.1};
OS   Chloroflexi bacterium 13_1_40CM_4_68_4.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1805077 {ECO:0000313|EMBL:OLC54369.1, ECO:0000313|Proteomes:UP000185706};
RN   [1] {ECO:0000313|EMBL:OLC54369.1, ECO:0000313|Proteomes:UP000185706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLC54369.1}.
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DR   EMBL; MNFM01000124; OLC54369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7HSI1; -.
DR   Proteomes; UP000185706; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 3.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR   PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF13492; GAF_3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          333..542
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   544 AA;  60026 MW;  D5BE3CBB3E8A9701 CRC64;
     MTPPADTERK LRELSFLHEV AQLASSARDW DEMLRIVIER TTDAMGVEVS SLYLLERREG
     LLRLVATNGL NRRYIGKATL RVGEGITGWV ANARVPAAAR QVRSDPRFKW IPGVDEERFT
     SMLSVPLLIH GELFGVVNVQ SVAERDFDGS QIEFLQTIAN QVAGIIEKGR LQREAERKLR
     EVSALFEVSN ILTSTLELDE VLSLIVQRLV RVYPDSAGAV FLRDGDDLRE RARSGETGKA
     VAQSARQAVS EARQIIAGEH LAFPLIVGDR LLGAVALRVP GTTDMAEEEI AFVGALANQA
     ALAIDKASLY AVERETTASL RELERARSEF VAVVTHDLRT PLSVIRGYLD LIAEKNGKSR
     VPIDEAVAQV GRLDQLVDRI LTGVRAARTK VPLRRTRFDL RAQVIATLDE LAPLARRHRL
     AGPRAGAPVW VRADRRRVSE VIAGLVHNAT KYAPERTRIT VRVEGRADRA IVSVSDEGAG
     VPPQERQRMF EPYARGDHTE IPGTGVGLFA SRRAIEAHGG DIWYEDGKTR GATFAFSLPL
     AMDK
//
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