ID A0A1F8QE45_9CHLR Unreviewed; 611 AA.
AC A0A1F8QE45;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2W35_02050 {ECO:0000313|EMBL:OGO33705.1};
OS Chloroflexi bacterium RBG_16_57_11.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797651 {ECO:0000313|EMBL:OGO33705.1, ECO:0000313|Proteomes:UP000179273};
RN [1] {ECO:0000313|EMBL:OGO33705.1, ECO:0000313|Proteomes:UP000179273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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:OGO33705.1}.
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DR EMBL; MGNS01000167; OGO33705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8QE45; -.
DR STRING; 1797651.A2W35_02050; -.
DR Proteomes; UP000179273; Unassembled WGS sequence.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF48; TWO-COMPONENT SENSOR HISTIDINE KINASE-RELATED; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
FT DOMAIN 13..132
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 294..459
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 611 AA; 67179 MW; 1D5FD20B9EF5269D CRC64;
MLGINDFLKK VPLFSGLPEH DLNTLCAMVE EVHLEMGEFL FHEGDAGEQA YVIQDGQIEI
LKNSGGREVL LALRQRGEVI GEMALLDAAP RFASARARTD SQLLSISHVH LGQLLDTSPS
AARAMLYTVT ARLRSTEIVL RQSEKMAQLG TLTAGIAHEL NNPAAAVQRG ADQLRQAIPE
LLLAHAGLQH EALSASQWAS LSALEQETRR RAAAPLDSDP LERSDREAEL EDWLVSQGVD
APWELAPVLA NLELNLAELG VDIDPRVQVL VLRWLAANFT IFSLIEEMSQ GAGRIGEIVK
ALKVYVYLDQ APVQPVDLHE GLDNTLVMLR SKLKSGVRVR REYDPAPIRI QAYGSELNQV
WTNIIDNAAD AMDGRGEIIL RTKRDQDWVE VEIEDNGPGI PEAIVEKIFS PFFTTKPVGK
GTGLGLNTSY NIVQKHGGEI KVYSRPGKTV FQVRLPVKLG AAQGGENPLV AIPQPSDEQL
KEILMKARVI AVVGISAQED TPAHTVPAYL QRKGYRIIPV NPNLKHVLGE KAYPDLLAVP
EPVDVVQIFR RSEAVLPVVE QAIQIGAHVV WMQEGIINEI AAEAGREAGL QVVMNTCMRT
THRRLFPQEK T
//
