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Database: UniProt
Entry: A0A1F8PH70_9CHLR
LinkDB: A0A1F8PH70_9CHLR
Original site: A0A1F8PH70_9CHLR 
ID   A0A1F8PH70_9CHLR        Unreviewed;      1633 AA.
AC   A0A1F8PH70;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   28-JUN-2023, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A2Y54_00425 {ECO:0000313|EMBL:OGO22497.1};
OS   Chloroflexi bacterium RBG_16_51_16.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797644 {ECO:0000313|EMBL:OGO22497.1, ECO:0000313|Proteomes:UP000178729};
RN   [1] {ECO:0000313|EMBL:OGO22497.1, ECO:0000313|Proteomes:UP000178729}
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:OGO22497.1}.
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DR   EMBL; MGNL01000127; OGO22497.1; -; Genomic_DNA.
DR   Proteomes; UP000178729; 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   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 7.
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; 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; IPR035965; PAS-like_dom_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; PF01590; GAF; 1.
DR   Pfam; PF13185; GAF_2; 5.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 6.
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; 7.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          1370..1594
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1612..1633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1633 AA;  179727 MW;  7CC736733D3E44EB CRC64;
     MSILEKENGL LRRITAVGIP DETLKELIAR KQPLTALQHL MQPQFKISHS YFIPADQTPI
     LPADVHYVYS TYEVQSEVPK GNAWNPDDFL IFPIEDSKGE ILGLISVDDP SDGLRPDLAT
     IDSIEAFSVQ AALVLAQNKL ISGLRDRVAT LDSGLQRQQK LLDVTQNDLP VLLRKDLEAT
     ISLHNLDQRA QRVRAGLAIT EQVSRQLDSS SALLALGRET LTQLGMTAAM VAENSADGPR
     LLHTLGSVPR TTNVDALFGQ RNPLRTCMQT GEAILVSSMD DSEEWRDSPL LTSLRVKSFI
     CLPVYIQEKP VAAMLALSPE TMPSFTAEDR QVYFQIARQS SVILQNISLL NETRRRLQEV
     NLLLDFSRRL TGLDSDEILK TLLNSAMHVI PSAHAGTVLV WNQQAGLLLP LAVSGYADNE
     TMGRIQYRSG EALPGAAYAE KRIRRVDEVN FARDYVLIPE NITLYRQAVG GRMPVSCIHV
     PILTGEQCLG VLTLDNFNTQ GAFKSDDETL LISLTQQVAL SFENVRLMQA MRERAGQLQA
     LNDVATSLTS SLRSDQLVGS LLDNLTPILP FDSAAFWFRE GDQLTVVATR GYPDTEDPLG
     ASVGVTENAL FDKMSQTGQA ISIGDVREDA RFPRVEAPRL SWLGIPLVSK GVLAGVLALE
     KWQAYYYAPE QIQVGLTFAS QAAVALENAR LYEDSLNRAE ELDERSQRLA LLNRFSSSLS
     GLLDIDQILQ LAAEELLKAV GAERVSVVTF ENNQAIWKTT VPRMKINLPR LLPEAPIFVH
     LRESLGVFNT DDAHNEGDVV PLKDMLGEET TALMVISIPS GQNLAGLLFA QSTGAAHFSP
     VEIELARTIV NQVSISLDNA RLYQSNLQTA NRLNLLHETS SEVSSHSEAD EIYLSVHKAA
     EKLMRVDSIA IGLLVEQSGE IEGVYLVEGK MRSLPIRVSK ERGLNGEVIR TGQSILLNDR
     AKIQAAGGRG FGKSEDGQSM ILVPMMAGGK VRGVLSVQSS EPGAYSNEDQ QILGTLANQA
     IVGIQNEQLL TETRRLTQEL DGRVTERTSQ LEHDQHHTET LLKILTEVSS SLDLDRALNR
     TLSLLNNTIG AEQGTIMLLH PEDNLLHFQA GYGYVSERSD IASRNLTLKI GEGLAGWVVR
     NRQPALVGDL HADPRWLKSS EGIDHRSCIA IPMIVGDDVI GVLLVFHRAV NYFNPDMQNL
     VKAVAAQVAV AINNAHLYEL IRDQADRLGV MLRKEQEDAS RSQAILAAVA DGVLVTGANN
     QISFINPSIE RILHVEKSKL LGSPLDSFAG LFGKSSGAWM TTIRRWSEEP SIYQAGDTYA
     EQLELEDGRI ALVHLAPVIM ENEFLGTVSI FSDITQQVEV DKMKSEFVST VSHELRTPMT
     SIKGYVDLLQ MGAAGALNDN QEHFVDIVSN NINRLNMLLD ELLDISRFEA GHVIITPAAV
     DLVHLAEEAV IKIKQRSEKE NKPMTIKLAI EEDLPQIIGD AQHVRTILNH LLDNAYNYTP
     ENGVISVQII SGEQDDVQVD IKDNGIGIPT ANQEQVFERF WRGDDERVLA TPGTGLGLPI
     VRQLVEMHKG KIWLKSLGVP GEGSVFSFTL PKHVARDRKA DMRTARLYGE GEDMFIPPKD
     PPRDMGTPGA SSS
//
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