ID A0A1F3KAZ4_9BACT Unreviewed; 1097 AA.
AC A0A1F3KAZ4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A2W98_07295 {ECO:0000313|EMBL:OFY25107.1};
OS Bacteroidetes bacterium GWF2_33_38.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797342 {ECO:0000313|EMBL:OFY25107.1, ECO:0000313|Proteomes:UP000177621};
RN [1] {ECO:0000313|EMBL:OFY25107.1, ECO:0000313|Proteomes:UP000177621}
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:OFY25107.1}.
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DR EMBL; MEOF01000006; OFY25107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3KAZ4; -.
DR STRING; 1797342.A2W98_07295; -.
DR Proteomes; UP000177621; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF07494; Reg_prop; 10.
DR Pfam; PF07228; SpoIIE; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 790..807
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 719..781
FT /note="Two component regulator three Y"
FT /evidence="ECO:0000259|Pfam:PF07495"
FT DOMAIN 895..1094
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|Pfam:PF07228"
SQ SEQUENCE 1097 AA; 126111 MW; EA1B0E99674FB257 CRC64;
MSFNSIFLYS QKPSITFERL GIDQGLSQSS ANCILEDENN FLWIGTQEGL NKYYGQNFCF
EIFKHDLVDT NSISDIWVYD IAQDKNGNIW IATRYGLNML NPKTRKIKRY FQDINEISSL
YNNEVFSVFV DSKGGVWVKT NDVLSLLDTT SGKFTHYEHY VNYFNTRSQT RFPIIEDKNG
LIWYGTVDGL NSFDRNFEQS KRYKFDSANP FSLSNNFVTA IFEDSKGTLW VGTQDGLNKF
NKKKKTFERY YNIPGNENSL VNNSVKAIVE DNNGMIWVGT DGGLSILDLG NNKFYNYRNQ
ANNPTGLSNN EILSFYKGSS DIIWIGTNGG GINKVDLKRK KFEIYRREAG ENTLNFSSNV
IASFFIDRDS LLWVGTYGEG LNIYNRKTGH IDIYSKSTNP AIVDDYVHAI GEDSDGKIWI
GTRNGINIYD QEKKTFSLIQ DYIPTTAKHL NLNSNRIYYF LEDRNKNMWI ASERGLIKIN
VKTEDIKIYR KNFRDSLSLC DDRVYSIIED NEGFLWIGTT NGLNKYDPKK DVFYQYKSKL
NSVNTISHNT IYSVFEDSEG IIWIGTAGSG LNKYDKKSDT FVYYTEKNGL PNGTIYEIEE
DNNGDLWFST GRGLAKLDKK TNTISSFTND DGLQGLEFNN GANFKSKDGE LFFGGTNGFN
SFYPELIKYN ENKPKTVFTY FEKTSTDGGL SRMYLDDIKE IHLSYKDHTF KIFFAALEYT
KPEKNSYMYM MENLKDEWIS LGTQSFKTFS NIPPGEYIFH LKSSNNDLVW NEEPISIKII
IEPPFWQTKW AYVLIILIVV GSIYYFIEVR TRKLKAANHI LREKQSAALE IARQKEELTV
KNKNITDSIN YAKRIQEAMM PSEYLFNKLL PESFILYKPK DIVSGDFYWI TEKNNKIFVA
AVDCTGHGVP GAFMSIIGFD LLRNITKEQG VEEPAQILNL LNEGVTETFV KNADNQQVKD
GMDIALCVYD KENSVVEFAG ALNPFFLIRD NDIISIRGNR FSVGMVDKGV QHKFEKHVIP
VKEGDVIYIF SDGYADQFGG PFGKKFKYSR FRQLLLTVHS LPMRKQKAFL DENIISWMGE
LEQVDDILVI GFRINKL
//