ID A0A1G0PIG4_9BACT Unreviewed; 1068 AA.
AC A0A1G0PIG4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-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=A2068_01410 {ECO:0000313|EMBL:OGU35403.1};
OS Ignavibacteria bacterium GWB2_35_6b.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798424 {ECO:0000313|EMBL:OGU35403.1, ECO:0000313|Proteomes:UP000178800};
RN [1] {ECO:0000313|EMBL:OGU35403.1, ECO:0000313|Proteomes:UP000178800}
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:OGU35403.1}.
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DR EMBL; MGZW01000105; OGU35403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0PIG4; -.
DR Proteomes; UP000178800; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF02518; HATPase_c; 1.
DR Pfam; PF07494; Reg_prop; 10.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 795..813
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 851..1068
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1068 AA; 122062 MW; 5937BC4C95C35BA0 CRC64;
MFLSVTYSEP HKYQFEKISV EHGLSQSIIL NIFQDSKGFL WISTQEGLNK YDGYKFIHYK
NEPGNNNSLS DNYVRTVLED TDYNLWITTD EGGLNKFDPE NETFTRFTHD EKNPNSIVDN
NTTAMVSDNS GNLWIGTNYN GLDYFDKRTE KFFHYRKDKT KNNALLDNHI TALYYDVDDK
YLWVGTYGGL NILELSTGKF IDLNKFLFTK GITENRWIRK IHRDRNSNIW IATDAAGLFK
INNFSSHENL SPKNITQFTH KPGINGSISG NSINAICETS SGEIFIGVWG GGLNKVIENK
TTGQITFQAW LNNPEEQGSL TENDINFLME DNAGVLWIGT YGDGLNKLSP HSLNFVHYKN
NPFTKNSMPD NHVTAVLEDE NDVVWIGTWK GLTKLDKKKN IFTHYKLSDD RITSIIKDRT
GNLWIGTLNK GLNRFDKNTG AFVTFVSDPQ NRQSISSNRI LSLLEARNGK IWIGTYYSGV
TIYDPAENSF TKLDTDSLEN FDNRINKLYE DNEGNIWIIT YRGIYKHYPV ENFTRNIKLK
NGKSENSFST GALNIIQDKQ NNFWIGTFGD GVYKLNYSPG ANSYPFTQYS LANNYVYGLQ
FDAADNLWVS TRNGLAKFNS AKATFDSFTN YEGVEFQEFL EGSFYNKQNG NLYFCSMQGL
LEFNPANIKV HYSQPQIEIT QLKIFNKPVK LGLLRKINTA DNSENITLGY NQNSISIELS
ALNFTAPQSI NYEYKLEGFD ETYIPADIET RTATYTNLPS GEYIFKIKAR LGAHQQWDYE
KHIYITVVPP FWETAWFRIL SIILFLFILY IIYSIRTISI RNRNEELQKE VKLRTKELEE
LNSAKDKFFS IIAHDLKGPF SYLLSNSEFL AKEINTIGKE DAGFLSANIN LATRNIYNLL
ENLLQWSKFQ MMGIKPEPEK IDLTQLITNN YELFKPHAEQ KKISITKNIQ PGITIFSDEN
IINTILRNLL MNAIKFTREE GSIQITSEKN NGNIIIRVSD TGIGMSRTQI DEILFGDSVV
SSQGTKNEKG TGLGLYLIKE FIEALNGQLK IESAKNKGTI VTCIIPAE
//
