ID A0A1F2RC51_9BACT Unreviewed; 961 AA.
AC A0A1F2RC51;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A3H95_04055 {ECO:0000313|EMBL:OFV93391.1};
OS Acidobacteria bacterium RIFCSPLOWO2_02_FULL_64_15.
OC Bacteria; Acidobacteriota.
OX NCBI_TaxID=1797181 {ECO:0000313|EMBL:OFV93391.1, ECO:0000313|Proteomes:UP000179236};
RN [1] {ECO:0000313|EMBL:OFV93391.1, ECO:0000313|Proteomes:UP000179236}
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:OFV93391.1}.
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DR EMBL; MEKS01000014; OFV93391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F2RC51; -.
DR STRING; 1797181.A3H95_04055; -.
DR Proteomes; UP000179236; 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 CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF13492; GAF_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 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 129..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 598..645
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 671..727
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 740..951
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 961 AA; 105252 MW; ECDEA985720B3793 CRC64;
MAEPVEARWL VWGRSGLALA VAVLLAALGV ANIATFARPH DVEDGVLWRA RAGAVTALDL
AAESAAARAG LERGDILLAV NGSPVRTAAD VIEYQRAGRD GTPLTYTIQH LGTRRTVDVV
LAPIPQASSM YFVLAAVGLF TLVVGASVRL RRPRDQATLH FFWLSVVFFG AFTFSFGGSF
DRLDWIFYWG DALTTALLPP VLLHFTLVFP HRRVATGASR FLVPLIYLPA LALAVLRIAA
VVQGSSDGPL FSRMIDVLDR TELVYVFLCA GTAFFVLARA FREITSVTAE RQLRWIWWGT
ALGVGPFALG YALPWALGAD PPFALQLTAV PLGLVPLTFA CAIVRYRLRD VEVIAKRGLV
YAVFGLASLA LYVALLKATD FVFANDSASH NWVIAVLATA VVVLLAQPVR EALQNALDRV
FFYRDRYDYR RALVAFARDL NTDLDIVHLS QRLVSRVVET LVVDRMALML ADERSGDFEA
IGSHGFTQAV PALERSSSFM MRLDASRTVA LDDPIAAARF TAEEVEAWRD AGIYYFVPCL
FEGRAIAVLA LGRKADDEPF NSEDLALLTA VAGQVATAIE NGRLYRQLHL KAEELGRLRE
FNENILESLD NGLAVFDPNE RIVRWNRALE EIYGIRREEA VGRTLGEMFD QAFVEALAAA
RREYPHGATL HRVPLQRRKG EDGRASRMLV NATEVPLQDP AGRVVAGTIL LVEDITDRVR
LEEQLQISEK MASIGVLAAG VAHEVNTPLT GISSFTQMLL EGADQSDPKT ALLEKIEKQT
FRAAKIVSGL LNLSRPGGTG NEHIDVDLNA VISDVFSLIE HQFEVGRIKI RRELAPTEVR
VVGAEQQLQQ VFLNLFLNAR DAMPKGGWLS VSTRVEDDLV VAEVADTGSG IPSEHLARIY
DPFFTTKAAG RGTGLGLSIT YGIVREHEGM IRCDSAIGKG TRFTLTLPRA AAERTQGAAR
M
//
