ID A0A1G0SIZ9_9BACT Unreviewed; 697 AA.
AC A0A1G0SIZ9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2V93_02100 {ECO:0000313|EMBL:OGU72368.1};
OS Ignavibacteria bacterium RBG_16_34_14.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798433 {ECO:0000313|EMBL:OGU72368.1, ECO:0000313|Proteomes:UP000176348};
RN [1] {ECO:0000313|EMBL:OGU72368.1, ECO:0000313|Proteomes:UP000176348}
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 -!- 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:OGU72368.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MHAF01000132; OGU72368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0SIZ9; -.
DR STRING; 1798433.A2V93_02100; -.
DR Proteomes; UP000176348; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:UniProt.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 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; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..311
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 354..406
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 432..484
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 495..688
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 697 AA; 80345 MW; 6C285E9B0E15C9AA CRC64;
MAYKENKPFD QAVRTLSSAL FKRGRALAWL TLIISLSITA YGWYSIKDSI DKEAKEKFDL
QTNEISNSII KRMRDYEQVL RGCLGLFNAS DEVTRKEWEN YVNSLEINES YPGILGMGFS
KVIKNVDKEK HTNQIRKEGF PNYKIWPEGI REIYTSIIYL EPFNEKNQRA FGYDMFSEPI
RRKAMETARD YGKVSVSGKV TLVQEFGEII QAGFLMYLPL YDKKMLATTP KESEKALIGY
VYSPFRMNDL MEGILIDQFK YIELEIFDDR KISNENLMYT SQVKSNSDNF ERNFFKKYKS
ININGRDWAL RLTSLPGFEA VTDRQKPLII LILGIVVSSL LFIIARNLGN IFIINKKLEQ
LLELTAEGIY GIDNRRRCTF INDSGAKMLG YEPEECLQKN MHELIHHHKE NGEIYPFYDC
PILESMEIKK GLSADSEVYW RKDGTCFPVE YSSYPIIDNG ETAGAVIAFN DITERKKAFE
QIESSLKEKE VLLREIHHRV KNNLQIISSM LNLQTNYITD KKSLAIFEES RNRVRSMALI
HEKLYQNESL SSLNIRDYVI ELVNNLMRSY RTDNRINSEI NISDIFINTD TAIPLGLIIN
ELVSNSLKYA FPDERRGKIT VSLIKFIGEK FQMIISDDGI GLPENFDMKS TNTLGLQLVS
SLVIQLDGEI ILTNQTGTKF EINFKGLNLK SSKNKSA
//
