ID A0A136K8D0_9BACT Unreviewed; 673 AA.
AC A0A136K8D0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=UZ03_NOB001000793 {ECO:0000313|EMBL:KXK05661.1};
OS Nitrospira sp. OLB3.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1617410 {ECO:0000313|EMBL:KXK05661.1, ECO:0000313|Proteomes:UP000070691};
RN [1] {ECO:0000313|EMBL:KXK05661.1, ECO:0000313|Proteomes:UP000070691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB3 {ECO:0000313|EMBL:KXK05661.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KXK05661.1}.
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DR EMBL; JZQY01000029; KXK05661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136K8D0; -.
DR STRING; 1617410.UZ03_NOB001000793; -.
DR PATRIC; fig|1617410.3.peg.802; -.
DR Proteomes; UP000070691; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KXK05661.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:KXK05661.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 34..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 371..591
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 306..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..613
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 73696 MW; BFEA8556727FA63E CRC64;
MTRFHQKPNP ILSIALVLSI AAVFVSEFYT KLGITVWVVY LIPLVLSYLT WNPLVPVAVG
SIASLLILIG LVISPVGIDP SLSLINRGMG AGTALALAAF GHQFIRGRLA VRKEEWVRMG
QTKLSERMMG DQSLRTLGEN ILQGLAEYVG AQGGAIFIDD GFGFHRTATF GVPEGAALPE
RFQVGDGLLG HALQQKQTIV VQDLPDGYFT IGSALGRSAP RHLLITPLGA DGVINTVLEL
GFFHRVHDSD KELLGRLAES IATAVRGARY RNRLQELLEE TQRQAEELQV QSEELRVANE
ELEEQSRALK ESHGRLEQQQ AELEQTNSQL EEQAQLLEGQ KDELSNAAAI SEAQKRQLER
VSRYKSEFLA NMSHEMRTPL NSTLILAKLL ADNPQGNLTP EQVKSAATIE SAGHDLLTLI
DDVLDLAKVE AGRIDLTPGQ VSLQRLIDSL HALFQPLATQ KGLQLQMRRA PGTPESIETD
WQRLEQVLKN LLSNAIKFTE AGRVSLDIAH LPDGRLAFAV EDTGIGISPD QHDLIFEPFC
QGDGTTNRKY GGTGLGLSIS REFVRLLGGD IHLASTPGQG STFTIHLPQR IPSSPPLRSA
PMASSPLPCE PPAPHARVSF GRSARERQRP ADRRRSGTAR RPSPRDPDRR GRRGLLSHPC
GPGPRDELQC AHR
//
