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Database: UniProt
Entry: A0A0N0NFI6_9ACTN
LinkDB: A0A0N0NFI6_9ACTN
Original site: A0A0N0NFI6_9ACTN 
ID   A0A0N0NFI6_9ACTN        Unreviewed;       695 AA.
AC   A0A0N0NFI6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=OV320_2474 {ECO:0000313|EMBL:KPI32298.1};
OS   Actinobacteria bacterium OV320.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI32298.1, ECO:0000313|Proteomes:UP000037870};
RN   [1] {ECO:0000313|EMBL:KPI32298.1, ECO:0000313|Proteomes:UP000037870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV320 {ECO:0000313|EMBL:KPI32298.1,
RC   ECO:0000313|Proteomes:UP000037870};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (AUG-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:KPI32298.1}.
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DR   EMBL; LJCX01000005; KPI32298.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0NFI6; -.
DR   PATRIC; fig|1592329.3.peg.1061; -.
DR   Proteomes; UP000037870; 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; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
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; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 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; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPI32298.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037870};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        28..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          398..450
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          458..678
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          296..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..695
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   695 AA;  72943 MW;  E637E922FC995419 CRC64;
     MRRRDERSGR AEPAGRTGRT RLPLRKSLLG RLLTVSALVA SCSVAATAWL AVQTTSVAIR
     QEQGRNLSTD ARIYDTLLGY AAGHPDWAGV DGTVRDLARE SGRRIVLTTE DRQPLLDSAA
     GTAPAAELPT QASAVVDPLS VDTVLVPDAV PVGTDRVDPR AVGPFLLPAK ERTVLRRATA
     RSAECLAGMG IAADVVDSPS GRPWVRFVSD GTDRDRELKC LSVDGAATTA TEERALRALE
     QLADACLKRQ GRTGVKLNLD LSWDRGYGQE GTDVGSSAPV PVPETGISKE EAIERRMAED
     KTAEDKAAED RAAAAGTTDG AAQARGSGYD RAVAACVGSA RREQLTAYVA APALLFIDGP
     GAVSVPGFDL SPANTARIAG VTALVLALTV GASVIAGTRL VRPLHALTGA AQRMRDGLDS
     APVPVGPDNE IGRLALAFND MAAHRTRLEE QRKVMVSDVA HELRTPLSNI RGWLEAAHDG
     LAEPDPAFVS SLLDEAVQLQ HLINDLQDLG AAEAGALRLH LEPVFVDDLL GQVAAAHQGP
     ADTAGVTLEV VTAPGSPPPP PVEADPVRLR QAVSNLLSNA VRHTPPGGRV TLRPYVTKGG
     DEVAVEVSDT GSGIPAGDLP HVFDRFWRAE KSRNRSTGGS GLGLAIVLKL AEAHGGTVSV
     TSTEGQGSVF TLRLPAMTDE DAERPRADEE TAVRP
//
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