ID   A0A0M8YF94_9PSEU        Unreviewed;       809 AA.
AC   A0A0M8YF94;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ADK67_20530 {ECO:0000313|EMBL:KOX23531.1};
OS   Saccharothrix sp. NRRL B-16348.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX23531.1, ECO:0000313|Proteomes:UP000037722};
RN   [1] {ECO:0000313|EMBL:KOX23531.1, ECO:0000313|Proteomes:UP000037722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX23531.1,
RC   ECO:0000313|Proteomes:UP000037722};
RA   Noorani M.;
RL   Submitted (JUL-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:KOX23531.1}.
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DR   EMBL; LGED01000198; KOX23531.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8YF94; -.
DR   STRING; 1415542.ADK67_20530; -.
DR   PATRIC; fig|1415542.3.peg.4434; -.
DR   Proteomes; UP000037722; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR013587; Nitrate/nitrite_sensing.
DR   PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR   PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08376; NIT; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KOX23531.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:KOX23531.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        319..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          529..641
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          646..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..680
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..752
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..809
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  89204 MW;  E0E5AA1AB3177C35 CRC64;
     MRSAVKQKST TETNYKTIRS RLTGVVVVPS IVLLIMWALF SSYTLFDGFY LRAVASGVKD
     ASIPAVQTFA ALQKERELSM TALSQPGLGT SNLEVQQAET DRAVVGMRTA FDELASQAPQ
     EIVDKINALN VLLDQLPQRR AALEAERASK TEIYTYYNSL LDAGDALFSV QARVVPDHES
     VKGAITAEEY FKAADWMSRA TSLASSALAA EQFTPEEHIE FANLVGAYHS SYDSIAPYAQ
     PEVREHYQFM IEGDQWKRLV EFEGRLIQNG PDPLNAGSLQ EWQNISGPIS DELVALVSEQ
     ASSAVNVTMG RGESKFRTVL IGSLVALLAV IIGILIAIRT SNRLVNRALI TRLTALKKDS
     LTLAHERLPD IVDRLREGKH VDVEVEVPPL DYGSDEIGQV ADAFNAAQYT AVAAAVKESQ
     AREGVNRVFL DIAHRNQGLV HRQLKILDKL EREEENPEQL DALFQLDHLA TRARRNAENL
     IILAGEQPGR QWRKPVRLLD VLRAAVAETE QYVRVKVNPV PDTALVGAAV ADTIHLIAEL
     VDNATAFSSP RSQVQVHASE VPQGIVVEIE DHGLGINPED REQHNAMLAD PPEFDAMRLR
     GESRLGLFVV ARLAARRGIH VELRDSPYGG TLALVLIPSA IVAGPTTATE PAETRQLPRR
     SFHDIPEQGD DSVRDARFPD GSRDLEGFWA QAEAAANQDS LPEVERLSGG LDLSQRSGEL
     DLPQRKRATS EWPADEPESA GTADRPELPR RRRQQNLAPQ LVRNDFHPSP EPLPEVDPEK
     SAERVRKGLS AFQRGTRDAR RTPADDLEP
//