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Database: UniProt
Entry: A0A3Q8VCN1_9ACTN
LinkDB: A0A3Q8VCN1_9ACTN
Original site: A0A3Q8VCN1_9ACTN 
ID   A0A3Q8VCN1_9ACTN        Unreviewed;       447 AA.
AC   A0A3Q8VCN1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-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=DLM49_15890 {ECO:0000313|EMBL:AZM60843.1};
OS   Streptomyces sp. WAC 01438.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2203204 {ECO:0000313|EMBL:AZM60843.1, ECO:0000313|Proteomes:UP000271045};
RN   [1] {ECO:0000313|EMBL:AZM60843.1, ECO:0000313|Proteomes:UP000271045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC 01438 {ECO:0000313|EMBL:AZM60843.1,
RC   ECO:0000313|Proteomes:UP000271045};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) 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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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DR   EMBL; CP029601; AZM60843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q8VCN1; -.
DR   OrthoDB; 9786919at2; -.
DR   Proteomes; UP000271045; Chromosome.
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   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
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; 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:AZM60843.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271045};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          170..226
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          234..436
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   447 AA;  47844 MW;  5C0B7EAA083EDA8C CRC64;
     MRGGYFRDLV AAGVRRAGIG AGLRWKLSAA IALVGALVAI VLSLVVHNAA RVSMLDNARD
     LADERIMIAQ RNYEMSGRLN FPNTKIDDPQ LPPELRERVE AGRRATYVAD RSGSPDIWAA
     VPLKNGHVMS LHSGFTDRSS DILQDLDQAL VIGSIAVVLG GSALGVLVGG HLSRRLRKAA
     SAANQVAKGE TDVRVRDSIG GVVRDETDDL ASAVDAMADA LRQRLEAERR VTADIAHELR
     TPVTGLLTAA ELLPPGRPTE LVLDRAKAMR TLVEDVLEVA RLDSASERAE LQDILLGEFV
     ARRVAAKDPD VTVQVVHESE VTTDPRRLER VLFNLLTNAA RHGKPPFEVT VEGRVIRVRD
     HGPGFPEALL AEGPSRFRTG SADRAGRGHG LGLTIAAGQA RVLGARLTFR NVRPAGAPEG
     VPAEGAVAVL WLPEHAPTNT GSYPVLA
//
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