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Database: UniProt
Entry: A0A117RDG8_9ACTN
LinkDB: A0A117RDG8_9ACTN
Original site: A0A117RDG8_9ACTN 
ID   A0A117RDG8_9ACTN        Unreviewed;       485 AA.
AC   A0A117RDG8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AQJ64_14600 {ECO:0000313|EMBL:KUN84721.1};
OS   Streptomyces griseoruber.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN84721.1, ECO:0000313|Proteomes:UP000052982};
RN   [1] {ECO:0000313|EMBL:KUN84721.1, ECO:0000313|Proteomes:UP000052982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN84721.1,
RC   ECO:0000313|Proteomes:UP000052982};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT   for the species Streptomyces griseoruber.";
RL   Submitted (OCT-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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:KUN84721.1}.
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DR   EMBL; LMWW01000016; KUN84721.1; -; Genomic_DNA.
DR   RefSeq; WP_055636698.1; NZ_LIQS01000407.1.
DR   AlphaFoldDB; A0A117RDG8; -.
DR   STRING; 1943.AQJ64_14600; -.
DR   OrthoDB; 9786919at2; -.
DR   Proteomes; UP000052982; 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:KUN84721.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          203..257
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          272..481
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   485 AA;  52764 MW;  CFF5BBAF10F78271 CRC64;
     MRRPRALRCG RGMHSLRVKL TLANVALLAI GIVAATAVSL MGMRHYLMDQ IDAELVKTRD
     SIAGTGLTLR KLDSLSALSF LRDRMVPGES DEESTADTVF TAVDATGRAV SLFGVPPTAA
     QSDLADAVRD PHALALKADP GDISMRGAAY RVTATRLGDG TYVLMATSTE ALRQGITKAL
     KLDLAVGTLL LALLACLTLF SVRRRMRPLE DMVETSSAIA EGDLTRRVPS SRETSLEVEQ
     LRLALNSMLH QVEAAYRTRE RSAGQLRRFV ADASHELRTP LSAIRGYLQL YDQGMLREPE
     ERKRAWDRMN GEVDRMGRLV DELLTLARLD QRPELRLRNV DVSRLVRDAA EDLRAQQPDR
     PVTVHADGTL LVRADESGLR QVLGNLVANV RTHTPTEVPV RLRVERVDGV VRLSVRDEGP
     GLAAEDAARV FDRFFRAGGG AGSGLGLAIV QGVVRAHGGE VSVRTAPGEG LGVTVELPTR
     PKSCV
//
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