ID A0A1Q5JJ80_9ACTN Unreviewed; 515 AA.
AC A0A1Q5JJ80;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AMK29_02870 {ECO:0000313|EMBL:OKJ69388.1};
OS Streptomyces sp. CB02261.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703940 {ECO:0000313|EMBL:OKJ69388.1, ECO:0000313|Proteomes:UP000186742};
RN [1] {ECO:0000313|EMBL:OKJ69388.1, ECO:0000313|Proteomes:UP000186742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02261 {ECO:0000313|EMBL:OKJ69388.1,
RC ECO:0000313|Proteomes:UP000186742};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ69388.1}.
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DR EMBL; LIVX01000001; OKJ69388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5JJ80; -.
DR Proteomes; UP000186742; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 1.20.5.1040; Sensor protein qsec; 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; 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 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:OKJ69388.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 239..291
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 306..515
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 55738 MW; 492F51E57B0626A0 CRC64;
MRACVSPEPD TGHRHQSQSQ AEDAGGPGRA LRRKARAPRL RPHPFGLRTR LVLAFLLVAA
VGCGTTAALT YRAARNAILE QTQDTAVSAF REQVDSLGIA LPVEAEQLRT SLLHIARQGK
PRPWRVYAEY GTLRVSSTDR PTSSVITPEL RDRATDQTTP HGSFQRVVKG GTPYLTIAVP
AVFHARSAAG APQRTGLVLY AVMDLTEEEA NIEAMVTAAR DGALPALAIA LIPALIAARG
VLRPVRELRH AAHSMGRGRL DTRIHAKGSD ELADLARTFN ESAAALERSV AELRSAEARA
RRFASDVSHE LRTPLAGMLA VTEVLDEDAG TLDSDTARAV RLISAETGKL AVLVEDLMEI
SRFDARAAEL HTDEVDAADC VRKTLQHRYW TDPEQVVPYL TEGIRARLDP RRFDVVVANL
VGNALKHGGA PVTVRLYVEG DELVTEVADR GPGIHPDVLP HVFDRFYKAD QARTRSAGSG
LGLAITRENV RLHGGTVTAA NHPEGGAVFT VRMPL
//
