ID A0A177I0G7_9ACTN Unreviewed; 847 AA.
AC A0A177I0G7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=kdpD {ECO:0000313|EMBL:OAH16583.1};
GN ORFNames=STSP_00360 {ECO:0000313|EMBL:OAH16583.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH16583.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH16583.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-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:OAH16583.1}.
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DR EMBL; LOHS01000010; OAH16583.1; -; Genomic_DNA.
DR RefSeq; WP_067270343.1; NZ_LOHS01000010.1.
DR AlphaFoldDB; A0A177I0G7; -.
DR STRING; 1716141.STSP_00360; -.
DR PATRIC; fig|1716141.3.peg.42; -.
DR OrthoDB; 9806130at2; -.
DR Proteomes; UP000077381; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR InterPro; IPR006016; UspA.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR Pfam; PF00582; Usp; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000077381};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAH16583.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 380..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 459..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 622..832
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 847 AA; 91015 MW; D43701413862B1A2 CRC64;
MGRGKLRIYL GAAPGVGKTY AMLSEAHRRV ERGTDCVVAF VEHYGRPRTE VMLHGLEQIP
RKELAYRDTA FTEMDVDAVL QRAPAVALVD ELAHTNVPGS RNDKRWQDVE ELLAAGIDVI
STVNIQHLES LGDVVESITG VRQRETVPDE VVRRADQIEL VDMSPQALRR RMAHGNIYKP
DKVDAALSNY FRPGNLTALR ELALLWVADR VDEYLQEYRS AHHVSKIWGS RERIVVGLTG
GPEGRTLIRR AARLAEKGAG GEVLAVYIAR SDGLTSASPK ELAAQRTLVE DLGGTFHHVI
GDDIPSALLE FARGVNATQI VLGSSRRKAW QYVFGPGVGA TVARESGPDL DVHIVTHEEV
AKGRGLPVAR GARLGRSRII WGWLAGVAGP ALLALLLTHI EADLGLANDM LLFLALTVAA
ALLGGLFPAL ASAAVGSFLL NWFFTPPLYR LTIADPRNIV AIFVFFAVAV SVASVVDLAA
RRTHQAARLR AESEILSFLA GSVLRGETTL DALLERVRET FGMESVALLE RESDVAPWTC
AGSVGPRSLV GRPEEADVDV PVGDHMALAL SGRVLPAEDR RVLAAFAAQA AVILDRQRLE
SEAEQARALA EGNRIRTALL AAVSHDLRTP LAAIKAAVTS LRSDDVAWSE EDQAELLEGI
EEGADRLDHL VGNLLDMSRL QTGTVTPLIR EIDLDEVVPM ALGGVPEDSV DLDIPESLPM
VAVDPGLLER SVANIVENAV KYSSGQRVLV AASALGDRVQ VRVVDRGPGV PDEAKERIFE
PFQRYGDAPR GTGVGLGLAV ARGFAEAMGG TLDAEDTPGG GLTMVLTLQA AAVRPQYGPY
LPAEAAS
//
