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Database: UniProt
Entry: A0A366ZJP1_9ACTN
LinkDB: A0A366ZJP1_9ACTN
Original site: A0A366ZJP1_9ACTN 
ID   A0A366ZJP1_9ACTN        Unreviewed;      1717 AA.
AC   A0A366ZJP1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DQ238_17220 {ECO:0000313|EMBL:RBY76431.1};
OS   Geodermatophilus sp. TF02-6.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=2250575 {ECO:0000313|EMBL:RBY76431.1, ECO:0000313|Proteomes:UP000253027};
RN   [1] {ECO:0000313|EMBL:RBY76431.1, ECO:0000313|Proteomes:UP000253027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF02-6 {ECO:0000313|EMBL:RBY76431.1,
RC   ECO:0000313|Proteomes:UP000253027};
RA   Ennis N., Dharumadurai D., Sevigny J., Hall J., Simposon S., Morris K.,
RA   Thomas W.K., Tisa L.S.;
RT   "Genome Sequence of Geodermatophilus sp. TF02-6.";
RL   Submitted (JUL-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   -!- 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:RBY76431.1}.
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DR   EMBL; QOHF01000020; RBY76431.1; -; Genomic_DNA.
DR   OrthoDB; 163538at2; -.
DR   Proteomes; UP000253027; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd16936; HATPase_RsbW-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17574; REC_OmpR; 1.
DR   CDD; cd07043; STAS_anti-anti-sigma_factors; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 3.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 3.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   Pfam; PF13466; STAS_2; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 3.
DR   SMART; SM00387; HATPase_c; 2.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 3.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RBY76431.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000253027};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          355..573
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          629..744
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          753..823
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1611..1717
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
FT   MOD_RES         677
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1717 AA;  180370 MW;  A456BD14326A5D35 CRC64;
     MTGQAPERSL FAGGGEVGRA MAERDWAQTP LGLPETWPPE LRNVVRIVLT SRFAMWAAWG
     PDLTFFYNDA YRDDTLQAKH PWALGRPARE VWAEIWDDIA PRIRSVLDTG VATWDEDLLL
     FLERNGYPEE TYHTFSYSPL SGPDGRTEGM LCVVTENTER VLGERRMAHL RDLAAAIGTS
     RTEADVLAAV GEQLGRNRAD LPFSATYLVD GSGTARLGCA AGIEPGSPAV PAVLTPDDGD
     PVWPLARLLA GEPVLVEDLA DRFPDLPTGA WDLPPRQAAA LPIASGVQDR GAVAGFLVVG
     LNPHRRSDDA YRGFLELVAN QIASALGNAG SYEAERRRAE ALAELDRAKT DFFSNVSHEF
     RTPLTLIAGP VAELHRSPAA DADPRVREEL EVIERNAQRL RKLVDTLLDF SRIQAGRIDA
     RFEPVDLAAT TAELASVFRS AVVRAGLAFT VDCPPLEAPV HVDRDMWEKV VLNLLSNALK
     YTFTGGITVR LRRDGGTARL TVSDTGTGIP AEELPRLFER FSRVRGARGR SGEGSGIGLA
     MVRELVGLHG GTIDVESTLG AGSTFTVTLL LGAAHLPAER LAEPAPDAPA VSPAAVPFVT
     EALRWLPGDD GDAAGTVAPS PAPGTAAGRV LVADDNADMR EYVLRLLAPR YDVRAVADGS
     SALEAALADP PDLVVSDVMM PGLDGVQLLA ALRADVRTAR VPVVLLSARA GEEAAVEGLA
     AGADDYLVKP FSAQELLARV GAHLQLGRVR RAAEERFTAV ADVAPALIWV ADPEGRRVFV
     NRGWTEFTGR PACEELGTGW EAGIHPEDRD RYARVVAAAT AQRSGWEVDV RLRRTDGAHH
     WLLERAAPIG ADEDFAGYVG SCTDINARTR ETARQTLLAE VGTALDRETT VDGQVGALAR
     LLVDRRLGDI CTVRLVGEDG RLRYAGIAGL DAATEAALAA LDPDAGLARE VLATGRPVRR
     APLPAGWPLR ADAPEGERAE TDRRLGMRSG LVVPLTVRGR VLAVLALARR GDAPPVDDDD
     RVLAEEIAAR AALAVDNAVL LADERAAAHR LALLQRATAE LSAATTPVEV ARAAADHLRA
     LTGPQSRVAV YELDAAHRAL VALAIDGASA AGERAWRVLP LSAPLIATAA VAERRAVWVE
     DVAASPPGAQ LPPELAESAR GFGLAAHVAL PLAVAGRVVG VVAIAWSTVQ RFSATDRGML
     LAVAEQCAQA LDRARLFRAE RGIAETLQRS LLPAQLPRLD RLALAAHYLP GAEGTQAGGD
     WYDVVELAGS RVAIAVGDVV GQGPAAAAVM GQLRSALSAA LLQGCGPAEA LELLDRFAVR
     LPGALASTAA CLVVDAAAGT VRWARAGHLP PLLVTAGGAR LLDGAGSGAV LGAPGRRPYT
     EGSADIAPGA TLLLYTDGLV ERRGELLDDG LGRVCDAAGR YAAADPARLT ARLLAEVLAD
     TDQPDDVALI AARLLPGPLA ERLPADPVRL SAVRRAVARW TAAAGLPEET AEDLQLALGE
     ALANAVEHAY GSDGVAGSSG GGQCSYGVSR DADGGVRVEV RDTGAWRPPP ENRGSRGRGL
     ELISTLATDV EVDHGPGSPG TTVRFRVPPA PVAPGARPPR AAYPAADGGA ARLLVHDEPG
     GLRVQVLGEV DLATAAAVRE EVLGCLDRLP PGSRATLDLR STGHLASAGV GVVLEALTRA
     GQAGVDLRVH TAPATPPARI LALAGVDDSA ARALPLR
//
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