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Database: UniProt
Entry: A0A252EBX3_9NOSO
LinkDB: A0A252EBX3_9NOSO
Original site: A0A252EBX3_9NOSO 
ID   A0A252EBX3_9NOSO        Unreviewed;      1128 AA.
AC   A0A252EBX3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-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=BV372_03160 {ECO:0000313|EMBL:OUL37237.1};
OS   Nostoc sp. T09.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1932621 {ECO:0000313|EMBL:OUL37237.1, ECO:0000313|Proteomes:UP000195076};
RN   [1] {ECO:0000313|EMBL:OUL37237.1, ECO:0000313|Proteomes:UP000195076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T09 {ECO:0000313|EMBL:OUL37237.1};
RA   Cruz-Morales P., Corona-Gomez J.A., Gutierrez-Garcia K.G., Barona-Gomez F.,
RA   Cibrian-Jaramillo A.;
RT   "Metagenomics of subcommunity co-cultures reveals the complexity of the
RT   cycad coralloid root endophytic microbiome.";
RL   Submitted (JAN-2017) 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:OUL37237.1}.
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DR   EMBL; MTAV01000006; OUL37237.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A252EBX3; -.
DR   OrthoDB; 9809348at2; -.
DR   Proteomes; UP000195076; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 4.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 5.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 5.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 4.
DR   SMART; SM00091; PAS; 5.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:OUL37237.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000195076};
KW   Transferase {ECO:0000313|EMBL:OUL37237.1}.
FT   DOMAIN          206..258
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          333..385
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          389..431
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          461..513
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          535..579
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          661..893
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          928..1041
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1049..1128
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          504..535
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         977
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1098
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1128 AA;  127060 MW;  0CB526E921F50CA8 CRC64;
     MSSQEEYNRQ LLEKCPVGLV LCRIDGTLID INPAYAAILG RTVPESLNLS YWQMTSENYT
     VKQAILENLE RTGRYGPYEQ EYIHKDGHLV PVRVSGQIIE QDGQKLIWSS VEDISDLRRA
     QLEHQHSEKI LKQSEARYRS LIKTNTQIIW VSTPEGICFE LKDWIAYTGQ TLAEAENGGW
     IEAVHPDDRG YTGEAWSIAV ANLSQYQIEY RIRGKDGNYR YFWVWGAPVI EEDGSVREWI
     GTCTDIQDRK LAEAENQRLK ERYRSLVTAT SQIVWGATPE GLGISSEMLT WIAYTGQTEE
     EVAGWGWIDP IHPDDRPHSF EAWSTAVANR SIYETEYRLR GKDGTYRYFS VCGAPVLEED
     GSIREWIGTC TDIHERLAAL RERKLAEAEN QRLLDMLNHC SDAIIVRDMS DKILYWNQGA
     ERLYSWMREE VKDQYIYKFI KKTFPKPKEL IVAELLEQGN WEGEVQHLTH DGIQITVQSR
     WTLQRDIDGQ PSAILEINTD ITARKQAEIA LRQLNQELEA RVAERTAALQ NTLAEAQGLN
     AILDNLADGL LVTDITGQIT HFNPAFIAMH GLTATAINGH YRELPISGLA NLIEQTQSHP
     QEVFAAEIAL AKERIGQAVA TAIFKKAVEN EPAACFGSAL LIRDITAEKE VDKMKTDFIS
     TVSHELRTPL TSVLGFASII KEKLETDVFP IISTEDRKLQ KTIKRVGDNL TIIVSEAERL
     TSLINDVLDI AKMEAGKVEW QMQPLDPTEL LDWATTSTSA LFETNGLQLV SEIEPGLPQI
     VGDRNRLLQV LINLISNAVK FTKSGSVTCR IKQRNDGVCI SVIDTGIGIA PEDQPKVFEK
     FRQVGDTLTD KPKGTGLGLP ICKQIVDHHG GRIWVESEPG KGSTFSFLIP TYTSDRKAST
     NLNLDALVKQ LKEHVITTNT VLNENRKTIL VVDDDVNIRE LLRQQLENEG YNVREAKDGM
     DAIHQIKTNR PDLILLDVMM PQINGFDVAA VLKNDPHTAD IPIIILSIIE NKERGYHIGI
     DRYLTKPINT EQLRNEIGSL LSQGTSSKKV LVVDKNASTL KTISDVLQTQ GYSVIEASNP
     QECINKALSA KPDMIIIDSI FSQEADLVKT LRFEKELENV FFIMLSDR
//
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