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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//