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Database: UniProt
Entry: A0A1Q5RAT9_9BRAD
LinkDB: A0A1Q5RAT9_9BRAD
Original site: A0A1Q5RAT9_9BRAD 
ID   A0A1Q5RAT9_9BRAD        Unreviewed;      1142 AA.
AC   A0A1Q5RAT9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AC629_37340 {ECO:0000313|EMBL:OKO72822.1};
OS   Bradyrhizobium sp. NAS80.1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1680159 {ECO:0000313|EMBL:OKO72822.1, ECO:0000313|Proteomes:UP000186592};
RN   [1] {ECO:0000313|EMBL:OKO72822.1, ECO:0000313|Proteomes:UP000186592}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAS80.1 {ECO:0000313|EMBL:OKO72822.1,
RC   ECO:0000313|Proteomes:UP000186592};
RA   Granada C., Sant'Anna F.H., Passaglia L.;
RT   "Genome of Bradyrhizobium sp. NAS80.1.";
RL   Submitted (JUL-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:OKO72822.1}.
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DR   EMBL; LGHL01000228; OKO72822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5RAT9; -.
DR   OrthoDB; 9801651at2; -.
DR   Proteomes; UP000186592; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 3.
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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:OKO72822.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:OKO72822.1}.
FT   DOMAIN          776..846
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          920..1139
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          470..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..508
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1142 AA;  121746 MW;  B7541C635C58A75B CRC64;
     MSSSDFQLRG VGDPRLAVHA TSPLPAWLWS IDGTRVLWAN PVGVRLFRAA NAAALAAKTF
     GPADPHRRQV AQLGRRLPAG GAVRLERLRG FGASLGTLMT CACARLDFAD GGHFTERSGV
     LVTALDPAGR TMPLVERLHR LVEGAKVPMA AFAPDGLFVG ASEAARPLLG FRDLGEAGLE
     QARSDALAQG RAETPIGIGQ MVLRRVGQGA DIGLVALIEP AVQQAAPATT TDAASDATED
     TVREDVARED VAAPAPEAPF PAAVPDHAQP ALPDKAPSEF TLVDPFAEPV ETPYTAATIE
     AAPESPVENP PEAIVSPQAR PITTGMVDRP SAEPPAPRQH PLRFLWQMDA EGRFVLGSDE
     FIRLMGAHTA AGFGRPWREI ADEFSLDPDG RIAQALASHD TWAGITVNWP ADGGEHVPVE
     LAGLPIYDRE RNFVGFRGFG VCRDLDALNR LDALRRFELF VEPPAQHALS ADVVEPKSEP
     ESELEAEPLE ETPLAEAPPP PIEPPAPETE PETKAETEAE LPEPVTEANS HPTDPETPVE
     TPPNVVPFRA PGDQRSPTLT PVENSAFNEL ARQLSERLER EQETIASVTS EPPAAEITPE
     PLTPEHEAPP APAEWLTEPA TPAHGHSARD RTLLDLLPSG ILIYRLDRLL YANPAFLARM
     GYASLGALED AGGLDALYVE PGVSPTSSTS QAGTPVTISA TVADGERPLA TTEAHLHTID
     WDGESAHALI CALPKATTVI AAPAVAAPVF VETVVTETLA TIPGAPEPEP EAGDADAEDL
     AAILDTTAEG IVMFDAEGNI HACNRSAEAL FGYDGEELLQ QNLTTLFAPE SQHVVVDYLE
     HLKGQDIASL LDHGREVLGR EKKGGVIPLA MIMGRTRPDG PNFFAVFRDL SQSKKGESEL
     KQARRLADGA ANAKADMLAR ISHEIRTPLN AIIGFAEVMI SERFGTLGNE RYGEYMKDIR
     ASGERVIAII DDLLELSRIE TGKLDLNFSN LNLNDLVEAC VTVMQPQANR ERIIIRTSLA
     HALPQVTADA RAMRQITMNL ISNSIRLASA GGQVIVSTAL TDRGAIALRI RDTGHGLSER
     EVAAAMEPFC TPPPGDASDS SALSLSLTKA LVEANRAQFN IKSAANSGTL IEVVFAQALA
     KA
//
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