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Database: UniProt
Entry: A0A164B4T2_9BRAD
LinkDB: A0A164B4T2_9BRAD
Original site: A0A164B4T2_9BRAD 
ID   A0A164B4T2_9BRAD        Unreviewed;       748 AA.
AC   A0A164B4T2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A4A58_05085 {ECO:0000313|EMBL:KZD25759.1};
OS   Tardiphaga robiniae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Tardiphaga.
OX   NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD25759.1, ECO:0000313|Proteomes:UP000076574};
RN   [1] {ECO:0000313|EMBL:KZD25759.1, ECO:0000313|Proteomes:UP000076574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vaf07 {ECO:0000313|EMBL:KZD25759.1,
RC   ECO:0000313|Proteomes:UP000076574};
RA   Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT   "Microsymbionts genomes from the relict species Vavilovia formosa (Stev.)
RT   Fed.";
RL   Submitted (MAR-2016) 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:KZD25759.1}.
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DR   EMBL; LVYV01000001; KZD25759.1; -; Genomic_DNA.
DR   RefSeq; WP_068730246.1; NZ_LVYV01000001.1.
DR   AlphaFoldDB; A0A164B4T2; -.
DR   STRING; 943830.A4A58_05085; -.
DR   Proteomes; UP000076574; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 2.
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); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KZD25759.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000076574};
KW   Transferase {ECO:0000313|EMBL:KZD25759.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        55..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          107..163
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          241..459
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          617..741
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          591..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         671
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   748 AA;  81440 MW;  AD1D60B068191BA4 CRC64;
     MAKGVFRIKV YFRRFARRFP WFAFVIRSFV MFSAAFGGAY GFISGSTSKD SGYDPHAFAI
     GASFLFALAC VALATMSIRM RFMGRRMRKL AAHNEALVDR NWELKEAEER ARSLFEAQGD
     LIVIRNSEGC ITFVNDAYCA LAEQSREALI GSRFELTLLE QGDIANEPNG TSMHDQKIAT
     ATGPRWIAWR EGLVRIDAGQ PAELQCVGRD VTDRTQTERA LGEARDHANA ANRAKSRFLA
     MASHEIRTPL NGILGMSGLL LDTPLTPEQT TYAKAVKTSG DALLSLIEEL LDYSKIEAGK
     IDLEHRPFAL AGLIEDITEL LAPRAQARNL EIAAYVDERL PLTVMGDAAR LRQVLLNLAG
     NAIKFTAAGG VALIVEPGIW PNEISFLVRD TGIGIAPDAQ QRIFREFEQA DEGTARHYGG
     TGLGLSISER IIKRMNGRIT LQSELGAGST FEVSVPLAAS DSGTATFMAP DLTSLSVMLV
     APQTIEASLM ALRLGRWGAQ TCTVSDIAVA QALLPERSWH AVMIDRALGA DAAEQLANAA
     IPHALRRIVL FTPAMRHELQ PATPSAFTGY LVKPLRATSL AARLTLQTDS PTIAADDPLD
     RDPATPEPTE AMASSLSILV AEDNEINALL MRSLLTRLGH KPVVTTNGDE ALESWLTSDS
     AGTPYDLVLM DIQMPKLDGI EVTKRIRARE AGQRVRRTPI LALTANALVE DRYACFEAGM
     DGFLMKPLDR DKLAEALKGL AKTRHVAA
//
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