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Database: UniProt
Entry: A0A254TRR7_9BURK
LinkDB: A0A254TRR7_9BURK
Original site: A0A254TRR7_9BURK 
ID   A0A254TRR7_9BURK        Unreviewed;       686 AA.
AC   A0A254TRR7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AYR66_25900 {ECO:0000313|EMBL:OWW22418.1};
OS   Noviherbaspirillum denitrificans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Noviherbaspirillum.
OX   NCBI_TaxID=1968433 {ECO:0000313|EMBL:OWW22418.1, ECO:0000313|Proteomes:UP000197535};
RN   [1] {ECO:0000313|EMBL:OWW22418.1, ECO:0000313|Proteomes:UP000197535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSA40 {ECO:0000313|EMBL:OWW22418.1,
RC   ECO:0000313|Proteomes:UP000197535};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OWW22418.1}.
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DR   EMBL; LSTO01000001; OWW22418.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A254TRR7; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000197535; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR029095; NarX-like_N.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF13675; PilJ; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197535};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          381..485
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         428
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   686 AA;  75648 MW;  6BE0ADBF216B88A1 CRC64;
     MQAESSSRFA GKYREIILAV ACFLVFDLAV LVLNFYISFQ ISEDALSINL AGRQRMLSQR
     MAKALLVIET DVERGATGAQ ARTELGRTVE LFDTTLKAFQ SGGTATGGDD KPVRLARVDS
     PEGRNVLAQA NELWLPYRQK LVPLLAPGAF TPLQLAEASE KARDTNLKLL ALMNALTSQL
     EQTANAKADT LRMVQTGGIL LALMNFAFIL FKFIRRLRDN DRKIEAAQKE TADILGTVTE
     GLFLLDSTMH IGSQYSASLQ RILGRPVAPG TDFRNLLGDL VKESTFDLAI DYIELLFGDR
     VKESLIGDLN PLTAVEFTFT NPEGMPVRRV LSMQFNRVRD NGKVSHLLVT VFDITAQVEL
     ENALADAKEK AKAEIEIMLD LLKVNPATLE QFLKNAEAAL LDINAHLRAA SSENNHRRMV
     GTIFRKIHAL KGEAAVLELH LFENLAQQFE SQLAELRDKG MVSGDDLLSL PFPVEEFLQK
     ISMVRDLIAR LSDYHSAFNV AADDGFASNL ATLAERIAAD HGKQVKIETD LDLMRSLPQR
     TRVELQDIAV QLLRNAVAHG IETAGERHER AKPAAGSIYI GLKPTESGEY ALTLRDDGRG
     LSPQHIRDAL LKSGRYNEAQ LAELDDRQIV MKIFEAGVST ATQVTRDSGH GVGMDVVKNK
     VAQLGARIRI SSRVDAFTQF SIHFAA
//
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