ID   A0A2S2CK63_9PROT        Unreviewed;       834 AA.
AC   A0A2S2CK63;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DEW08_00200 {ECO:0000313|EMBL:AWK84819.1};
OS   Azospirillum thermophilum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=2202148 {ECO:0000313|EMBL:AWK84819.1, ECO:0000313|Proteomes:UP000245629};
RN   [1] {ECO:0000313|Proteomes:UP000245629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFH 70021 {ECO:0000313|Proteomes:UP000245629};
RA   Zhao Z.;
RT   "Azospirillum thermophila sp. nov., a novel isolated from hot spring.";
RL   Submitted (MAY-2018) 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   ---------------------------------------------------------------------------
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; CP029352; AWK84819.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S2CK63; -.
DR   KEGG; azz:DEW08_00200; -.
DR   OrthoDB; 9796100at2; -.
DR   Proteomes; UP000245629; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
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; 3.
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; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   Pfam; PF13426; PAS_9; 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; 3.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AWK84819.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000245629};
KW   Transferase {ECO:0000313|EMBL:AWK84819.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          204..247
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          277..329
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          330..400
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          468..691
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          715..830
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         766
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   834 AA;  90641 MW;  3F7AFCCB581FA58F CRC64;
     MNDATSLVDE PRRGGRWSGS GHPVATALLY ALAPLGLAGL AGGLLIDNDP VAWAGTLAAA
     AGVALLVGRA ASATRRSSRL GLLLGGALEG LPAGQLLCDG DDNVVFINGA FRELSGWRDG
     ERPLDALERR FAGDPDGLAE FRRLRERVRA GTAASAELAV PYEGRPPVWL RLQGQPVYGF
     PGSVHWRVED ITARRELEQV MLREQAKLVD FMDHAPVGFF SVDQDGHFLF VNATLAKWLG
     CSPTDLVEGG RTLHEMLATP PAGAAPYDLF EGGGPEQRGE LAMRGPGGRR FQASVAQTVV
     RAEDGRQVHT RSVVRDLTPE REWQEALRLS EQRFQRFFED APIGIALVDE HGRLAECNEA
     FLALIGSAAQ EVIGRPMPDL IVPAERDMVA ERLKEVQGGG DPAAPLEIRL SAGRELSAQL
     YARRLGGVGP DGAAGLILHF IDMTERKSLE AQFAQSQKMQ AVGQLAGGVA HDFNNLLTAM
     IGFCDLLLLR HKPGDQSFSD IMQIKQNANR AANLVRQLLA FSRQQTLQPR VINVTDVLAE
     LANLLRRLIG ENIELKMIHG RDLGLIKVDQ NQLEQVIINL VVNARDAMAG GGRLTIVTSN
     YAVANAERRE HETIPPGDYV SVEVIDTGCG IPRENLQRIF EPFFSTKEVG SGTGLGLSTV
     YGIVRQTGGF VFVDSAVGEG TTFTILLPRH QGEIRPVDSG EPRERRGSDL TGTGTILLVE
     DEDAVRVFSA RALRNKGYQV LEAKNGEAAL QQIESNGSRI DLLITDVVMP QMDGPTLARH
     VRRLRPDMRV IFISGYAEDR LGDIDGVEVA HFLPKPFSLK QLASKVKEVI REGK
//