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Database: UniProt
Entry: H0PW18_9RHOO
LinkDB: H0PW18_9RHOO
Original site: H0PW18_9RHOO 
ID   H0PW18_9RHOO            Unreviewed;       444 AA.
AC   H0PW18;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AZKH_4191 {ECO:0000313|EMBL:BAL26470.1};
OS   Azoarcus sp. KH32C.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL26470.1, ECO:0000313|Proteomes:UP000007106};
RN   [1] {ECO:0000313|EMBL:BAL26470.1, ECO:0000313|Proteomes:UP000007106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH32C {ECO:0000313|EMBL:BAL26470.1,
RC   ECO:0000313|Proteomes:UP000007106};
RA   Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA   Senoo K.;
RT   "Complete genome sequence of Azoarcus sp. KH32C.";
RL   Submitted (NOV-2011) 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};
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DR   EMBL; AP012304; BAL26470.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0PW18; -.
DR   STRING; 748247.AZKH_4191; -.
DR   KEGG; aza:AZKH_4191; -.
DR   PATRIC; fig|748247.4.peg.4150; -.
DR   eggNOG; COG3284; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_39_4; -.
DR   Proteomes; UP000007106; Chromosome.
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; 1.
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   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 1.
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); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAL26470.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007106};
KW   Transferase {ECO:0000313|EMBL:BAL26470.1}.
FT   DOMAIN          31..77
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          192..436
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          149..183
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   444 AA;  47854 MW;  45EF3B2BCD0F2914 CRC64;
     MAANEPLIDA SDEPDAPGDG VQQLTAAFAR LSRTYELILH ATTEGVLGLD QDGRINYANA
     AAGRMLGRQV EDMLGQTVDV VVGRGADSTA EAAGTVPWRP PFTSEQARRR SEFHRPGGAA
     FAVEYSVARI IEDEACEGAV LVFSDVSDRD RAERALQESL VELRETNQRL SDTRDQLLQS
     EKMAAIGQLA AGVAHEINTP IGYVKANVGT LLRYFNDLMT LVQTYEQTEH HLDSEHQALL
     RAARQACDLD FLREDTPALL NETQSGLASV ARIVRELMEF SASGEQGEWQ SSDLQQLIEG
     AIIAAASRTG SDATIVREQG ELPPIFCLAS GIRQVFSNLL VNAMQAVGQG GRIVVRCAGE
     DGERVRVEIE DDGEGITEEN LARVFNPFFT TRPVGSGTGM GLSVADTIVR RHGGRIEIDS
     ARGRGTTVRV TLPLAPEAVP GSTS
//
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