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Database: UniProt
Entry: A0A0E3ZH21_9BACT
LinkDB: A0A0E3ZH21_9BACT
Original site: A0A0E3ZH21_9BACT 
ID   A0A0E3ZH21_9BACT        Unreviewed;       451 AA.
AC   A0A0E3ZH21;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=PKOR_21920 {ECO:0000313|EMBL:AKD05234.1};
OS   Pontibacter korlensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=400092 {ECO:0000313|EMBL:AKD05234.1, ECO:0000313|Proteomes:UP000033109};
RN   [1] {ECO:0000313|EMBL:AKD05234.1, ECO:0000313|Proteomes:UP000033109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X14-1T {ECO:0000313|EMBL:AKD05234.1,
RC   ECO:0000313|Proteomes:UP000033109};
RX   PubMed=26057562; DOI=10.1038/srep10929;
RA   Dai J., Dai W., Qiu C., Yang Z., Zhang Y., Zhou M., Zhang L., Fang C.,
RA   Gao Q., Yang Q., Li X., Wang Z., Wang Z., Jia Z., Chen X.;
RT   "Unraveling adaptation of Pontibacter korlensis to radiation and
RT   infertility in desert through complete genome and comparative
RT   transcriptomic analysis.";
RL   Sci. Rep. 5:10929-10929(2015).
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; CP009621; AKD05234.1; -; Genomic_DNA.
DR   RefSeq; WP_046313531.1; NZ_CP009621.1.
DR   AlphaFoldDB; A0A0E3ZH21; -.
DR   STRING; 400092.PKOR_21920; -.
DR   KEGG; pko:PKOR_21920; -.
DR   PATRIC; fig|400092.3.peg.4816; -.
DR   HOGENOM; CLU_688517_0_0_10; -.
DR   OrthoDB; 9766459at2; -.
DR   Proteomes; UP000033109; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 2.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AKD05234.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033109};
KW   Transferase {ECO:0000313|EMBL:AKD05234.1}.
FT   DOMAIN          234..445
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          162..227
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   451 AA;  51209 MW;  BF4AE2023DDC2103 CRC64;
     MQRSILKIDV NNELDVVLAY KRAMQLSERL GMQQANQTKF ATAVSEICRN VIEYVGNGTI
     QYSLTEVSGY KYLEALVTDR GRGIGNLELI LARTDYNNNG SRGTGIINSK KLVDLFEIES
     DSERGTRVRL GKRLSQTGPT VTYHALEKWV EEFNHESDIS PYAEIKRQNM QLLEVLEQLR
     MRNLEAEQQL QEIRRLNTQL QQSNHDVSQL LEEREKKNHM LQEINQSLDA FAHTVSHDLR
     APLQNINGIT TALEACLEAG QFEEANFVLP MLRQQTQKMD RLITGILAYS LAGHHNLPKK
     ALDLQVLLHQ VISSLNVPAS FVIEVQDDLP VLYTQEVYLY QVFSNLIGNA IKYHDRPEQA
     HLQVSYTLGS DWLYFTVIDN GPGVAPELQQ QIFDMYETGQ SFPQADSSGL GLSIVRKIIE
     EKGGKVWVES EGRGSRFSFT WPKAELIQEG L
//
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