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Database: UniProt
Entry: W8F061_9BACT
LinkDB: W8F061_9BACT
Original site: W8F061_9BACT 
ID   W8F061_9BACT            Unreviewed;       631 AA.
AC   W8F061;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Hsw_0331 {ECO:0000313|EMBL:AHJ95926.1};
OS   Hymenobacter swuensis DY53.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ95926.1, ECO:0000313|Proteomes:UP000019423};
RN   [1] {ECO:0000313|EMBL:AHJ95926.1, ECO:0000313|Proteomes:UP000019423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY53 {ECO:0000313|EMBL:AHJ95926.1,
RC   ECO:0000313|Proteomes:UP000019423};
RA   Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT   "Complete genome sequence of ionizing-radiation resistance bacterium
RT   Hymenobacter swuensis DY53.";
RL   Submitted (JAN-2014) 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; CP007145; AHJ95926.1; -; Genomic_DNA.
DR   RefSeq; WP_044000782.1; NZ_CP007145.1.
DR   AlphaFoldDB; W8F061; -.
DR   STRING; 1227739.Hsw_0331; -.
DR   KEGG; hsw:Hsw_0331; -.
DR   PATRIC; fig|1227739.3.peg.599; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_114_67_10; -.
DR   OrthoDB; 9810447at2; -.
DR   Proteomes; UP000019423; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat 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   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF17874; TPR_MalT; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00028; TPR; 5.
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; SSF48452; TPR-like; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AHJ95926.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019423};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:AHJ95926.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..631
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004908038"
FT   TRANSMEM        356..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          412..629
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          375..402
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   631 AA;  70425 MW;  59479E633B6E3B24 CRC64;
     MRRFLLVAFL LCCLAGTVAA RAAAVPALLR QLRTQPADTA RVRLLNELCY ALHDNEPTRA
     LPYGEQSVAL ARRLNHSQGL LRALLNLASC YANLADGPHA LQLQQEALLL ARRLRSNDGL
     VRSYTGMGGV YHERNDTAAA LRNYRRALTY AYLPDVQVRS QLMLFGNLGN LYFYLKQQQE
     GLVFTRRALQ LARRTRDRAG ESLYLADLGS FYMQMNQLDT AEGLLRQAVS IVEPLHNHRF
     EAGHLELLAT VLLLQNELPE AEQLTRRALR LARQIDYKER VLDSYNLLAE INVSRKQFEE
     AYEWQSRFRD LNDSLNSRSR VQTLTALQTR YETADKEHLI RRLTERESVM QQRNRALWGA
     IAALLLGLGG MAYLYTKLRR SRAELSSNHR ALEEVTKELR QLAASKDRLY AIVAHDLRGP
     VTSFAGVTEL IDFYLKQGDE DGLRRLPALV RQSAYQLNHL LDNLLNWAVN QTGELAFRPK
     RLLVADLYQE ATRLYANAAE AKQITFHLDC PPHVAVWADA HMTETILRNL VGNALKFTPA
     GGSISLRTEA GTGGNVALCV QDTGSGIAPD QITALFSPDG LAPLRGSRSG TGLGLLLCRA
     FVDRQGGSLA IESTPGQGTT VCVHLPAAHL E
//
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