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Database: UniProt
Entry: W7YBA9_9BACT
LinkDB: W7YBA9_9BACT
Original site: W7YBA9_9BACT 
ID   W7YBA9_9BACT            Unreviewed;       446 AA.
AC   W7YBA9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=JCM21142_305 {ECO:0000313|EMBL:GAF01691.1};
OS   Saccharicrinis fermentans DSM 9555 = JCM 21142.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC   Saccharicrinis.
OX   NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF01691.1, ECO:0000313|Proteomes:UP000019402};
RN   [1] {ECO:0000313|EMBL:GAF01691.1, ECO:0000313|Proteomes:UP000019402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF01691.1,
RC   ECO:0000313|Proteomes:UP000019402};
RA   Starns D., Oshima K., Suda W., Iino T., Yuki M., Inoue J., Kitamura K.,
RA   Iida T., Darby A., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequence of Cytophaga fermentans JCM 21142T, a Facultative
RT   Anaerobe Isolated from Marine Mud.";
RL   Genome Announc. 2:e00206-14(2014).
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   -!- 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:GAF01691.1}.
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DR   EMBL; BAMD01000002; GAF01691.1; -; Genomic_DNA.
DR   RefSeq; WP_052343241.1; NZ_KI912107.1.
DR   AlphaFoldDB; W7YBA9; -.
DR   STRING; 869213.GCA_000517085_03195; -.
DR   eggNOG; COG2205; Bacteria.
DR   OrthoDB; 9796457at2; -.
DR   Proteomes; UP000019402; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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; 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; 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; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
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};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019402}.
FT   DOMAIN          227..446
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          186..220
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   446 AA;  50910 MW;  577ECF0D4A53A72B CRC64;
     MAKQSYQEFI SQHLKLDHDL ESCIYELFNP NNVMLGDDFF VASALSMCTY LNADYAFIAR
     INPREETLEM LANCHKGEIV QGSVLQCDDE PCKQVIADNI VTYKESVRAA FPDSKLLKEC
     EAEAFCGVPL YNASRKPIGV LLTLYSHKIS DAKKIETLMF MYSSKVGSEL EHRDRQLELR
     MHNMELLVFK EELISKNREL DQINNELKKV TLKAEEGNKL KSSFLANLSH EIRTPMNAII
     GFTELLKSNN LSVEEKDEYL NIIYQNGNQL MRVMDALIDI SKLQAKVYVE QKQRVRVNKM
     VSELHRNYSQ EIKAMRKDIR ILMLPGAADG MDILHTHKEA LCKVFDHLID NAIKFTHHGT
     VYIGYTVGDG CYEFFVKDTG VGIVKGQEEN IFDLFRQGDV EKSREFGGNG IGLSIVKKYV
     EIMDGSVWAE CNQKEGALIK FIIPMK
//
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