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Database: UniProt
Entry: D0TSK2_9BACE
LinkDB: D0TSK2_9BACE
Original site: D0TSK2_9BACE 
ID   D0TSK2_9BACE            Unreviewed;       424 AA.
AC   D0TSK2;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HMPREF0102_03046 {ECO:0000313|EMBL:EEZ03984.1};
OS   Bacteroides sp. 2_1_22.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=469588 {ECO:0000313|EMBL:EEZ03984.1, ECO:0000313|Proteomes:UP000005775};
RN   [1] {ECO:0000313|EMBL:EEZ03984.1, ECO:0000313|Proteomes:UP000005775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_1_22 {ECO:0000313|EMBL:EEZ03984.1,
RC   ECO:0000313|Proteomes:UP000005775};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., Chen Z.,
RA   Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   McDonald J., Allen-Vercoe E., Strauss J., Ambrose C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain 2_1_22.";
RL   Submitted (JUL-2009) 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; GG705175; EEZ03984.1; -; Genomic_DNA.
DR   RefSeq; WP_004314350.1; NZ_GG705175.1.
DR   AlphaFoldDB; D0TSK2; -.
DR   HOGENOM; CLU_000445_89_35_10; -.
DR   Proteomes; UP000005775; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEZ03984.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          222..424
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   424 AA;  49826 MW;  967E0619C489E9BB CRC64;
     MKLIYYIILR ITLALTFILT VWAIFFYVTM IDEVNDEVDD ALEDYSETII IRALAGEELP
     SKTNGSNNQY YMMEVSKEYA ESREDIQYKD SMVYIEEKEE TEPARILTTI FKDDEGRYHE
     LTVSTPSIEK DDLRDAIQVW IIFLYVALLF CIIIISVWVF YRNMRPLYVL LHWLDGYQTG
     KKNKPLSNET QITEFRKLNE AAIRYVERTE QMFEQQKQFI GNASHEIQTP LAICRNRLEM
     LMEDDSLSEK QLEELMKTHQ TLEYITKLNK SLLLLTKIDN GQFTDTKQLE LNGLLKQYLQ
     DYEEVYDYRN IEVTIDEQDI FNVTINESLA VALLTNLLKN AFVHNIDGGH IRITVTKNSI
     TFRNSGVKNP LDKEHIFERF YQGTKKEGST GLGLAIADSI CRLQHLSIRY YFEQKEHCFE
     ISRQ
//
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