ID F8X3E2_9BACT Unreviewed; 887 AA.
AC F8X3E2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF9456_02770 {ECO:0000313|EMBL:EGK05569.1};
OS Dysgonomonas mossii DSM 22836.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=742767 {ECO:0000313|EMBL:EGK05569.1, ECO:0000313|Proteomes:UP000006420};
RN [1] {ECO:0000313|EMBL:EGK05569.1, ECO:0000313|Proteomes:UP000006420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22836 {ECO:0000313|EMBL:EGK05569.1,
RC ECO:0000313|Proteomes:UP000006420};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dysgonomonas mossii DSM 22836.";
RL Submitted (APR-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};
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:EGK05569.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADLW01000014; EGK05569.1; -; Genomic_DNA.
DR AlphaFoldDB; F8X3E2; -.
DR STRING; 742767.HMPREF9456_02770; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_113_1_10; -.
DR Proteomes; UP000006420; 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; cd00082; HisKA; 1.
DR CDD; cd01987; USP_OKCHK; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR Pfam; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF02702; KdpD; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006420};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 402..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 670..882
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 887 AA; 100373 MW; 874AD0DE01C40C86 CRC64;
MEENRPDPDK LLTSINQEEE IKKRGKLKIF FGMSPGVGKT YSMLQTAHID LSKGVDVVVG
YIESHNRPET SALLEGLEII PRKKIEYKGT SLEEMDLDAI ILRHPYLVLV DELAHTNAEG
SRHAKRYQDI QELLDNGINV YTTVNIQHLE SRNDTVAQIT GVTVKETIPD ELFEMADDVE
LIDITPNVLL DRLAEGKIYG LPESREAAKN FFRKGNITAL REMSLRLVAD RVDKQLKSYM
QQKQIAGPWK SGLHLLVLVG PSKSSAKLIR WAKNLSYTMG ADLVALHVEN TQVLNEEQQE
QLSKNIDLAR EFGAEVIITS GSDLVSTTLD IAHKENITHI IIGKSGKQSF FSSLFSRDNF
VNRLLKESGE IDIYVIEPGF EAKQYKRKLV SYPDFSSSYK HYIIAFLAVL ATVLLCLPIV
RETGYQSISF ILLFVILILS MFFRLGPIMM ASAVSAVAWD FFFITPQYTL KITQPEDLLA
FCMFFAVALV TGTLTAKVRK QERLTRKRAE KTNALFHLTK QLANAENTKK ILEVSKEDIN
NYFGVDAYFL LQDGEGRLKK KQQNAKPGDF TESEYSIAQW VFKHSKKAGK HTDTLSLSEY
TFYPLKSIKT KPGVVAIKPK KKFNGETELF WDTFLTQISN TLEHHDFAQQ AKKANLLDES
DKLYKTLFNS ISHELRIPIA TIMGASDTLL ADSHPEKVRK ELYSEILTAS GRLNRLVENL
LNISRLETGK ITLHTDWCDM NDLFNKVTDN LRDELKAYRL DIVVPQTMPL VKLDFGLMEQ
VLHNLVYNSC KYSTPGTSIR LKSFYDNEYL IIQEMDRGPG FPPDTLPFVF NKFFKTEHKA
TGGLGLGLSI AKGFVEAHKG TISVENRQNG GARFTIKIPT KISYINA
//
