ID   A0A3N2NQ32_9BACT        Unreviewed;       645 AA.
AC   A0A3N2NQ32;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Tetratricopeptide repeat-containing sensor histidine kinase {ECO:0000313|EMBL:ROT24585.1};
GN   ORFNames=EEL53_00690 {ECO:0000313|EMBL:ROT24585.1};
OS   Muribaculaceae bacterium Isolate-114 (HZI).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX   NCBI_TaxID=2486475 {ECO:0000313|EMBL:ROT24585.1, ECO:0000313|Proteomes:UP000273368};
RN   [1] {ECO:0000313|EMBL:ROT24585.1, ECO:0000313|Proteomes:UP000273368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate-114 (HZI) {ECO:0000313|Proteomes:UP000273368};
RA   Clavel T., Strowig T.;
RT   "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT   host preference, and functional potential of this yet undescribed family.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:ROT24585.1}.
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DR   EMBL; RIBN01000001; ROT24585.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2NQ32; -.
DR   Proteomes; UP000273368; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF13181; TPR_8; 2.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ROT24585.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000273368};
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        23..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          465..516
FT                   /note="Signal transduction histidine kinase subgroup 3
FT                   dimerisation and phosphoacceptor"
FT                   /evidence="ECO:0000259|Pfam:PF07730"
FT   DOMAIN          558..632
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|Pfam:PF02518"
SQ   SEQUENCE   645 AA;  72260 MW;  02F76FC7D03A9BC5 CRC64;
     MFCPKCSCII GRILLTLTKS LELFNFCHLL NIYLYSIIIL KIKTMISICP HKLFIYAITA
     CIACIPSFGS PAGKNNDWID EIDSYVNSNP DSAIILCNDA IREHYPLDGS EKVALLTIRG
     NANFTLGNYD TAKADFRKAA DLAFDIADTL AYINALSDLG VAYRVSQQQD SAMACYNHAL
     NMIKDGRFPD MEANILTSLA ILFANQGRLK EAIPFAEKGW KKAKLTDDIE TQIYAASSLG
     SALFLAGDHN RGLATQRSII KIAERKGIPR YILKTYASVI AMHNRLGNTD SVNYYINRGR
     TLLDKVPEAS IESVGFLEQS FVVLTKMGRY KESLDIQMKI LNMLDSRPFM PLHLLYQRIA
     LNYKGLGDIE RMNDAYIKAI EIADSIHQSD INKQMSDFNA RYHAAEKELA IAALRHEKSR
     RGMIIAILAG VIAATSLLLI IYLRSRRRKT ELANIKARIE GIEQERGRLA HELHDGVCND
     LLGIELALAG GRNDTAEISE MLRATRNEVR SISHELLPPS FNRLSLSQLI AAYAYKSDGF
     VEYLPSQDQI DLDMEQSMNL YRIIQEWIAN IRHHGAARYA TISLKQSGNE TILDICDNGI
     AFNPDEANSS GLGIDNIRQR VKAINGTIDF TRRNNINIMS VKIFK
//