ID A0A150JAL1_9EURY Unreviewed; 839 AA.
AC A0A150JAL1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Bacterioopsin transcriptional activator {ECO:0000313|EMBL:KYC54236.1};
GN Name=bat_1 {ECO:0000313|EMBL:KYC54236.1};
GN ORFNames=AMQ74_00104 {ECO:0000313|EMBL:KYC54236.1};
OS Candidatus Methanofastidiosum methylthiophilus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Methanofastidiosa;
OC Methanofastidiosum.
OX NCBI_TaxID=1705564 {ECO:0000313|EMBL:KYC54236.1, ECO:0000313|Proteomes:UP000075578};
RN [1] {ECO:0000313|EMBL:KYC54236.1, ECO:0000313|Proteomes:UP000075578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U1lsi0528_Bin089 {ECO:0000313|EMBL:KYC54236.1};
RX PubMed=26943620;
RA Nobu M.K., Narihiro T., Kuroda K., Mei R., Liu W.T.;
RT "Chasing the elusive Euryarchaeota class WSA2: genomes reveal a uniquely
RT fastidious methyl-reducing methanogen.";
RL ISME J. 0:0-0(2016).
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:KYC54236.1}.
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DR EMBL; LNGD01000003; KYC54236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150JAL1; -.
DR Proteomes; UP000075578; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00062; PBPb; 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 SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 273..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 345..415
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 419..471
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 472..524
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 546..600
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 618..836
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 296..340
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 462..489
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 839 AA; 96021 MW; 594F96319FE4AF62 CRC64;
MRLMNNCVFI SMIICLFLFL PLFSVITGDS SKLVLKVGLY EDEPLIFRDT NGNVKGLYAD
ILGYIAAKEG WEIEYVYGTL NEGLVRIKDK EIDILTAVAY SPERATYTEF SNETVFPNWA
QVYTRPSLEI ESFLDLEYKR IAVVKGDIYY VGPNGIKNLM ENFDLNCTFV EVNDYLEVIR
LIEEERVDAG ILTRLYESEL QNNLKLAKSP LIYSPIKLLF GFPKASPQNQ YLIEKIDYHL
KILKDDHNSV YYSSINEYMP IYSVKEVQVF PKWLKTLIVA IFLVLIIFVT VSMILSREVK
KRTNHLNQAI EDLQEEIAHR VSAENSLKES QKKYRELTDK LLLESKSKFE SIYNNAAAGI
DLLDKNFKFI DLNDRLAEMF GYNKSELIGK SILDFTFPED IEITLKNLNS IVNGNIDIYS
LEKRFKKKDG SIFWGDVSAS AIMDENKNLQ AIVGVIIDIT SRKKAEELLE ESEEKYRELV
ENANSILAKF DKEGRIISMN DFGLKLFGYE EHELKGKTWI ETILPRIESN GKNLENLANE
ILNDPDKYSI SINENIKKNG ERIWVYWNNK PIYENGVLTG ILSVGTDITE RKKAEEELYK
ANKQLEEADR LKSIFLSSMS HELRTPLNSI IGFTGILLQG LAGDLNEEQK KQLGIIKKSS
QHLLSLINDI LDISKIEAGK LELDCENFDL KEVIEDVIST FDAIAKDKNL KIESIIPENV
TIYNDKRRFK QIIINLVGNA IKYTNEGGVK IIGEVLDKNN IEIRIIDTGV GIKKEDLSRI
FEPFQQLDEK LTKKVEGTGL GLHLVKKLLI LMKGNISLES EYGKGSIFTI IMPLKERDE
//
