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Database: UniProt
Entry: A0A367F204_9ACTN
LinkDB: A0A367F204_9ACTN
Original site: A0A367F204_9ACTN 
ID   A0A367F204_9ACTN        Unreviewed;       535 AA.
AC   A0A367F204;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Signal transduction histidine kinase subgroup 3 dimerisation and phosphoacceptor domain-containing protein {ECO:0000259|Pfam:PF07730};
GN   ORFNames=DTL70_13695 {ECO:0000313|EMBL:RCG23687.1};
OS   Streptomyces diacarni.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2800381 {ECO:0000313|EMBL:RCG23687.1, ECO:0000313|Proteomes:UP000252914};
RN   [1] {ECO:0000313|EMBL:RCG23687.1, ECO:0000313|Proteomes:UP000252914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW51701 {ECO:0000313|EMBL:RCG23687.1,
RC   ECO:0000313|Proteomes:UP000252914};
RA   Li L.;
RT   "Streptomyces reniochalinae sp. nov. and Streptomyces diacarnus sp. nov.
RT   from marine sponges.";
RL   Submitted (JUN-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:RCG23687.1}.
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DR   EMBL; QOIN01000042; RCG23687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367F204; -.
DR   OrthoDB; 5241784at2; -.
DR   Proteomes; UP000252914; 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   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR   PANTHER; PTHR24421:SF63; SENSOR HISTIDINE KINASE DESK; 1.
DR   Pfam; PF07730; HisKA_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252914};
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        27..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          218..284
FT                   /note="Signal transduction histidine kinase subgroup 3
FT                   dimerisation and phosphoacceptor"
FT                   /evidence="ECO:0000259|Pfam:PF07730"
FT   REGION          407..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          199..226
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        469..483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   535 AA;  55799 MW;  639FA85313CEAF96 CRC64;
     MLRWGRQKRH DWEKRSRLAQ VEVSTRWLLL LTPAIYYLGG MPGFFADISP DRLPMSLGAT
     VAVLALVQGG LSVRGLRVAM ECYLGGAEAP RRLLAAVLAV FALETAVLVV MLVRGWAGTA
     AAPALALFAV VPSLSGLYAL TVSRRRAVVV PLVVSALVLA AFALAGMAWP SLLGTFLVLV
     FGSLCGAFSV RGTAWYLAVM RELDEAKEAQ SRLAVAEERL RFSRDLHDVM GRNLSVIALK
     SELATQLARR GADSAIEQML QVQRLARESQ TEVREVVRGY REAGLETELA GARGVLRAAG
     VDCRVESTAP EMDRSVQSAL GWVVREGATN VLRHADAARC LISLTTGAPG TVALLMENDG
     AEPGAADRGS GLTGLAERLA VLGGTLVRAG ADAEGVFRLH AEVPLHAEDP GEVSGDDASG
     PPHADDASGS ARGDGEASGA AAGSETFEEG QVGGGGRLAV AGPDTDTSRG ASPDEHRPAP
     GEGQRQVREQ AQGQAQGQGR GQGQGQGQVQ VDRPGGLLRR ALARGGVTSG GGPRG
//
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