ID L1L9I8_9ACTN Unreviewed; 704 AA.
AC L1L9I8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein {ECO:0000313|EMBL:EKX69370.1};
GN ORFNames=STRIP9103_05837 {ECO:0000313|EMBL:EKX69370.1};
OS Streptomyces ipomoeae 91-03.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX69370.1, ECO:0000313|Proteomes:UP000010411};
RN [1] {ECO:0000313|EMBL:EKX69370.1, ECO:0000313|Proteomes:UP000010411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91-03 {ECO:0000313|EMBL:EKX69370.1,
RC ECO:0000313|Proteomes:UP000010411};
RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL Submitted (NOV-2012) 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:EKX69370.1}.
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DR EMBL; AEJC01000008; EKX69370.1; -; Genomic_DNA.
DR AlphaFoldDB; L1L9I8; -.
DR PATRIC; fig|698759.3.peg.102; -.
DR Proteomes; UP000010411; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 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 PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF10; SENSORY TRANSDUCTION HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EKX69370.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010411};
KW Transferase {ECO:0000313|EMBL:EKX69370.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 533..624
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 604..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 73673 MW; 862E0C3DA09947A5 CRC64;
MSPRRSRRTA VALAGVGAVF GAFVLVLVAD DRHADSTSTV FSGAVGGLYL GAGLAARWRR
PDNAVGLLML LVGIGWFAED LQISTDPAVH TVGLFLRSAS SGFLIPLLLV FPDGRLRSRH
DGEDGEEGEG GETGPPVVAV VDRRAHPVAA PVVDRRAHPV TAAVVDRTLV AAGCAVAFVL
VPVSVFFHAS VTPNLLLLHP VRDLHEVVEA VQFVMSGAVV AVLVWRWATA TPPARRALAP
LLVVGVVGAL ASGLDGAFGS ASESSHPPLI TVAHLTVLLL PLTFLAGVWR VRLGRTAVAE
LLRRMPLASR AELREALAKA LGDRSLQVGF PAPDGTGYVD VEGRPLSVPP GRQATDLERD
GRRVGVLVHD PALREDRYVL EAVVSAAALE LDNQALVAEL RESRRRVIEA GDEQRREVER
ALHDGAQQKF INLGLRLRLA RRRVDAWEAG GASGGSVGGV PGGGAGAVEL AGMLDDALAM
LEQGHAELRV AARGIHPVVL SEAGLVPALR SLASDLPLTV DIHAAGLPPL PEPIELTAYY
VVKEAISNVL RHADAETVRV ELRCEDGALR LSVTDDGVGG ADPAGGGTGL LGLRHRVTAY
DGELSVRGGP DGGTVVAVTL PTGGERKPPD EDGRDGSLDQ GGRDGLLDRG GRDGLLDRGG
RDGLLDRGGR DGLLDRGGRD GPLDQGGREE PLDQGGREER GEPG
//
