ID A0A2V4NPX4_9ACTN Unreviewed; 487 AA.
AC A0A2V4NPX4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:PYC78158.1};
GN ORFNames=C7C46_17315 {ECO:0000313|EMBL:PYC78158.1};
OS Streptomyces tateyamensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=565073 {ECO:0000313|EMBL:PYC78158.1, ECO:0000313|Proteomes:UP000248039};
RN [1] {ECO:0000313|EMBL:PYC78158.1, ECO:0000313|Proteomes:UP000248039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21389 {ECO:0000313|EMBL:PYC78158.1,
RC ECO:0000313|Proteomes:UP000248039};
RA Schwalen C.J., Hudson G.A., Mitchell D.A.;
RT "Bioinformatic expansion and discovery of thiopeptide antibiotics.";
RL Submitted (MAR-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:PYC78158.1}.
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DR EMBL; PYBW01000053; PYC78158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4NPX4; -.
DR OrthoDB; 3534856at2; -.
DR Proteomes; UP000248039; 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 InterPro; IPR007168; Phageshock_PspC_N.
DR PANTHER; PTHR24421; NITRATE/NITRITE SENSOR PROTEIN NARX-RELATED; 1.
DR PANTHER; PTHR24421:SF65; SENSOR HISTIDINE KINASE COMP; 1.
DR Pfam; PF13581; HATPase_c_2; 1.
DR Pfam; PF04024; PspC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:PYC78158.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248039};
KW Transferase {ECO:0000313|EMBL:PYC78158.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..90
FT /note="Phage shock protein PspC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04024"
FT DOMAIN 354..447
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|Pfam:PF13581"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 52067 MW; 1F498A1F35E96D25 CRC64;
MAAPGTEPTS SPPLAENPAG AGGEPSPVPG RPPYRKLYRS PHSRMLGGVA HGLAVHLGLP
VAWVRVGFVL LFFANGIGVL LYAAFWFVVP IGIGEPALGS DWVWAGGQFV PAGASGITPD
PLRKDRRGRL GRLRDLLQGT FQGEPVIAET VPPGTEPGSR PGTSRQNAGQ LAALLMLVIG
VMALLNALGI QSAKPYTWPL LAIGVGVALV WRQADDSRWQ RWFGLDGGRR RTAVARVGAG
VLLVTAGIIG FLVLQGIGST PAAVVEASLA VLAGVAVLTG PYALRMWQDL GAERTARIRA
QERAEIAAHI HDSVLHTLTL IQRRAEDPKE VQRLARAQER ELRLWLYRPE AAAEAAPDTL
AERIREVVAE VEDRHGVPIE LVCVGDCPMD EKIAAQLRAA REAMVNAAKY GGGGPVQVYA
EVEGRTVLVY VRDRGPGFDP ETVPEDRMGV RESIIGRMKR NGGTARVRPA PDGGTEVELE
MERAADD
//
