ID A0A0Q8PWE9_9ACTN Unreviewed; 634 AA.
AC A0A0Q8PWE9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:KRB74760.1};
GN ORFNames=ASE03_20130 {ECO:0000313|EMBL:KRB74760.1};
OS Kitasatospora sp. Root187.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB74760.1, ECO:0000313|Proteomes:UP000051829};
RN [1] {ECO:0000313|EMBL:KRB74760.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB74760.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB74760.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB74760.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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:KRB74760.1}.
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DR EMBL; LMHX01000004; KRB74760.1; -; Genomic_DNA.
DR RefSeq; WP_057231917.1; NZ_LMHX01000004.1.
DR AlphaFoldDB; A0A0Q8PWE9; -.
DR STRING; 1736486.ASE03_20130; -.
DR Proteomes; UP000051829; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF26; HEAT SHOCK PROTEIN (HSP90 FAMILY)-RELATED; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 2.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Kinase {ECO:0000313|EMBL:KRB74760.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051829};
KW Transferase {ECO:0000313|EMBL:KRB74760.1}.
FT REGION 139..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 634 AA; 67539 MW; 3832D8863D9033E1 CRC64;
MSEGLQPGRL PEQNLRTTEV DLGGLVGVLA THLYSTPLVA LRELVQNAHD SHTRRLLEDP
GSAAGVIRVR ADQAGRTISI EDAGAGLTEP EIHAYLATVG TGYTRLLRDL TGDQSLIGAF
GLGFLSAFSV ADEVTVTTTS HREPGLGHRY RSRGGEQYSV EQVPARPAPG TVVELLLKPE
HARLADEYAL REVLGRYCVL LPIPVLVGED EQPVNGVQVP WRAELTGDQS PARMRFAAAF
GRHFEPLATL PVAPVEGVTD AVGLLWVQDG GSYGSSDNRD LAVYLRGMLL AEDARDLLPP
WAGFIGGVIE SNRLTPTAGR EDLQRDEQYR ALQRVLADAV VEGLYEIARL EPAAWRRILA
RHGQELLGAA LVDDRLFTLL ADDVPVPTSQ GELTAGALRA AGDGAVHVAL GAGGGFEEML
YRAMQVPIAR GDRYAVLPFL RRYAALRECR LVELGSESGD RELFRDPERP LPREEFAWLS
GALTDPGERL VPARFDPPGL PLVLVPDREA ELKARIENDQ ADARIPSAAL QLARAFTART
DGTVKARLYL NLAAPAVQQL LAAYRAGHTG SATAAGLLRS LKVIMAAAAG SAAGDLAAAL
GGVGTAVAAL TAAVPEGPAT PDGPTDDQDG TPNR
//
