ID A0A1T5AMF7_9SPHI Unreviewed; 627 AA.
AC A0A1T5AMF7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:SKB36221.1};
GN ORFNames=SAMN05661099_0877 {ECO:0000313|EMBL:SKB36221.1};
OS Daejeonella lutea.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Daejeonella.
OX NCBI_TaxID=572036 {ECO:0000313|EMBL:SKB36221.1, ECO:0000313|Proteomes:UP000189981};
RN [1] {ECO:0000313|Proteomes:UP000189981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22385 {ECO:0000313|Proteomes:UP000189981};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; FUYR01000001; SKB36221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5AMF7; -.
DR STRING; 572036.SAMN05661099_0877; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000189981; 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:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF97; ENDOPLASMIN; 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; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000189981}.
SQ SEQUENCE 627 AA; 70833 MW; D267048E7BF264BC CRC64;
MQEKGTISIH TENIFPIIKK FLYSDNEIFL RELVANAVDA TQKIKRLSSL GEYKGDLGEL
KVSVSFDEKK KTITISDNGL GMTGEEIKKY INQIAFSGAT EFVEKFKDAK DANEIIGKFG
LGFYSAFMVA DQVEIQSLSY KEGSEPARWI CDGSTEFEIS AGNRTERGTD IILHVNKESK
EFLDKGKLQG ILDKYCKFLP VPVQFGNKST SEPDGEDADG KPKYKSVEVP NIINNTSPIW
TKSPTELKDE DYLSFYQELY PFSEAPLFWI HLNVDYPFNL TGVLYFPKLK NDFEMQRNKI
KLFSRQVFIT DEVKDVVPEF LMLLHGIIDS PDIPLNVSRS FLQADSSVKK INTYITKKVA
DKLASLFKAD RKAYEEKWSD IGLFVKYGMI SEEKFYDKGK DFVLMGNTAK EYFTVDEYKE
KVKANQTDKD GNLVLLYATD AAKQDSFIQS ANKKGYDVLL MDSPIDTHFI SQMEQKLEKV
NLKRVDAASA DKIISKDENI VAVLNDEEKE KVKGIFEKAI VKPGMKVEVD SLNPDELPVI
VTMDEFMRRM KDMAAMGGGM NFYGNLPDSY NVTINGNHKL VGKILQTSDE AEQTQLAKQA
FDLALLSQGM LTGAELTEFV NRSVSLI
//