ID   A0A2K8VAF7_9FLAO        Unreviewed;       628 AA.
AC   A0A2K8VAF7;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:AUC14665.1};
GN   ORFNames=BTO06_05705 {ECO:0000313|EMBL:AUC14665.1};
OS   Tenacibaculum sp. SZ-18.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=754423 {ECO:0000313|EMBL:AUC14665.1, ECO:0000313|Proteomes:UP000232695};
RN   [1] {ECO:0000313|EMBL:AUC14665.1, ECO:0000313|Proteomes:UP000232695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZ-18 {ECO:0000313|EMBL:AUC14665.1,
RC   ECO:0000313|Proteomes:UP000232695};
RA   Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (DEC-2016) 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; CP019335; AUC14665.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8VAF7; -.
DR   OrthoDB; 9802640at2; -.
DR   Proteomes; UP000232695; Chromosome.
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; IPR019805; Heat_shock_protein_90_CS.
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.
DR   PROSITE; PS00298; HSP90; 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:UP000232695}.
SQ   SEQUENCE   628 AA;  71481 MW;  FB7794AE7FFFC77B CRC64;
     MSKGSINVSV ENIFPLIKKF LYSDHEIFLR ELISNATDAT TKLKHLISIG EAKVEYGNPQ
     IEIKIDKENK TLHITDQGLG MTADEVEKYI NQIAFSGAEE FLEKYKDSNN ETGVIGHFGL
     GFYSAFMVAD KVEIITKSYK EEPAAHWTCD GSPEYTLEAH NKTERGTEII LHISEDEKDF
     LEDSKVSGLL SKYNRFNQIP IKFGTKTETL PLPEDAAEDA KPETQEVDNI INNTTPAWTK
     KPADLEGEDY SKFYRELYPM QFEEPLFHIH LNVDYPFNLT GILYFPRLTQ NMDIQKDKIQ
     LYQNQVFVTD NVEGIVPDFL QMLKGVIDSP DIPLNVSRSY LQADGAVKKI SGYITKKVAD
     KLASLFKKDR ADFEQKWNDI KVIIEYGMLS EEKFFDKAKK FALYPTVNDT FFTFDELVEK
     TKEAQTDKDG NHVILYAANK DAQHSYIEDA KAKGYEVLLL DTPIVPHLMQ KLEMESGDAK
     IQFKRVDADH IDNLIKKDDT IISKLSEGEK EKLKPVIEGA VNNSSYTVQL EAMDSSSSPF
     LITVPEFMRR MKEMQATGGG MMGMGNMPEM YNLVVNTNHE LVSDILNADE DKQKQLISQA
     FDLAKLSQNL LHGEELTNFI KRSYDLIK
//