ID   A0A1H5IWX3_9FLAO        Unreviewed;       637 AA.
AC   A0A1H5IWX3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:SEE44664.1};
GN   ORFNames=SAMN04487765_2608 {ECO:0000313|EMBL:SEE44664.1};
OS   Tenacibaculum sp. MAR_2010_89.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=1250198 {ECO:0000313|EMBL:SEE44664.1, ECO:0000313|Proteomes:UP000198792};
RN   [1] {ECO:0000313|EMBL:SEE44664.1, ECO:0000313|Proteomes:UP000198792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mar_2010_89 {ECO:0000313|EMBL:SEE44664.1,
RC   ECO:0000313|Proteomes:UP000198792};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNUB01000005; SEE44664.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5IWX3; -.
DR   STRING; 1250198.SAMN04487765_2608; -.
DR   Proteomes; UP000198792; 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; 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:UP000198792}.
FT   REGION          207..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   637 AA;  72116 MW;  01BF4AEE0B5D1A4E CRC64;
     MSKGNINVSV ENIFPLIKKF LYSDHEIFLR ELISNGTDAT TKLKHLISIG EAKTELGDAK
     IEISIDKDAK TLTIKDQGLG MTADEVEKYI NQIAFSGAEE FLEKYKDDKN ETGVIGHFGL
     GFYSAFMVAD KVDLITKSFK DEPAAHWTCD GSPEYTLVEH DKSDRGTEII LHIADDSTEF
     LEEAKISGLL NKYNRFNQVP IKFGTKQVND PDFTPQTTTN KDGKETTEPH KQIDVDNIIN
     NTNPAWTKKP ADLEAEDYTN FYRELYPMQF EESLFHIHLN VDYPFNLTGI LFFPKLSQNL
     DMQKDKIQLY QNQVFVTDNV EGIVPDFLQM LKGVIDSPDI PLNVSRSYLQ ADGAVKKISG
     YITKKVADKL SSLFKKDRAD FEQKWNDIKV IIEYGMLSED KFFDKAKKFA LYPTVSDSFF
     TFDELIEKTK DAQTDKDGNH IILYASNKEA QHSYIQDATA KGYEVVILDS PIVSHLMQKL
     ETSGESKVQF TRVDSDFIDN LIKKDDTVIS KLTDEEKETL KPVIEGAVNN KSYTVQLEAM
     DSSSSPFLIT VPEFMRRMKE MQASGGGGGM MGMGNLPEMY NLVVNTNHPL VSEILTAEEG
     KKKELITQAF DLAKLSQNLL HGEELTNFIK RSYELIK
//