ID   A0A1N6HGW0_9BACT        Unreviewed;       607 AA.
AC   A0A1N6HGW0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:SIO18845.1};
GN   ORFNames=SAMN04488055_3364 {ECO:0000313|EMBL:SIO18845.1};
OS   Chitinophaga niabensis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=536979 {ECO:0000313|EMBL:SIO18845.1, ECO:0000313|Proteomes:UP000185003};
RN   [1] {ECO:0000313|EMBL:SIO18845.1, ECO:0000313|Proteomes:UP000185003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24787 {ECO:0000313|EMBL:SIO18845.1,
RC   ECO:0000313|Proteomes:UP000185003};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FSRA01000001; SIO18845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N6HGW0; -.
DR   STRING; 536979.SAMN04488055_3364; -.
DR   Proteomes; UP000185003; 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:UP000185003}.
SQ   SEQUENCE   607 AA;  69065 MW;  248BB5DBCC7861D1 CRC64;
     MQKGAIRVQT ENIFPIIKKF LYSDHDIFLR ELVSNAVDAT QKLKTLASVG EFKGDIGNTD
     ITVSLDKEKK TITISDRGVG MTAEEVDKYI NQVAFSGAEE FVNKYKGQTD GANIIGHFGL
     GFYSSFMVSS QVEIYSKSWR PDTKAVRWEC DGSPEYELEE TVKEERGTDI VMHINEESEE
     FLDENRIRTI LEKFCRFLPV PIRFQDTQIN NTSPAWVKKP SELTAEDYQN FYKELYPFAE
     PPLFWIHLNV DYPFNLTGIL YFPKITKSYE IQKDKISLYS NQVYVTDEVK NIVPEFLMLL
     HGVIDSPDIP LNVSRSYLQG DPNVKKINAH ITKKVADKLD EMFRTDRKSF EEKWEHIGLF
     VKYGMMTEDK FADKASKFHV MADVDNSTFY TLEEYRTATG ALQTNTEGKL VILYATNPVQ
     QDSYIQAAKA KGYKVVKLDT MVDAGFINQM ETKWENVQFN RVDADIADNL INNEAKAISV
     LSEEQEGKLK EMFGQQIPQP NIKVELKGLS AQDQPVIVTR SEFMRRMKDM AAMGGSASMF
     AGMPDEITMT VNANHPIYLN ILGEGNAEKQ QKLVRNLADL ALLSQNLLQG AELTAFVNRS
     VELMGKE
//