ID   A0A1H4F9W3_9SPHI        Unreviewed;       629 AA.
AC   A0A1H4F9W3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:SEA93262.1};
GN   ORFNames=SAMN05443550_10752 {ECO:0000313|EMBL:SEA93262.1};
OS   Pedobacter hartonius.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=425514 {ECO:0000313|EMBL:SEA93262.1, ECO:0000313|Proteomes:UP000198850};
RN   [1] {ECO:0000313|EMBL:SEA93262.1, ECO:0000313|Proteomes:UP000198850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19033 {ECO:0000313|EMBL:SEA93262.1,
RC   ECO:0000313|Proteomes:UP000198850};
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; FNRA01000007; SEA93262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4F9W3; -.
DR   STRING; 425514.SAMN05443550_10752; -.
DR   Proteomes; UP000198850; 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; 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:UP000198850}.
SQ   SEQUENCE   629 AA;  71059 MW;  55C6B2D33F0EFC8F CRC64;
     MSIEEKGSIS IHTENIFPII KKFLYSDNEI FLRELVSNAV DAVQKIKRLA ALGQFNGELG
     DTFVEVALDE EKKTITISDS GLGMTAEEIK KYINQVAFSG ASEFVEKFKD AKDANEIIGK
     FGLGFYSAFM VADLVEIQTL SYQDGAEPAR WVCDGSTSYE ISEGSRTTRG TDIILHINAE
     SEEFLSKHKI EEILDKYGKF LPVPIKFGTK TTQEPDGEDE EGKPKTVAVE VDNIINTTAP
     IWTKAPADLS DQDYLDFYKQ LYPFSEDPLF WIHLNVDYPF NLTGVLYFPK VKNDFDMQRN
     KIKLFSRQVF ITDEVKDIVP EFLMLLHGVI DSPDIPLNVS RSFLQADSNV KKINSYITKK
     VADKLHELFN KDRKSYEEKW GDIGLFVKYG MVSEEKFYDK AKDFALLTNT KNEHYTLEEY
     REKVAPVQTD KNGQVVYIYT NDPAKQDSFI QSTGKKDYDV LLMNSAIDNH FVSSLEQKLD
     KTLLKRVDSS VASKLIEKDD SVESVLTEEQ SAKVKEVFEK AIVKPGFQVE IVGLHPEEFP
     VTVTMDEFMR RMKDMAQMGG GMSFYGNLPD SYKVAINGNH KLVNRILQTE DAAEQGALAK
     QAVDLALLSQ GMLTGAELTA FVNRSVELI
//