ID A0A3N4H3I8_9BACT Unreviewed; 627 AA.
AC A0A3N4H3I8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:RPA69933.1};
GN Name=htpG {ECO:0000313|EMBL:RPA69933.1};
GN ORFNames=EF405_01170 {ECO:0000313|EMBL:RPA69933.1};
OS Cyclobacteriaceae bacterium YHN15.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae.
OX NCBI_TaxID=2487897 {ECO:0000313|EMBL:RPA69933.1, ECO:0000313|Proteomes:UP000274029};
RN [1] {ECO:0000313|EMBL:RPA69933.1, ECO:0000313|Proteomes:UP000274029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YHN15 {ECO:0000313|EMBL:RPA69933.1,
RC ECO:0000313|Proteomes:UP000274029};
RA Chen Z.;
RT "Cecembia caeni sp. nov.,isolated from a lake.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RPA69933.1}.
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DR EMBL; RKQB01000001; RPA69933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4H3I8; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000274029; 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}.
SQ SEQUENCE 627 AA; 72103 MW; DC30B1ACA4E9B928 CRC64;
MQEKGTISIH TENIFPIIKK FLYSDHEIFL RELVSNAVDA TQKIKRLAQL GQYNGELGDV
TVEVSFDKDK KTITISDKGL GMTAEEVKKY INQIAFSGAT EFMEKFKDSK DANEIIGKFG
LGFYSAFMVA NQVEINTLSY QEGAEATRWT CDGSTEFEIS AGDRKERGTD VILYINEDSE
EFLDKWKLQG ILDKYCKFLP VPIKFGTKTE SMEDGVDDKG DKKWKSVEVD NIINTTAPIW
TKSPNELKDE DYLNFYKELY PMSEDPLFWI HLNVDYPFNL TGVLYFPKVK NDFEFQKNKI
KLFSRQVFIT DEVKDIVPEF LMLLHGVIDS PDIPLNVSRS FLQADSSVKK INNYITKKVA
DKLSELFKKD RKVYEDKWND IGLFVKYGMI SEEKFAEKGK DFSLLKNTKG EFFTLAEYKD
KVKAIQTDKN EQVVYLYSTN LDKQDAFIQS ANKKDYDVLV MDSPIDNHFI QHLEMKEEKT
SLKRVDADVV DKLIQKEDTY ANLLTEEQSQ KVKEIFEKAI NNKNYTLEVE GLSPEEMPVT
VTMEEFMRRM KEMAQMGGGM SFYGAMPDNY KVAINGNHPA IDKILKTENE EDQAKLAKQS
FDLALLAQGM LTGKDLTEFV KRSVELI
//