ID A0A2S0HTA1_9FLAO Unreviewed; 629 AA.
AC A0A2S0HTA1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:AVI49865.1};
GN ORFNames=C5O00_01245 {ECO:0000313|EMBL:AVI49865.1};
OS Pukyongia salina.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Pukyongia.
OX NCBI_TaxID=2094025 {ECO:0000313|EMBL:AVI49865.1, ECO:0000313|Proteomes:UP000238442};
RN [1] {ECO:0000313|EMBL:AVI49865.1, ECO:0000313|Proteomes:UP000238442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RR4-38 {ECO:0000313|EMBL:AVI49865.1,
RC ECO:0000313|Proteomes:UP000238442};
RA Kim Y.-S., Jang Y.H., Kim K.-H.;
RT "Genomic analysis of the strain RR4-38 isolated from a seawater
RT recirculating aquaculture system.";
RL Submitted (FEB-2018) 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; CP027062; AVI49865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0HTA1; -.
DR KEGG; aue:C5O00_01245; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000238442; 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:UP000238442}.
FT REGION 208..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 72228 MW; 8ECAA8EE9602EA9C CRC64;
MSSGTINVSV ENIFPLIKKF LYSDHEIFLR ELISNATDAT LKLKHLTNIG EAKVEYGNPM
IEVKIDKDKK QLHIIDQGIG MTAEEVEKYI NEIAFSGAEE FLEKYKDKNA DDAGIIGHFG
LGFYSAFMVA NKVEIITKSY KDEPAAHWTC DGSPKYTLEE ADKTERGTEI ILHISEDDTE
FLEESRIREL LVKYNKFMPV PIKFGTRTET LPKPEDAKED DPAPTKEVDN IINNPNPAWT
KQPADLKDED YKKFYRELYP MQFEEPLFNI HLNVDYPFNL TGILYFPKLT NDLNIQKDRI
QLYQNQVFVT DNVEGIVPEF LTMLRGVIDS PDIPLNVSRS YLQADGAVKK ISSYITRKVA
DKLKSLFNDN REDFEGKWDD IKIVIEYGML TEDKFFDKAQ EFALYPTVDG DYYTFEELKD
AIKDAQTDKD DKLVILYASD KEQQHSYIEA AKNKGYKVLL LNSPIVSHLL QKMESKNENT
SFVRVDSDAI DTLIKKEDEP ISKLSEEEKE QLKGMLTEII PSEKFSVQLE AMDSDASPFI
ITEPEFMRRM KEMQQTGGGG MFGMGAMPDM FNLVVNTNHE LVGQILNTKT QKKKERLVNQ
ALDLAKLSKN LLKGEEMTRF IRRSYDMIK
//
