ID   A0A1Y0MTK2_9FLAO        Unreviewed;       635 AA.
AC   A0A1Y0MTK2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:ARV13734.1};
GN   ORFNames=BTO07_00630 {ECO:0000313|EMBL:ARV13734.1};
OS   Polaribacter sp. SA4-12.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1312072 {ECO:0000313|EMBL:ARV13734.1, ECO:0000313|Proteomes:UP000195470};
RN   [1] {ECO:0000313|EMBL:ARV13734.1, ECO:0000313|Proteomes:UP000195470}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA4-12 {ECO:0000313|EMBL:ARV13734.1,
RC   ECO:0000313|Proteomes:UP000195470};
RA   Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (DEC-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; CP019334; ARV13734.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0MTK2; -.
DR   OrthoDB; 9802640at2; -.
DR   Proteomes; UP000195470; 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:UP000195470}.
SQ   SEQUENCE   635 AA;  71508 MW;  E15E3FDE27CEFCEF CRC64;
     MAKGNINVSV ENIFPLIKKF LYSDHEIFLR ELISNGTDAT SKLKHLIAIG EAKTELGDAK
     IEISIDKDAK TITIKDQGLG MTADEVEKYI NQIAFSGAEE FLDKYKDNEA GIIGHFGLGF
     YSAFMVADKV ELITKSFKDA PAAHWTCDGS PEFTLVEHEK SDRGTEIILH IAEDSLDFLE
     DSKIEGLLNK YNRFNQVPIK FGTKEINDPE FTPATTKDAE GKETTEAHKQ ITVDKIINNT
     EPAWTKAPAD LSDEDYENFY RELYPMQFEE SLFHIHLNVD YPFNLTGILF FPKLSTSMDM
     QKDKIQLYQN QVFVTDNVEG IVPDFLQMLK GVIDSPDIPL NVSRSGLQAD GAVKKISGYI
     TKKVADKLSS LFKKDRPDFE KKWNDIKVII EYGMLSEDKF FDKAKKFALY PTVTDSYFTF
     DELIEKTKDS QTDKEGNHVV LYTSNKEAQH SYIQEATAKG YEVLVLDSPI ISHLMQKLEG
     AGEKVKFSRV DADHIDNIIK KDDNVISKLS DEEKETLKPI IEAAVPSKTY TVQLEAMDSA
     SSPFMITVPE FMRRMKEMQA SGGGGGMMGM GNFPDMYNLV VNTNSPLVSE ILNNKDEAAQ
     KGLISQAFDL AKLSQNLLHG EDLTNFIKRS YELIK
//