ID   A0A077EA02_9FLAO        Unreviewed;       631 AA.
AC   A0A077EA02;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Chaperone protein HtpG {ECO:0000313|EMBL:AIL44362.1};
GN   ORFNames=BD94_0587 {ECO:0000313|EMBL:AIL44362.1};
OS   Elizabethkingia anophelis NUHP1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Elizabethkingia.
OX   NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL44362.1, ECO:0000313|Proteomes:UP000028933};
RN   [1] {ECO:0000313|EMBL:AIL44362.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NUHP1 {ECO:0000313|EMBL:AIL44362.1};
RX   PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9;
RA   Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M., Lin R.T.,
RA   Yang L.;
RT   "First case of E anophelis outbreak in an intensive-care unit.";
RL   Lancet 382:855-856(2013).
RN   [2] {ECO:0000313|EMBL:AIL44362.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NUHP1 {ECO:0000313|EMBL:AIL44362.1};
RX   PubMed=26019164; DOI=10.1093/gbe/evv101;
RA   Li Y., Liu Y., Chew S.C., Tay M., Salido M.M., Teo J., Lauro F.M.,
RA   Givskov M., Yang L.;
RT   "Complete Genome Sequence and Transcriptomic Analysis of the Novel Pathogen
RT   Elizabethkingia anophelis in Response to Oxidative Stress.";
RL   Genome Biol. Evol. 7:1676-1685(2015).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; CP007547; AIL44362.1; -; Genomic_DNA.
DR   RefSeq; WP_024564599.1; NZ_CP007547.1.
DR   AlphaFoldDB; A0A077EA02; -.
DR   STRING; 1338011.BD94_0587; -.
DR   KEGG; eao:BD94_0587; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_2_10; -.
DR   Proteomes; UP000028933; 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; 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   631 AA;  71660 MW;  F922A62C1BBEEB6A CRC64;
     MAKGNINVSV ENIFPLIKKF LYSDHEIFLR ELISNATDAT LKLKHLTSIG EAKVEYGNPK
     IEVKIDKDNK TLHIIDQGLG MTAEEVEKYI NQVAFSGAEE FLEKYKDSAK DSGIIGHFGL
     GFYSAFMVAD KVEIISKSYK EGESAVHWTC DGSPEFTLEE TTAKTDRGTE IILHIAEDST
     EFLEESRIRE LLLKYNKFMP VPIKFGMKTE TLPLPEGAAE DAKPETIEVD NIINNPNPAW
     TKSPSELTNE DYQKFYHELY PMQFEEPLFN IHLNVDYPFN LTGILFFPKL GNNLNIEKDK
     IQLYQNQVFV TDEVKGIVPD FLMLLRGVID SPDIPLNVSR SYLQADGAVK KISSYITKKV
     ADKMVSLINE NREDYEKKWN DIKVVIEYGM ISEDKFYEKS DKFALYPTTD GKHYLWEELT
     EKIKPLQTDK DGKLVVLYAS NTNEQDSYIQ NAKAKGYEVL LLDSPIIPHL IQKLESSKEN
     ISFARVDADH INNLIKKDEP VIAKLNDTEK ETLKKSVEEA VNDQAYTVQL EDLDSDDAPF
     IITQPEFMRR MKDMQMTGGG GMFAMGGFPD MYNLVVNANS DLATGILKTE NTEDKNALVK
     QALDLAKLSQ NLLKGKDLTD FIQRSFAQLK K
//