ID   HTPG_ALIF1              Reviewed;         631 AA.
AC   Q5E6Q9;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE   AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=VF_0792;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_00505}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00505}.
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DR   EMBL; CP000020; AAW85287.1; -; Genomic_DNA.
DR   RefSeq; WP_011261487.1; NC_006840.2.
DR   RefSeq; YP_204175.1; NC_006840.2.
DR   AlphaFoldDB; Q5E6Q9; -.
DR   SMR; Q5E6Q9; -.
DR   STRING; 312309.VF_0792; -.
DR   EnsemblBacteria; AAW85287; AAW85287; VF_0792.
DR   KEGG; vfi:VF_0792; -.
DR   PATRIC; fig|312309.11.peg.784; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000537; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.790; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
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_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..631
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224235"
FT   REGION          1..342
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          343..559
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          560..631
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   631 AA;  71628 MW;  4BAF739C4015A63B CRC64;
     MSEQTANKET RGFQSEVKQL LHLMIHSLYS NKEIFLRELI SNASDASDKL RFKALSNGDL
     YEGNADLGVK LSFNEAANTL TISDNGIGMS REDVIEHLGT IAKSGTADFF SKLSEDQSKD
     SQLIGQFGVG FYSAFIVADA VTVRTRAAGS EKDQGVQWHS EGEGDYTIED ITKESRGTDI
     ILHMREEGKE FLNEWRLKEV IGKYSDHIGI PVSIWTVEKD EEGKDKEGKW EQVNKAQALW
     TRSKSDIEDA EYQEFYKHVS HDFADPLTWS HNKVEGKNDY TSLLYIPAKA PFDMMNRDHK
     SGLKLYVQRV FIMDDAEQFM PTYLRFVKGL IDSNDLPLNV SREILQDNKV TQSLRSACTK
     RVLGMLEKMA KKDDEKYLTF WKQFGQVLKE GLAEDLANKE KIAGLLRFAT TEKDSSEQAL
     GLAGYVERMK EEQDKIFYLT ADSYAAAKNS PHLEQFKAKG IEVVLMYDRI DEWLMSYLTE
     FDGKQFQSIT KAGLDLSKFE DEAEKEKHKE TEEEFKSVVE RTKSYLGDRV KEVRTTFKLA
     TTPAVVVTDD FEMGTQMAKL LEAAGQAAPE VKYIFEINPD HALVKQMADE ADEEAFGRWV
     EMLLGQAMLA ERGSLEDPSQ FLSAMNQLLA K