ID   HTPG_PSYIN              Reviewed;         634 AA.
AC   A1STI2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Ping_0956;
OS   Psychromonas ingrahamii (strain 37).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000510; ABM02797.1; -; Genomic_DNA.
DR   RefSeq; WP_011769360.1; NC_008709.1.
DR   AlphaFoldDB; A1STI2; -.
DR   SMR; A1STI2; -.
DR   STRING; 357804.Ping_0956; -.
DR   EnsemblBacteria; ABM02797; ABM02797; Ping_0956.
DR   KEGG; pin:Ping_0956; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000639; Chromosome.
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..634
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014941"
FT   REGION          1..345
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          346..562
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          563..634
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   634 AA;  71501 MW;  FF00B7C9F8479F9D CRC64;
     MEHQQNHTFS ADTGKLLKLM IHSLYSNKEI FLRELVSNAA DAADKLRFKA LSDGSLFEND
     GDLRVRLSFD ADLKTITISD NGIGMSRDEV IEHLGTIAKS GTSDFFEQLS GDQVKDSQLI
     GQFGVGFYSS FIVADKVTVN TRKAGEPASQ GTCWISTGES DYTVADIEKA GRGTEITLHL
     RDDETEFLND YKLRGIVSKY SDHISIPVEM FKEATEESEG SDGEKVPATE ATWEAVNKAT
     ALWSCSKSEL KDEEYKEFYK HIANDFEDPL TWSHNKVEGE QAYTSLLYIP KRAPYDLWNR
     EKAHGLKLYV QRVFVMDDAE QFMPTYLRFV KGVLDSNDLP LNVSREILQD TRVTAKLRSG
     CTKRVLDLLT KLAKKDDDAY NLFWKEFGQV LKEGPAEDSS NKEKIGKLFR FSSTETDSTE
     QTVSLDAYIS RMTEGQDKIY YITADSFNAA KNSPHLEVLR EKGIEVLLLS DRIDEWLLSH
     LPEYDGKTFT SVTQGDLDLG KLDSEEKKKE QEKQETEFAS FVERVKAVLG DKVKDVRLTH
     RLTSTPSCIV ADNDDMSTQM AKLMAQMGQP VPESKPVFEL NPEHVMIVKL ADMADEDLFA
     QWSELLLEQA ILSEKGSLDD PSEFVGRINK LLLA