ID   HTPG_PSYCK              Reviewed;         666 AA.
AC   Q1Q978;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Pcryo_1998;
OS   Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS   / K5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=335284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL   Submitted (MAR-2006) 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; CP000323; ABE75775.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1Q978; -.
DR   SMR; Q1Q978; -.
DR   STRING; 335284.Pcryo_1998; -.
DR   PRIDE; Q1Q978; -.
DR   KEGG; pcr:Pcryo_1998; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000002425; 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; 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   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT   CHAIN           1..666
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000258518"
FT   REGION          1..374
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          375..593
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          594..666
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   666 AA;  74747 MW;  4970000F1FB1F98F CRC64;
     MSELNPVDNQ KVDSINVDKS SPELKKHTFE AEVAQLLHLV THSLYSNSDI FVRELVSNAS
     DACDKLRFEA TNDDSLYEDD GELKIRIAVD EDAKTITFTD NGIGMNEADA IENLGTIAKS
     GTKAFLDKLS ESQKQDGQLI GQFGVGFYSG FIVADTISVE TRKAGEPADK GVRWVSDGTG
     SFTVEPITKE TRGTAITLHL KEQYSEGEES YLDRGKIKQL VNKYSDHISL PIQMRKEVWQ
     EDEVEEGSDT PANGQMVLTD EWETINKASA LWTRSASEIE DEEYIDFYKN ITYDMDAPLA
     WTHNRVEGRV QYTQLLYIPK KAPVDLYTRE QQHGLKLYVK RVFIMDEAEQ LLPMYLRFVK
     GVIDSADLPL NVSRELLQES RDVKSIRDGN ARRILTLLAS LANSEDSDKQ EKFAQFYAEF
     GDVIKEGVGE DMGNQERIAK LLRYATSTQD SVTTSFEDYK ARMKEGQKAI YYLTADNLAA
     AKNSPQLELF KKKGIEVILM TSRVDEWAMN FLTSFDETPL QNIAKGAVDL GDLQDEAEKA
     EAEKAQETMK PIVDKLKTAL GERAKDVKVS TRLVDSPACL VVGEGELSPQ MIQMLKQMGQ
     DVPESKPTLE VNPDHPLIKK LESSEQSAED FDKLAQVIFD QALLADGGQL DDPAAYLRRV
     NELLMR