ID   HTPG_PSYA2              Reviewed;         656 AA.
AC   Q4FQZ1;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 112.
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=Psyc_1719;
OS   Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=259536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX   PubMed=20154119; DOI=10.1128/aem.02101-09;
RA   Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA   Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA   Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA   Murray A., Thomashow M., Tiedje J.M.;
RT   "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT   Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT   temperature growth.";
RL   Appl. Environ. Microbiol. 76:2304-2312(2010).
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; CP000082; AAZ19567.1; -; Genomic_DNA.
DR   RefSeq; WP_011280980.1; NC_007204.1.
DR   AlphaFoldDB; Q4FQZ1; -.
DR   SMR; Q4FQZ1; -.
DR   STRING; 259536.Psyc_1719; -.
DR   PRIDE; Q4FQZ1; -.
DR   EnsemblBacteria; AAZ19567; AAZ19567; Psyc_1719.
DR   KEGG; par:Psyc_1719; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000546; 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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..656
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224225"
FT   REGION          1..364
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          365..583
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          584..656
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   656 AA;  73615 MW;  0EDC0AC2EF7679CB CRC64;
     MSEQNPTDSK NPELKKHTFE AEVAQLLHLV THSLYSNSDI FVRELVSNAS DACDKLRFEA
     TNDDSLYEDD GELRIRIAVD EDAKTITFTD NGIGMNEADA IENLGTIAKS GTKAFLDKLS
     DSQKQDGQLI GQFGVGFYSG FIVADTISVE TRKAGDAAEN GVRWVSDGTG SFTVENISKT
     ERGSSITLHL KEQYSEGEDG YLDRSKIKRL VNKYSDHISL PIQMRKEIWQ EDEVEEGDDT
     PANGQMVLTD EWETINKASA LWTRTASDVE DDEYVDFYKN ITYDMDAPLT WTHNRVEGRV
     QYTQLLYIPK KAPVDLYTRE QQHGLKLYVK RVFIMDDAEQ LLPMYLRFVK GVIDSADLPL
     NVSREILQES RDVKSIRDGN ARRILTLLAS LANSEDADKQ EKFAQFYAEF GDVIKEGVGE
     DMGNQERIAK LLRYATSTQD GEMTSFEDYK ARMKDGQKAI YYLTADNLAA AKNSPQLELF
     KKKGIEVILM TSRVDEWAMN FLTSFDETPL QNIAKGAVDL GDLQDEAEKA EAEKAQETMK
     PVVDKLKAAL GDRAKDVKVS TRLVDSPACL VVGEGELSPQ MIQMLKQMGQ DVPESKPTLE
     VNPDHPLIKK LESSEQSAED FDKLAQVIFD QALLADGGQL EDPAAYLRRV NELLMK