ID   HTPG_YERPS              Reviewed;         624 AA.
AC   Q66DP8;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=YPTB0995;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH20235.1; -; Genomic_DNA.
DR   RefSeq; WP_002208601.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66DP8; -.
DR   SMR; Q66DP8; -.
DR   EnsemblBacteria; CAH20235; CAH20235; YPTB0995.
DR   KEGG; yps:YPTB0995; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001011; 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; Stress response.
FT   CHAIN           1..624
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224240"
FT   REGION          1..336
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          337..552
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          553..624
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   624 AA;  71031 MW;  6E357E8B9C0F16F7 CRC64;
     MNMKGQETRG FQSEVKQLLH LMIHSLYSNK EIFLRELISN ASDAADKLRF RALSNPELFE
     GDGELRVRLS FDKEKRTLTL SDNGIGMTRD EVIDNLGTIA KSGTKAFLES IGSDQAKDSQ
     LIGQFGVGFY SAFIVADKVT VRTRAAGAPA DTGVFWESAG EGDYTIADIT KDERGTEITL
     HLREGEDEYL DDWRLRSVIS KYSDHIALPV EIQVKNEEDG TVTWEKINKA QALWTRGKAE
     ISDDEYKAFY KHIAHDFTDP LSWSHNRVEG KQEYTSLLYI PAQAPWDMWN RDHKHGLKLY
     VQRVFIMDEA EQFMPNYLRF VRGLIDSNDL PLNVSREILQ DSRITQNLRS ALTKRVLQML
     EKLAKDDAEK YQQFWQQFGM ALKEGPAEDG SNKETIAKLL RFASTHTDSS AQTVSLEDYV
     SRMAEGQEKI YYITADSYAA AKSSPHLELF RKKGIEVLLL SDRIDEWMMS YLTEFEGKAF
     QSVSKADDSL NKLADEENPE QQEAEKALEP FVERVKTLLG ERVKDVRLTH RLTDTPAIVT
     TDADEMSTQM AKLFAAAGQQ APEVKYIFEL NPDHGLVKRA AEVTDDTQFA QWVELLLDQA
     LLAERGTLED PNQFIRRMNQ LLTA