ID   HTPG_SERP5              Reviewed;         623 AA.
AC   A8GAV2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Spro_1138;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-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; CP000826; ABV40242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8GAV2; -.
DR   SMR; A8GAV2; -.
DR   STRING; 399741.Spro_1138; -.
DR   PRIDE; A8GAV2; -.
DR   EnsemblBacteria; ABV40242; ABV40242; Spro_1138.
DR   KEGG; spe:Spro_1138; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
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..623
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000060529"
FT   REGION          1..336
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          337..551
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          552..623
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   623 AA;  70744 MW;  B427BBC8ADDB57BB CRC64;
     MSMKGQETRG FQSEVKQLLH LMIHSLYSNK EIFLRELISN ASDAADKLRF RALSAPELYE
     GDGELRVRLS FDKDQRTLTI ADNGIGMNRE EVIENLGTIA KSGTKAFLES IGSDQAKDSQ
     LIGQFGVGFY SAFIVADKVT VRTRAAGAAA DQGVFWESIG EGDYTIADVS KEDRGTEITL
     HLREGEDEYL DAWRLRSVIG KYSDHIALPV EIETKNEEDG TVTWEKINKA QALWTRSKAD
     VTDEEYKEFY KHIAHDFTDP LSWSHNRVEG KQEYTSLLYI PAQAPWDMWN RDHKHGLKLY
     VQRVFIMDEA EQFMPNYLRF VRGLIDSNDL PLNVSREILQ DSRVTQNLRG ALTKRVLQML
     EKLAKDDAEG YQKFWQQFGL VLKEGPAEDA NNKETIAKLL RFASTQSESS AQTVSLEEYV
     GRMAEGQEKI YYITADSYAA AKSSPHLELF RKKGIEVLLL SDRIDEWMMS YLTEFDGKPF
     QSVSKADDAL DKLADETEEQ KAAEKQLEPF VDRVKTLLGD RVKDVRLTHR LTDTPAIVIT
     DADEMSTQMA KLFAAAGQEA PAVKYIFELN PEHALVKRAS DVGDNEQFAE WIDLLLDQAL
     LAERGTLEDP NQFIRRMNKL LSA