ID   HTPG_SHEB9              Reviewed;         637 AA.
AC   A9L569;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 79.
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};
GN   OrderedLocusNames=Sbal195_2663;
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195;
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., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-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; CP000891; ABX49831.1; -; Genomic_DNA.
DR   RefSeq; WP_006086212.1; NC_009997.1.
DR   AlphaFoldDB; A9L569; -.
DR   SMR; A9L569; -.
DR   EnsemblBacteria; ABX49831; ABX49831; Sbal195_2663.
DR   GeneID; 11772753; -.
DR   KEGG; sbn:Sbal195_2663; -.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000770; 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..637
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000081526"
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..637
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   637 AA;  71663 MW;  ABF129F430F73C28 CRC64;
     MSQQETHGFQ TEVKQLLHLM IHSLYSNKEI FLRELVSNAA DAADKLRYLA LTNDALYEGD
     GELRVRISAD KEKGTVTIED NGVGMTRDGV IEHLGTIAKS GTADFFKNLS GESSKDSQLI
     GQFGVGFYSA FIVAKKVTVR TRAAGHKADE AVLWESEGEG NFTVDTITKA SRGTEITLHL
     RDEEKEFADD WRLRSIITKY SDHISVPVEM WQEGTPESDG ADGEKIPATE GQWKVMNKAT
     ALWMRSKADI SDEEYQEFYK HISHDYTDAL LWSHNRVEGK QEYTNLLYIP AKAPWDMWNR
     DRKHGLKLFV QRVFIMDDAE QFMPSYLRFV QGLIDSNDLP LNVSREILQD NHVTKAMRTG
     ITKRVLGMLE KLAKDDAEKY QQFWAEFGQV LKEGPAEDFA NRERIAGLLR FASTHTGSAA
     PTVSLDDYIS RMKEGQTKIY YIVADSHEAA ANSPHLELLR KKGIEVLLMS ERIDEWLINH
     LTEYKEKQLH SVTRGDLELG ELEDASEKEA QEKLEQESVA LVERIKAALG STVADVKVTS
     RLTDTPACVV AGEGEMSTQM IKLMQAAGQP VPEVKPTFEI NPAHPLVSRL NDLQDEAAFA
     DWSNLLLQQA QLSEKGSLAD PSAFIKLMNQ MLLANMK