ID   HTPG_SHELP              Reviewed;         639 AA.
AC   A3QF50;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=Shew_2232;
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000606; ABO24098.1; -; Genomic_DNA.
DR   RefSeq; WP_011866030.1; NC_009092.1.
DR   AlphaFoldDB; A3QF50; -.
DR   SMR; A3QF50; -.
DR   STRING; 323850.Shew_2232; -.
DR   EnsemblBacteria; ABO24098; ABO24098; Shew_2232.
DR   KEGG; slo:Shew_2232; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001558; 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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..639
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000014955"
FT   REGION          1..347
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          348..564
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          565..639
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   639 AA;  71857 MW;  4F06C5EECCCFB77E CRC64;
     MSHQETHGFQ TEVKQLLNLM IHSLYSNKEI FLRELVSNAA DAADKLRYEA LTKDELYEGD
     GELRVRVSAD SEKGTVTIED NGIGMTRDGV IEHLGTIAKS GTAEFFKNLS GDESKDSQLI
     GQFGVGFYSA FIVADKVTVR TRAAGHAADE AVQWESAGEG EFTVENIVKE SRGTEIILHL
     REEEKEFASD YRLRSIITKY SDHISVPVEM WQEGTPAQEA TEEGGEAIPA TEGHWKAMNK
     ATALWTRNKS DVTDEEYQEF YKHISHDFAD PLLWSHNRVE GKQEYTSLLY IPSKAPWDLW
     NRDRKHGLKL FVQRVFVMDD AEQFMPSYLR FVQGLIDSND LPLNVSREIL QDNKITTALR
     TAVTKRVLGM LEKLAKNDPE KYQTFWAEFG QVLKEGPAED FANKEKIAGL LRFASTHTNE
     AAHTVSLSDY VERMKEGQSK IYYIVADSHE AAANSPHLEL LRKKGIEVLL MSERIDEWLI
     NHLSEFDGKQ LHSVTRGDLE LGELEDAAEK EAQEKLETES EGLVKRVKEV LGDKVAEVKV
     TSRLTDTPAC VVAGAGEMSS QMIKLMQAAG QAVTESKPVF ELNPEHPLVK RLDTEQDEEV
     FGQWAELLLQ QAQLSEKGSL ADPSAFIKLM NKMLLASVK