ID   HTPG_PHOPR              Reviewed;         634 AA.
AC   Q6LTE2;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=PBPRA1023;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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; CR378666; CAG19434.1; -; Genomic_DNA.
DR   RefSeq; WP_011217768.1; NC_006370.1.
DR   AlphaFoldDB; Q6LTE2; -.
DR   SMR; Q6LTE2; -.
DR   STRING; 298386.PBPRA1023; -.
DR   PRIDE; Q6LTE2; -.
DR   EnsemblBacteria; CAG19434; CAG19434; PBPRA1023.
DR   KEGG; ppr:PBPRA1023; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000593; Chromosome 1.
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..634
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224220"
FT   REGION          1..344
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          345..561
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          562..634
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   634 AA;  71856 MW;  A007AD70A700D6BB CRC64;
     MSEQGTHINK ETRGFQSEVK QLLHLMIHSL YSNKEIFLRE LISNASDAAD KLRFRALSQP
     DLFENDADIG VKLSFNAEAG TLTVSDNGIG MNRDDVIEHL GTIAKSGTKD FFSKLSNDES
     KDSQLIGQFG VGFYSSFIVA KSVTVNTRAA GEAADKGVSW TSEGEGDYTV EDINKTTRGT
     DIILHLRDDE AEFLNEHRLR DIIGKYSDHI GIPVHILVTE NDDEGKPTGS KWEQINKAQA
     LWTRNKSEIT EEEYKEFYNH VSHDFAEPLT WSHNRVEGTQ DYTSLLYVPS KAPWDMNNRD
     SKHGLKLYVQ RVFIMDDAQQ FMPSYLRFMR GLIDSNDLPL NVSREILQDN KVTQALRKAS
     TKRALTMLDR MAKNDAEKYQ TFWTEFGQVL KEGPAEDFSN REKIANLLRF SSTHNDTADQ
     TVSVADYVSR MKEGQEKIYF LTADSFTAAK NSPHLEQFRA KGLEVILMHD RIDEWLMSQL
     PEFDGKPFQA ITKADLDLSK FENEEDKEKQ KEAAEEFKSV VERAKGYLGT RVKDVRTTFK
     LHDTPAVVVT DENEMGTQMA KLLAAAGHDA PEVQYIFEIN PEHGLVKQMA NEADEETFGR
     WVELLLGQAM LAERGSLEDP SQYVAAVNKL LTKV