ID   HTPG_PSET1              Reviewed;         637 AA.
AC   Q3IKQ2;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=PSHAa1207;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(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; CR954246; CAI86282.1; -; Genomic_DNA.
DR   RefSeq; WP_011327891.1; NC_007481.1.
DR   AlphaFoldDB; Q3IKQ2; -.
DR   SMR; Q3IKQ2; -.
DR   STRING; 326442.PSHAa1207; -.
DR   PRIDE; Q3IKQ2; -.
DR   EnsemblBacteria; CAI86282; CAI86282; PSHAa1207.
DR   KEGG; pha:PSHAa1207; -.
DR   PATRIC; fig|326442.8.peg.1161; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   BioCyc; PHAL326442:PSHA_RS05955-MON; -.
DR   Proteomes; UP000006843; Chromosome I.
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..637
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224221"
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;  72502 MW;  F4FFCBCA8D038779 CRC64;
     MTAAQKETLG FQTEVKQLLN LMIHSLYSNK EIFLRELVSN ASDAADKLRF LALSQGDLYQ
     GDADLRVRIS ADKEANTITI SDNGIGMTRD EVISSLGTIA KSGTAEFFKN LTGDQSKDSQ
     LIGQFGVGFY SAFIVADLVT VRTRKAGETT AYEWESQGEG EYTLQEIEKE GRGTDIILHL
     REEEKEFADE WRLRSIVTKY SDHISTPVQM YKAEVPESEG EDGEKIPAVP GEWESINRAT
     ALWTRDKSEL SDDEYKEFYK HVSLDWEDPL SWAHNKVEGK TEYTSLLYIP KKAPFDLWNR
     DRQSGLKLYV QRVFIMDDAE QFMPSYLRFV KGLLDSNDLP LNVSREILQD NKVTQAIRKG
     CTSRIIKMLE RMAKNKADDY QVFWNEFGQV IKEGPAEDAA NKEAICKLLR FSSTHTDSAT
     QDVSLEQYVE RMNEGQEKIY YVVADTFTAA KNSPHLEIFR KKGIEVLLLS DRVDEWMMSH
     LTEFADKQLQ SITRGDLDLG KLDDEETKKA QEESEKEVAG LVERIKTALG DEVKEVRFTH
     RLTDSPACVV SDDNDMSSQM QKLMESVGQA APEAKPVFEL NPEHQLVKHL NDEQDEDKFA
     QWSHVLLDQA LLAERGTLKD PTGFVTRLNK LMLELSK