ID   HTPG_ACIAD              Reviewed;         640 AA.
AC   Q6FF82;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=ACIAD0316;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67275.1; -; Genomic_DNA.
DR   RefSeq; WP_004920581.1; NC_005966.1.
DR   AlphaFoldDB; Q6FF82; -.
DR   SMR; Q6FF82; -.
DR   STRING; 62977.ACIAD0316; -.
DR   EnsemblBacteria; CAG67275; CAG67275; ACIAD0316.
DR   GeneID; 45232829; -.
DR   KEGG; aci:ACIAD0316; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_6; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   BioCyc; ASP62977:ACIAD_RS01500-MON; -.
DR   Proteomes; UP000000430; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..640
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000224193"
FT   REGION          1..352
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          353..571
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          572..640
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   640 AA;  71979 MW;  ECF4959752990BE8 CRC64;
     MTEQTATQNY SFQAEVAQLL HLVTHSLYSN PEIFLRELIS NASDACDKLR FEGINHPEYY
     EDDANLRVRV SLDKENKTIT ISDNGIGLSQ QEAIDNLGTI AKSGTKDFMS KLTGDQKSDA
     QLIGQFGVGF YSGFIVADKI TVESRRAGLP ANDGVRWISG GTGDFEVQQI TKDSRGTSII
     LHLRDDALDY LDAWKVKQII NKYSDHISLP IEMQKEVWQE EEVAEGEEPK GGQYVKTDEW
     EVINSASALW TRSKNEISEE QYIEFYKNLT HDFDAPLAWS HNRVEGNTEY TQLLYIPAKA
     SSDIFTREAK AGIKLYVKRV FIMDDADNLI PNYLRFVKGV IDSADLPLNV SRELLQESRD
     VKTIREGNTR RVLTLLDGLA KSEDEKDQEK FKTFYQEFGS VLKEGLGEDF TNRERILKLL
     RYATSNQDEI STSFADYKAR MKEGQKAIYY VSADSLAAAK NSPQLELFKK KGIEVLLMSE
     RVDEWAMNFV HEFDGTPLQN VSKGAVDLGD LQDAEEKKAL EQAAEQFKPV VDKLTDALKD
     KTKEVRVTTR LVDSPACLVT SDGELSPQLI RMLKQAGQAV PESKPILEIN PEHPLVQKLE
     GSAQFDDLAN VIFDQAVIAE GGLPEDPAAY VKRINSLLLK