ID HTPG_RHORT Reviewed; 626 AA.
AC Q2RYB8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
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=Rru_A0072;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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; CP000230; ABC20877.1; -; Genomic_DNA.
DR RefSeq; WP_011387833.1; NC_007643.1.
DR RefSeq; YP_425164.1; NC_007643.1.
DR AlphaFoldDB; Q2RYB8; -.
DR SMR; Q2RYB8; -.
DR STRING; 269796.Rru_A0072; -.
DR EnsemblBacteria; ABC20877; ABC20877; Rru_A0072.
DR KEGG; rru:Rru_A0072; -.
DR PATRIC; fig|269796.9.peg.126; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_5; -.
DR PhylomeDB; Q2RYB8; -.
DR Proteomes; UP000001929; 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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..626
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000237002"
FT REGION 1..329
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 330..549
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 550..626
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 68834 MW; 3C274C85F1108EDD CRC64;
MSEETLSFQA EVSKLLDIVV HSLYSDRKIF LRELISNASD ACDKLRYEGL TQPALLEGDG
AFRIRLSIDA EAGTLTIADN GIGMNRHELI ENLGTIARSG TQAFAEALKA KSQAASGDVS
LIGQFGVGFY SAFMVADKVE VVTRRAGEAQ GWRWSSDGKG SFSVSEVEGA GRGAAITLHL
REDARDFLDE HRLREIVKTY SDHIAIPVDY AGKEGEPERL NEASALWTRP RDQITDEQYA
EFYHHVAHGF ETPWHTLHYR AEGKLEYTAL LFVPGQQPFD LFTQDRKPRV KLYVNRVFIT
DDCEELLPSY LRFVRGVVDS SDLPLNVSRE MLQDDPRLRK IKGGLTKRLI DDLAKRARDD
ESAYLTFWEN FGAVLKEGIY EDFERKEDLV ALARFRTTAS DTPVSLETVI GRMKEGQSAL
YYITGDDATA LARSPQVEGF VARGVEVLLL TDPIDEFWVS AVPKVGDTAL KAVAQGSADL
ERLALIDGKQ PPDDAEHAPA ETAKMDALIA AMKAALGTAV ADVRVSARLT DSPVCLVAKE
GAMSLHLQKL LRQANQGSEL SGDRVLEINP RHALVKTLAE RAATGGSVDE AALLLMDQAR
ILEGEAPADA IAFARRLTEV MGKGLI
//