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HTPG_RHORT
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   25-MAY-2022, entry version 90.
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; Proteobacteria; 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   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
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: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..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
 
 
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