HTPG_RHOPS
ID HTPG_RHOPS Reviewed; 628 AA.
AC Q12ZX1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-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=RPD_4402;
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000283; ABE41618.1; -; Genomic_DNA.
DR AlphaFoldDB; Q12ZX1; -.
DR SMR; Q12ZX1; -.
DR STRING; 316057.RPD_4402; -.
DR PRIDE; Q12ZX1; -.
DR EnsemblBacteria; ABE41618; ABE41618; RPD_4402.
DR KEGG; rpd:RPD_4402; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_5; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR BioCyc; RPAL316057:RPD_RS22145-MON; -.
DR Proteomes; UP000001818; 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; 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; Stress response.
FT CHAIN 1..628
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014944"
FT REGION 1..334
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 335..550
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 551..628
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 628 AA; 68759 MW; D718C8FF25F313C7 CRC64;
MTTTDTASET KPFQAEVAEL LNLMVHSVYS ETDIFLRELI SNASDALDKL RYESIATPAL
MEAGGAPKIQ IVPRKAPDTL TVIDNGIGMN RQELIDNLGT IAKSGTKSFL TKLTEAKDGA
GLIGQFGVGF YAAFMVADNI VVTSRRAGSG EVWTWSSSGG AGFEIAPASE EAAARVVRGT
EIVLHLKPDA AKYLEAYQIE RIVSEYSDNI QFPIELVPEE GEPRQINSAS ALWQRSKSEL
TEEDYNQAYK QIAGAFDEPA MTLHYRAEGR QSYAVLLFAP ATKPFDLFEP ERKGRIKLYV
RRVFITADAD LLPPYLRFLR GVIDSEDLPL NLSREMLQNN PQLAQIRKAV TGKVIGELES
LADKKPEDFA RIWEAFGPVL KEGLYEDYER REKLLALARF TTTAGEKRTL SQYVEAMKEN
QTEIYYLVGD SIERLKSNPK LESATARGIE VLLLTDGVDA FWTSGQLDFG GKPLKSLSQG
DVNFDLIPKL DADKPDDKPD ETKADEATVI AVIKDALGER VSDVKASQRL TSSASCLVAG
GFGPDRELEK MLARANKGAA TKPVLEINLG HPLVAALADA KADKADATDL SFLLLEQAQI
LDGELPEDPA AFAGRLNRLV LRGLVAHG