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 01-MAY-2013, entry version 47.
DE RecName: Full=Chaperone protein HtpG;
DE AltName: Full=Heat shock protein HtpG;
DE AltName: Full=High temperature protein G;
GN Name=htpG; OrderedLocusNames=RPD_4402;
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
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.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA Lykidis A., Oda Y., Harwood C.S., 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 (By
CC similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
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DR EMBL; CP000283; ABE41618.1; -; Genomic_DNA.
DR RefSeq; YP_571519.1; NC_007958.1.
DR ProteinModelPortal; Q12ZX1; -.
DR STRING; 316057.RPD_4402; -.
DR PRIDE; Q12ZX1; -.
DR EnsemblBacteria; ABE41618; ABE41618; RPD_4402.
DR GeneID; 4024927; -.
DR KEGG; rpd:RPD_4402; -.
DR PATRIC; 23284050; VBIRhoPal120395_4569.
DR eggNOG; COG0326; -.
DR HOGENOM; HOG000031989; -.
DR KO; K04079; -.
DR OMA; LTDSPAC; -.
DR ProtClustDB; PRK05218; -.
DR BioCyc; RPAL316057:GHDC-4473-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0006457; P:protein folding; IEA:HAMAP.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1; -.
DR InterPro; IPR003594; HATPase_ATP-bd.
DR InterPro; IPR001404; Hsp90.
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; SSF55874; ATP_bd_ATPase; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR PROSITE; PS00298; HSP90; FALSE_NEG.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Nucleotide-binding; Stress response.
FT CHAIN 1 628 Chaperone protein HtpG.
FT /FTId=PRO_1000014944.
FT REGION 1 334 A; substrate-binding (By similarity).
FT REGION 335 550 B (By similarity).
FT REGION 551 628 C (By similarity).
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
//
