ID HTPG_RICBR Reviewed; 621 AA.
AC Q1RIV1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-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=RBE_0632;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae
RT in gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04713.1; -; Genomic_DNA.
DR RefSeq; YP_537802.1; NC_007940.1.
DR ProteinModelPortal; Q1RIV1; -.
DR STRING; 336407.RBE_0632; -.
DR PRIDE; Q1RIV1; -.
DR EnsemblBacteria; ABE04713; ABE04713; RBE_0632.
DR GeneID; 3995922; -.
DR KEGG; rbe:RBE_0632; -.
DR PATRIC; 17882714; VBIRicBel102610_0724.
DR eggNOG; COG0326; -.
DR HOGENOM; HOG000031989; -.
DR KO; K04079; -.
DR OMA; LTDSPAC; -.
DR ProtClustDB; PRK05218; -.
DR BioCyc; RBEL336407:GJCY-651-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; IPR019805; Heat_shock_protein_90_CS.
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; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Nucleotide-binding; Stress response.
FT CHAIN 1 621 Chaperone protein HtpG.
FT /FTId=PRO_0000258525.
FT REGION 1 328 A; substrate-binding (By similarity).
FT REGION 329 544 B (By similarity).
FT REGION 545 621 C (By similarity).
SQ SEQUENCE 621 AA; 70598 MW; 7730F1715528B5E7 CRC64;
MKQEKKKFDA EVGKILNLMI HSLYSNKEIF MRELISNASD ACDKLRYLSQ SEAELVAGDS
NFKITVKGDK NNGQVIIRDN GIGMNKEDLI ENLGTIARSG TANFLKNLSG DSKKDNMLIG
QFGVGFYSSF MVADKVTVTS RKAGEDKVYV WESEGEGEYI VSSSDREFSR GTEIALHIKK
EEDSFLDHFR LKHIVKSYSD HIAVPIYFFD EGDNNEIQLN SASALWTRSK SEITEEQYKE
FYKSLSYAVD DPWVTMHNKN EGAIEFTNLL FIPSSKTYDL FHPDRKRRVK LYIKRVFISD
ENIDLIPSYL RFLRGVVDSE DLPLNISRES LQHNNVLEKI KNAITKRVLG ELKKKKEDSP
DEYNNFWANF GGALKEGLCE ATTDHEKLLE VCIFRSALHN KMISLDEYIK GFKEGQNTIY
YLSGDNPDKL LSSPQIEGLL SKNIDVLLFT DTVDDFWVNV NSEYKGHTIK SATRSDIDVD
QATSSSEEKN KDDKKSDDEY KSLTDYFKEV LGILVKDVKI SKKLTSSPAC LAVSEAAMDI
RMERFLIEQK QIANASAKNL ELNPKNKIIE KIFNDLKANN KNNEELVKLI FDQACILEGE
PVADTGAFSK RLNDIVQKAI L
//
