HTPG_MANSM
ID HTPG_MANSM Reviewed; 626 AA.
AC Q65RV7;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=MS1696;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016827; AAU38303.1; -; Genomic_DNA.
DR RefSeq; WP_011200864.1; NC_006300.1.
DR AlphaFoldDB; Q65RV7; -.
DR SMR; Q65RV7; -.
DR STRING; 221988.MS1696; -.
DR PRIDE; Q65RV7; -.
DR EnsemblBacteria; AAU38303; AAU38303; MS1696.
DR KEGG; msu:MS1696; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000000607; 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; IPR019805; Heat_shock_protein_90_CS.
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.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT CHAIN 1..626
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000224215"
FT REGION 1..338
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 339..554
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 555..626
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 71306 MW; 89AB73158166AE24 CRC64;
MSNKETCGFQ TEVKQLLQLM IHSLYSNKEI FLRELISNAS DAADKLRFKA LSAPELYEGD
GDLKVRISFD DKKGTLTVSD NGIGMTREQA VDHLGTIAKS GTKEFLSALG NDQAKDSQLI
GQFGVGFYSA FIVADKVEVR SRAAGVAADK GVLWASAGEG EYSVENIEKK DRGTEITLFL
REDEKEFLNE WRLREIIGKY SDHIGLPVEI LTKEYDEEGK ESGVKWEKIN KAQALWTRSK
AEISDDEYKE FYKHISHDFA DPLSWMHNKV EGNQEYTSLL YVPGKAPWDL FNREQKHGLK
LYVQRVFIMD DAEVFMPNYL RFMRGLLDSN DLPLNVSREI LQDNKTTAAL RKALTKRSLQ
MLEKLAKDEP EKYAVFWKEF GLVLKEGVAE DFANKEQIAK LYRFASTHTD SSEQNVSFED
YISRMKEGQK AVYYITADSY VAAKNSPHLE LFNKKGIEVL LLSDRIDEWM LSYLTEFDGK
PLQSVTKADL DLGDLADKEE ENQKEQDEKF DSFIQRVKSL LGERVKDVRI THRLTDTPAV
VSTDNDQMTT QMAKLFAMSG QPVPEVKYTF EINPQHELVK KAAKVTDETE FGDWIELLLN
QAMLAERGSL ENPVAFIKLV NALLAK