HTPG_CHLL3
ID HTPG_CHLL3 Reviewed; 625 AA.
AC Q3B3E6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Plut_1273;
OS Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS luteolum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=319225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 273 / BCRC 81028 / 2530;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelodictyon luteolum DSM 273.";
RL Submitted (AUG-2005) 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; CP000096; ABB24135.1; -; Genomic_DNA.
DR RefSeq; WP_011358007.1; NC_007512.1.
DR AlphaFoldDB; Q3B3E6; -.
DR SMR; Q3B3E6; -.
DR STRING; 319225.Plut_1273; -.
DR PRIDE; Q3B3E6; -.
DR EnsemblBacteria; ABB24135; ABB24135; Plut_1273.
DR KEGG; plt:Plut_1273; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_1_10; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000002709; 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; Stress response.
FT CHAIN 1..625
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000237000"
FT REGION 1..332
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 333..545
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 546..625
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 625 AA; 70689 MW; 229944FF4F55D52C CRC64;
MSNKQNTAVQ EFEYKAEMKQ LLDLIVHSLY THPEIFLREL VSNASDALSK ARFSALTDDT
MAKVSGEAAI RISLDAKTAA FAIEDTGIGM TEEELIANLG TVARSGTLGF MQALRQEKKE
LDGNLIGQFG VGFYSVFMVT DDVTVETRSA RAGSEGLRWR SSGQGTYTIE KIDKKEPGTR
ISFTLKDEHK EFAEEYRVEH IIKKYSNFVD FPIYLETKQL NSITALWQRP KSELKQEEVN
EFYKFISNDF NEPLDYLHVS VEGAVSFKAI LFLPKEAPME LLYRQGELEN KGPQLYVKKV
MIQHECRDLL PEYLRFIAGV VDTEDLSLNV SREIVQSSPV MSKIRQILTG KILGWFEELA
TAQPEKFRTF YKAFGPIVKI GLNTDFTNRD KLIELLRFES TKTGEGEYVT LKEYAARMAP
DQKEIYYHSG AGRAQLLANP NLEYFQDKGI EVLLLSDPVD VFVIPSIHEY DKKQLKSIEK
ADIDFSKATK DKTEPIAENL LVPLLKIFRE TLGEGIEDVV ESHRLVSSPV TLVSGKDAMD
SQMERMMKMM QQEMPAGRKI LEVNPSHPII RNLSGMMMAN DNNPLIRTAI HQLYEGALLL
EGGLDSTTGF VSRMNELIEA ATLSR