HTPG_CHLCH
ID HTPG_CHLCH Reviewed; 629 AA.
AC Q3ARP2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=Cag_1071;
OS Chlorobium chlorochromatii (strain CaD3).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=340177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CaD3;
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 Chlorobium chlorochromatii CaD3.";
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; CP000108; ABB28333.1; -; Genomic_DNA.
DR RefSeq; WP_011362097.1; NC_007514.1.
DR AlphaFoldDB; Q3ARP2; -.
DR SMR; Q3ARP2; -.
DR STRING; 340177.Cag_1071; -.
DR PRIDE; Q3ARP2; -.
DR EnsemblBacteria; ABB28333; ABB28333; Cag_1071.
DR KEGG; cch:Cag_1071; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_10; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
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..629
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000236989"
FT REGION 1..336
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 337..549
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 550..629
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 629 AA; 71711 MW; 743260AEFE564AF0 CRC64;
MSSTENNGTA VPLQEFEYKA EMKQLLDLII HSLYTHPEIY LRELISNASD ALSKARFNAL
TDQDMLDKDA ELAIRLTLNA EEKSVVIEDS GIGMTEEELI ANLGTVAKSG TLGFMQSLKE
QQQQLDGNLI GQFGVGFYSV FMVTEEVTVE TRSFHSNAQG YRWRSSGQGT YTIEQIDKAT
RGTRISFKLK EEHQEFAEEY RVEQIIKKYS NFVDFPIYLG ERQLNSMTAL WQRPKSELKD
EEVNEFYKFV ASDFNDPLDY LSISVEGMVS FKALLFLPKE APPELMYRQS ELENRGPQLY
VKKVLIQNEC RDLLPEYLRF IAGVVDTEDL SLNVSREMVQ SSPVMAKIRQ ILTGKILGWF
EMLAKEQPEK FKTFYKAFGP IIKIGLNTDF TNREKLIELL RFESTKTEEG EFVTLREYVE
RMGSEQKEIY YHSGNNRAQL LAHPNIEYFR EHGIEVLLLS DPVDMFVIPS IHEFDKKPLK
SIEKADCDFS QQSSNKAEPV APNLLNPVLQ AFKEALSNEV EDVVESRRLV SSPVTLVSGK
DAIDSQLERM MKMMNTPMPP AKRILEVNSS HPIVRNIAGM IMADANNPLI KTVARQLYEG
ALFLEGSLED ATSYVTRMNE LIEAATLTR