HTPG_CHLPD
ID HTPG_CHLPD Reviewed; 626 AA.
AC A1BFP7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
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};
GN OrderedLocusNames=Cpha266_1188;
OS Chlorobium phaeobacteroides (strain DSM 266).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266;
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., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) 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; CP000492; ABL65224.1; -; Genomic_DNA.
DR RefSeq; WP_011745048.1; NC_008639.1.
DR AlphaFoldDB; A1BFP7; -.
DR SMR; A1BFP7; -.
DR STRING; 290317.Cpha266_1188; -.
DR EnsemblBacteria; ABL65224; ABL65224; Cpha266_1188.
DR KEGG; cph:Cpha266_1188; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_10; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000008701; 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; 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; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
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; Reference proteome;
KW Stress response.
FT CHAIN 1..626
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014909"
FT REGION 1..332
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 333..546
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 547..626
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 71107 MW; EAB0C22FCEF6F348 CRC64;
MTNNDTPGMR EYEYKAEMKQ LLELIVHSLY THPEIFLREL ISNASDALSK VRFNALTDES
IINSDAGLAI RITLDPEAHT IVIEDNGTGM TEEELILNLG TVARSGTLGF LQALKEQQKE
LDGNLIGQFG VGFYSVFMVT DEVTVETRSS GADSAGYRWR SGAAGTFTIE RIEKEQRGTK
ISFALKDEFK EFSEAYRIEQ IIRKYSNFVD FPIFLGDNQI NTISALWQRS KNEVSDEERN
EFYKFLSNDF NPPLDSLHLS VEGKVCFKAL LFLPEEAPPE LMYRQGDLES RGPQLYVKKV
LIQQECRDLL PEYLRFVAGV VDTEDLPLNV SREVVQSSKV MANIRQILTG KILSWFESMA
TDQPEKFRKF YKAFGPFLKI GLNTDFTHRD RIIGLMRFES TKTAEGEYVT FKEYVERMEA
GQNEIYYHSG SNRIQLLAHP NLEYFQHKGI EVLLLSDPVD VFVIPSIHEY DKKPLKSIEK
ADIDFTRTGD DKTEPPLPET LSQPLLGLFR QTIGDVIEDV VESHRLVSSP VTLVSGKDSL
DSSMEKMMKM MHAEMPAAKK ILEVNTSHPI IKNLSGMIMA NEHNPLIRTV IQQLYDGALL
HEGNLDATTG FLQRMNELIE AATMSR