HTPG_SULNB
ID HTPG_SULNB Reviewed; 620 AA.
AC A6QBI2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=SUN_1894;
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum; unclassified Sulfurovum.
OX NCBI_TaxID=387093;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009179; BAF72841.1; -; Genomic_DNA.
DR RefSeq; WP_012083657.1; NC_009663.1.
DR AlphaFoldDB; A6QBI2; -.
DR SMR; A6QBI2; -.
DR STRING; 387093.SUN_1894; -.
DR EnsemblBacteria; BAF72841; BAF72841; SUN_1894.
DR KEGG; sun:SUN_1894; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_7; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 246194at2; -.
DR Proteomes; UP000006378; 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; 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; Reference proteome;
KW Stress response.
FT CHAIN 1..620
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000014961"
FT REGION 1..339
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 340..546
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 547..620
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 620 AA; 70620 MW; A761F50BDFDCAEA7 CRC64;
MAKHQFQTEI GQLLKLMTHS LYSNKEIFIR ELISNASDAL DKFNYLSLTD EKFKEENWSG
KISIKLDKDD NSLTIGDNGI GMNEEDLMDN LGTIAKSGTK AFMENLTGDA KKDSNLIGQF
GVGFYSVFMV AEKVDVISKK AGEEQAYMFS TDGTGEYEVK PVTKDEHGTV IYIKLKEDEK
EFLDKWRVQE VVKKYSNHIA YPIILNYTEE ETTGEGDEKE TKTVQKSEQI NEATALWTLP
KSELKEEDYI EFYKTISHGD DEPLTYLHNK VEGANEFTTL FYIPKKAPMD LYRADYQPGV
KLYVKRVFIT DDDKELLPPY LRFVRGIIDS EDLPLNVSRE LLQENRILAN IKQNSVKKIL
GAIKKLDSEK MEIFTEQYNR VIKEGIYTDH TNKETLLGIV RYKSSSEEGM VSLDDYISRG
DSEKKEIYYI VGADEKVLRN SPLLEAYKKA NIEVLIMDDE EVDSIVAPMI GSYKEWTFKD
ITTIDAPDSK TEEEKEEISK EFKPLTDKIK EVLGDEVKEV KISTRLTESP SCVLKDASDP
MAGMAAMFAQ MGQEMPEIPL ILEINPEHEM IKKLDKVEDE SLFNDLSWIL LDSAKLSEGL
EPKDKGAFAH RVASLATKAL