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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
 
 
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