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HTPG_BRADU
ID   HTPG_BRADU              Reviewed;         625 AA.
AC   Q89CK8;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=bll7789;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC53054.1; -; Genomic_DNA.
DR   RefSeq; NP_774429.1; NC_004463.1.
DR   RefSeq; WP_011090513.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89CK8; -.
DR   SMR; Q89CK8; -.
DR   STRING; 224911.27356073; -.
DR   EnsemblBacteria; BAC53054; BAC53054; BAC53054.
DR   GeneID; 64027535; -.
DR   KEGG; bja:bll7789; -.
DR   PATRIC; fig|224911.44.peg.7932; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   InParanoid; Q89CK8; -.
DR   OMA; MRRMKEM; -.
DR   PhylomeDB; Q89CK8; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IBA:GO_Central.
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; Reference proteome;
KW   Stress response.
FT   CHAIN           1..625
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062974"
FT   REGION          1..334
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          335..549
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          550..625
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   625 AA;  68932 MW;  B11F58943F923D1C CRC64;
     MTTSDSAVHT QPFQAEVSEL LHLMVHSVYS ETDIFLRELV SNASDACDKL RYEAIESPAL
     LGEGDALKIR IIPNKTAGTL TIADNGIGME RQELIDHLGT IARSGTKAFV SKLKEAKDGL
     GLIGQFGVGF YSAFMVADKI IVVSRRAGES DVWSWTSSGG SGFEIARASE EDAARVTRGT
     EIVLHLKDDA KKYLETYEIE RIVGAYSDNI LFPIELVPEE GEPRQINSAS ALWQRSKSEL
     SAEDYKKAYQ QIASAFDDPA MTLHYRAEGR YSYAVLLFAP STKPFDLFEP SRKGRVRLYV
     RRVFITDDAD LLPGYLRFIR GVVDSEDLPL NISREMLQNN PQLVQIRKAV ATRVVSELEG
     LAEKDAENFA KIWDAFGAVL KEGIYEDFER REKLLALSRF TTTTGEKRSL KQVVADFKPN
     QTEIYYLVGD SIERLKSNPR LEAATARGIE VLLLSDPVDA FWTSMPTEFE GKPLKSLSQG
     DLNLDLIPRV DATDEAKKDE PEADEAATIA VIKAALGERV SDVKASTRLT SSASCLVADS
     QGPSRELERI LSQQNRGMRA KPVLEINLRH PMVGAITKAQ AGSKAVDDLS LLLLEQAQIL
     DGELPEDPAA FAARLNRLVL QGLGG
 
 
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