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HTPG_CLOAB
ID   HTPG_CLOAB              Reviewed;         624 AA.
AC   Q97E05;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 114.
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=CA_C3315;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK81247.1; -; Genomic_DNA.
DR   PIR; D97307; D97307.
DR   RefSeq; NP_349907.1; NC_003030.1.
DR   RefSeq; WP_010966587.1; NC_003030.1.
DR   AlphaFoldDB; Q97E05; -.
DR   SMR; Q97E05; -.
DR   STRING; 272562.CA_C3315; -.
DR   PRIDE; Q97E05; -.
DR   EnsemblBacteria; AAK81247; AAK81247; CA_C3315.
DR   GeneID; 44999809; -.
DR   KEGG; cac:CA_C3315; -.
DR   PATRIC; fig|272562.8.peg.3494; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_9; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000000814; 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; IPR019805; Heat_shock_protein_90_CS.
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; 2.
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.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Stress response.
FT   CHAIN           1..624
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000062981"
FT   REGION          1..341
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          342..550
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          551..624
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   624 AA;  72407 MW;  131C769B501EB26C CRC64;
     MAVKQFKAES KRLLDLMINS IYTNKEIFLR ELISNASDAI DKCYYRSLVD TNITFNKDDF
     YIRISADKEN KTLTITDTGI GMTKDDLENN LGTIAKSGSF AFKSENEAKE GVDIIGQFGV
     GFYSAFMVAD DVTVISRSVD SEEAYKWESK GVEGYTIEKC EKETPGTEIV LKIKENTDDE
     KYDEFLDEYK LRSLIKKYSD FIKYPIKMMT KKTRPKKDND KETEEYLEDE TLNSMVPIWR
     KNKNELKQED YDNFYMDKHF GFEKPLKTIH SNVEGVVSYN TLLFIPASAP YDFYTKEFEK
     GLELYSNGVM IMQKCGDLLP DYFSFVQGLV DSPDLSLNIS RELLQHDRQL KFIAKKIKEK
     IKSELLSMAK NDRENYVKFF NSFGRQLKYG VYSDFGSNKE VLQDLLMFYS STEKKLVTLD
     EYVSRMKEDQ KYIYYAAGES NEKIEKLPQT EVVKDKGYEI LYFTDDVDEF AIKMLMKYKE
     KEFKSVSNKD LGFEADEKES KKETEENKDL FDFMKEVLDG KVKEVRASSR LKSHPVCLSN
     DGELSIEMEK VLKMMPDNNN VKAEKILEIN TNHEMFNSIK AAFKDDKDKL KKYASLLYNE
     ALLIEGLPIE DPVQFANDVA SLMK
 
 
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