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HTPG_EXIS2
ID   HTPG_EXIS2              Reviewed;         621 AA.
AC   B1YG43;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, 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}; OrderedLocusNames=Exig_2981;
OS   Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS   255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-2008) 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; CP001022; ACB62427.1; -; Genomic_DNA.
DR   RefSeq; WP_012371842.1; NC_010556.1.
DR   AlphaFoldDB; B1YG43; -.
DR   SMR; B1YG43; -.
DR   STRING; 262543.Exig_2981; -.
DR   EnsemblBacteria; ACB62427; ACB62427; Exig_2981.
DR   KEGG; esi:Exig_2981; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_9; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 246194at2; -.
DR   Proteomes; UP000001681; 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; 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   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..621
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000127028"
FT   REGION          1..340
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          341..547
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          548..621
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   621 AA;  71609 MW;  6CF94EFA96023300 CRC64;
     METKQFKAES KRLLEMMIHS IYTHKEIFLR ELISNASDAM DKIYYKALTD ETITFDKDAY
     KITIEPNKET RQLILRDTGI GMTKDELEEN LGTIAKSGSL AFKAENESKD GHDIIGQFGV
     GFYSAFMVAD TVTVVTKPFG SDVAYKWESH GVDGYTIEEV EKEMVGTDIT LHIKANEEDE
     NYDEYLEPYR LRSIIKKYSD FIRYPIEMEE TEQRPVEGSD ETESVTVMKT VNSMVPIWRK
     NKRELTDEDY RNFYQEKRYG FDAPIKHIHI SADGAVRYQS ILFIPEQPSF DYYSKEFEKG
     LELYANGVLI MEKCSDLLPD HFSFVKGMVD SEDLSLNISR EMLQHDRQLK LIAKNIQSKI
     KTQLEALLRD DREKYETFYQ AFGRQLKFGI YNDYGMQKDT VKDLVLFHSA KEKKLVTLAE
     YVAAMPEEQK YIYYASGEST DRLDKLPQSE LVKDKGFDIL YFTEEIDEFA IQMLLNYDGK
     EFKSVTSSDL GIEQTEQAET TETQAEMFKA MQEVLAGHVK EVKASTRLKS HPVCFATDGA
     VSIEMEKILK AMPNNQDVAA VKILELNTSH DVFRAIETAY AEDRPKFERY TKLMYQQALL
     MEGLPIEDPV AFANEVCALM I
 
 
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