(data stored in ACNUC7421 zone)

SWISSPROT: B1VRU1_STRGG

ID   B1VRU1_STRGG            Unreviewed;       638 AA.
AC   B1VRU1;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   07-JUN-2017, entry version 64.
DE   RecName: Full=Chaperone protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE   AltName: Full=Heat shock protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE   AltName: Full=High temperature protein G {ECO:0000256|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000256|HAMAP-Rule:MF_00505};
GN   OrderedLocusNames=SGR_680 {ECO:0000313|EMBL:BAG17509.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17509.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17509.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00505}.
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DR   EMBL; AP009493; BAG17509.1; -; Genomic_DNA.
DR   RefSeq; WP_012377982.1; NC_010572.1.
DR   ProteinModelPortal; B1VRU1; -.
DR   STRING; 455632.SGR_680; -.
DR   EnsemblBacteria; BAG17509; BAG17509; SGR_680.
DR   GeneID; 6209684; -.
DR   KEGG; sgr:SGR_680; -.
DR   PATRIC; fig|455632.4.peg.663; -.
DR   eggNOG; ENOG4105CJX; Bacteria.
DR   eggNOG; COG0326; LUCA.
DR   HOGENOM; HOG000031989; -.
DR   KO; K04079; -.
DR   OMA; SDHEIFL; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006950; P:response to stress; IEA:InterPro.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
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; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1VRU1.
DR   SWISS-2DPAGE; B1VRU1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00505};
KW   Chaperone {ECO:0000256|HAMAP-Rule:MF_00505};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00505};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001685};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW   ECO:0000313|EMBL:BAG17509.1}.
FT   DOMAIN       28    185       HATPase_c. {ECO:0000259|SMART:SM00387}.
FT   REGION        1    343       A; substrate-binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00505}.
FT   REGION      561    638       C. {ECO:0000256|HAMAP-Rule:MF_00505}.
SQ   SEQUENCE   638 AA;  71218 MW;  CC4D933E94AFFF96 CRC64;
     MSGSVETLEF QAETRQLLRL VIHSIYSNKD IFLRELISNA SDALDKLRLE SLTDSSLETE
     SADPHIALEV DPEARTLTVR DNGIGMTRED LVELIGTIAK SGTAGLLEKI KESKDAATAE
     NLIGQFGVGF YSAFMVADQV TLLTRRAGTD TGTRWESDGE GTYAIQSEDG LPVGTSVTLH
     LKPVDSEDGR ADYLSESKIR QIVKQYSDFI RWPIRMATER TAADGATTRE TDTLNSMKAL
     WARPRTEVSE EEYHEFYQQI SHDWLPPAET IHMRAEGTFE YEALLFIPSQ APFDLFSRET
     KPGVQLYVKR VFIMDDCEAL MPNYLRFVKG VVDAHDLSLN VSREILQHDR QIHGVRRRLV
     KKVLGALKDM QSKDAERYAK VWEQFGRALK EGLVEDTDNT ETLLQLVSAA STHDPDRTTT
     LREYVERMKD GQDTIYYLTG ESRAMVENSP HMEAVAAKGY EVLILTDPVD EVWVDRVPAF
     DGHTLQSIAK GQVDLGESTD GEKEDDAAKA QREKDFAALL PWLTTALSEQ VKEVRLSSRL
     TTSAACIVGD AHDVTPTLEK MYRAMGQEIP TVKRILELNP SHPLVTALRT AHDADVDDPA
     LKEVAELVYG SALLAEGGDL PDPARFTRLL ADRLARTL
//

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