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Database: UniProt
Entry: G8NTW8_GRAMM
LinkDB: G8NTW8_GRAMM
Original site: G8NTW8_GRAMM 
ID   G8NTW8_GRAMM            Unreviewed;       621 AA.
AC   G8NTW8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
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=AciX8_3223 {ECO:0000313|EMBL:AEU37524.1};
OS   Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU37524.1, ECO:0000313|Proteomes:UP000007113};
RN   [1] {ECO:0000313|EMBL:AEU37524.1, ECO:0000313|Proteomes:UP000007113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC   {ECO:0000313|Proteomes:UP000007113};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA   Haggblom M., Woyke T.;
RT   "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000256|HAMAP-
CC       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|ARBA:ARBA00008239, ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00505}.
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DR   EMBL; CP003130; AEU37524.1; -; Genomic_DNA.
DR   RefSeq; WP_014266399.1; NC_016631.1.
DR   AlphaFoldDB; G8NTW8; -.
DR   STRING; 682795.AciX8_3223; -.
DR   KEGG; gma:AciX8_3223; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_0; -.
DR   OMA; MRRMKEM; -.
DR   OrthoDB; 9802640at2; -.
DR   Proteomes; UP000007113; 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:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00505};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00505};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00505}; Reference proteome {ECO:0000313|Proteomes:UP000007113};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW   ECO:0000313|EMBL:AEU37524.1}.
FT   DOMAIN          24..179
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          1..337
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT   REGION          547..621
FT                   /note="C"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   621 AA;  70394 MW;  23B80615F1FBED5C CRC64;
     MSKREFQTEV SQLLQLIIHS LYSHPEIFLR ELISNSSDAL DKLRHLTLTD DAFKGLAFDP
     RIDLELDEAN KTLTIADTGI GMNEEDLVAH LGTIARSGTK NFLSQLSGDA KRDSNLIGQF
     GVGFYSAFMV ADRVEVVSRK AGEELAWRWT SDGKTGFDIE PAERLVAGTT VTLHFNEEGE
     QYANSWRLQE VVKKYSNHIA FPIFLTYDKS EWNDAEKKSE KTHTTEQVNA ASALWRRPKN
     ELTETDYKEL YKSISGDWED PLFWFHTKAE GSLDYTTLFY IPAKAPLDLY QAEYKTGVKL
     YVKRVFIMDD AKELLPSYLR FVRGIIDSED LPLNVSREIL QQNRVLTSIR TASVKKILSE
     LKNIAANQPE QYLKFIAEYN RPLKEGLYSD FANRETLLDL IRFKSTKVEG LTSLADVKSR
     MKEGQKSLYY ITGGAESLLR TSPLLEIYKK KDLEVLILDD DIDEIVFSGV EKYGDIDLKA
     VNKASTSEDL QDEAEPDKAE TLKPLLDKLK ATLGDRVKEV RASVRLADSP SCIVSDEAEP
     SMKMQQMLRA MGQKDIPALK PTLEINPDHE IVKKLLARPD DVTTEDAAWL LFDQALLMEG
     VPLPDPALFV QRLNRILNLS I
//
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