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Database: UniProt
Entry: N9WJK5_9CLOT
LinkDB: N9WJK5_9CLOT
Original site: N9WJK5_9CLOT 
ID   N9WJK5_9CLOT            Unreviewed;       623 AA.
AC   N9WJK5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
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   ORFNames=HMPREF1092_00261 {ECO:0000313|EMBL:ENZ03075.1};
OS   Clostridium thermobutyricum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=29372 {ECO:0000313|EMBL:ENZ03075.1, ECO:0000313|Proteomes:UP000013097};
RN   [1] {ECO:0000313|EMBL:ENZ03075.1, ECO:0000313|Proteomes:UP000013097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=209318 {ECO:0000313|EMBL:ENZ03075.1,
RC   ECO:0000313|Proteomes:UP000013097};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Courvalin P., Lambert T.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium colicanis 209318.";
RL   Submitted (JAN-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ENZ03075.1}.
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DR   EMBL; AGYT01000007; ENZ03075.1; -; Genomic_DNA.
DR   RefSeq; WP_002596765.1; NZ_KB850956.1.
DR   AlphaFoldDB; N9WJK5; -.
DR   PATRIC; fig|999411.4.peg.244; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_1_3_9; -.
DR   Proteomes; UP000013097; Unassembled WGS sequence.
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; 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_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; 2.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
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.
DR   PROSITE; PS00298; HSP90; 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:UP000013097};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT   REGION          1..341
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT   REGION          550..623
FT                   /note="C"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   623 AA;  72475 MW;  8F8CC2339A880F51 CRC64;
     MEKKQFKAES KRLLDIVINS IYTNREIFLR ELISNASDAI DKIYYKTLSD SSLIFNKGDY
     FIKLIPNMEE RTLTIRDTGI GMTEAELEEN LGVIAKSGSL QFKNENELKD GYDIIGQFGV
     GFYSAFLVAD HVKVITKAFG GDKAFVWESD GVDGYTISEG EKDSFGTDIV LHLKENTEDE
     NFDEYLNEYK LRSLIKKYSD FIRYPIKLDA KKSRLKEGSE DEYEEYIEEE IINSMVPLWR
     KNKKELTDED YNNFYFEKRF GFDKPLKHIH ISVDGMISYN SIMFIPENTP YDYYTKEYKK
     GLELYSNGVL IMEKCEELLP DYFGFVKGIV DSQDLSLNIS RELLQHDRQL KRIAKNIKNK
     IKNELESMIK NDREAYEKFY KSFGRQLKYG VYDDFGANKD DLKDLIMFYS SKEKKMVTLN
     EYIERMPEDQ KYIYYASGES NDRIEKMPQT EMVLDKGYEI LYFTEDIDEF AIKMLQSYKE
     KEFKSVSAGD LGIENKEEET KANEENKDLF TGIKEALSGK VKEVKASSRL KKYPVCLSAE
     GELSIEMEKI LNSMPNNEGV KSEKVLEINT GHEVFNSLKN AYSSDKDKFN LYVNLLYNQA
     LLMEGLSIED PTEFANDICK LMK
//
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