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Database: UniProt
Entry: D7GU26_9FIRM
LinkDB: D7GU26_9FIRM
Original site: D7GU26_9FIRM 
ID   D7GU26_9FIRM            Unreviewed;       668 AA.
AC   D7GU26;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=Molecular chaperone, HSP90 family {ECO:0000313|EMBL:CBL41318.1};
GN   ORFNames=CK3_16490 {ECO:0000313|EMBL:CBL41318.1};
OS   butyrate-producing bacterium SS3/4.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL41318.1, ECO:0000313|Proteomes:UP000008961};
RN   [1] {ECO:0000313|EMBL:CBL41318.1, ECO:0000313|Proteomes:UP000008961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41318.1,
RC   ECO:0000313|Proteomes:UP000008961};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Clostridiales sp. SS3/4.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL41318.1, ECO:0000313|Proteomes:UP000008961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS3/4 {ECO:0000313|EMBL:CBL41318.1,
RC   ECO:0000313|Proteomes:UP000008961};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; FP929062; CBL41318.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7GU26; -.
DR   KEGG; bprs:CK3_16490; -.
DR   PATRIC; fig|245014.3.peg.62; -.
DR   HOGENOM; CLU_006684_3_2_9; -.
DR   BioCyc; BBAC245014:G1314-1405-MONOMER; -.
DR   Proteomes; UP000008961; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
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   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   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};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
SQ   SEQUENCE   668 AA;  77093 MW;  00FFD9C43044AF87 CRC64;
     MAKSGSLSIN SENIFPIIKK WLYSDHDIFY RELVSNGCDA ITKLKKLALM GEYETPDDET
     YKVQVTVNPK EKTIRIEDNG LGMTEDEVDE YINQIAFSGA QDFLNKYKDK ANEDQIIGHF
     GLGFYSAFMV ADKVTIDTLS YKQDAKPVHW ESEGGTEFDM KEGTKEGHGT VITLYLNEDS
     AEFANEYRAR EILDKYCAFM PVEIYLNDET AEPQYDTIEK DELTDKDTVI ETIVEPAKTE
     EKEKEDGTKE TVEVSPAKEK YKIARRPVAV NDTNPLWNKH PNECTDEEYK EFYRKVFQDF
     KEPLFWIHLN MDYPFNLKGI LYFPKINMEY ESIEGKIKLY NNQVFIADNI KEVIPEFLML
     LKGVIDCPDL PLNVSRSALQ NDGFVKKISD YITKKVADKL SGMCKTDREN YEKYWDDINP
     FIKFGCLKDE KFDEKMKDYI LYKNLDGKYL TLADCLEENK EKHENKIFYV TDEKEQSQYI
     NMFKEAGIDA VILPNPIDSP FMQHVEQKNE GLKFLRIDAD VNETFKDSEE TDEAAKEQEK
     KDAETLAEVF KKAIGNDKLN VKVEKLKNEG LASMITVSEE SRRMQDMMKM YSMYGGGADM
     FPAEETLVLN ANNGLVKYVL NNKDGEKTPM LCEQLYDLAK LAHGSLSPER MTKFIARSSE
     IMKEEYGA
//
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