ID A0A1M6DKM9_9CLOT Unreviewed; 625 AA.
AC A0A1M6DKM9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:SHI73816.1};
GN ORFNames=SAMN02745176_01160 {ECO:0000313|EMBL:SHI73816.1};
OS Lutispora thermophila DSM 19022.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Lutispora.
OX NCBI_TaxID=1122184 {ECO:0000313|EMBL:SHI73816.1, ECO:0000313|Proteomes:UP000184442};
RN [1] {ECO:0000313|EMBL:SHI73816.1, ECO:0000313|Proteomes:UP000184442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19022 {ECO:0000313|EMBL:SHI73816.1,
RC ECO:0000313|Proteomes:UP000184442};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQZS01000007; SHI73816.1; -; Genomic_DNA.
DR RefSeq; WP_073025291.1; NZ_FQZS01000007.1.
DR AlphaFoldDB; A0A1M6DKM9; -.
DR STRING; 1122184.SAMN02745176_01160; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000184442; Unassembled WGS sequence.
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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000184442}.
FT COILED 503..537
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 625 AA; 72639 MW; D7F3C348B275DBAD CRC64;
MNRESGSISI QTENIFPIIK KWLYSDKDIF VRELISNGVD AINKLKRLAS IGEAEISSEE
KFEVKVSFNK DEKTIKFIDN GIGMTAEEVK KYINQVAFSG AKEFIEKYKD KMGEEAEIIG
HFGLGFYSAF MVSKKVEVDT LSYQSGAEAV KWISEGGTEY ELTSSERASR GTTVTLYIDE
ESEEFLDEYK LRGIIQKHCA FLPVKIYLED EKFKKEGEDR KPLNDINPLW LKNPKDCTEE
EYKAFYRKVF NDFNDPLFWI HLSVDYPFNL KGILYFPKLR HEYEISEGQI KLYNNQVFVA
DNIKEIIPEF LMLLKGTIDC ADLPLNVSRS FLQKDSNVIK LSKHITKKVA DKLTELFEKE
REKYEGFWKD ISPFIKYGSI KDRNFYDKIK DVLIFKSING NYLTLNEYFE KTGGKKEGDK
EENKIFYASD EKKQHQYIKL FKDQGLEAVV LDSVIDNHFI SYLEMYELNV KFYRIDSDLA
DSLKDIETEG KEDKAKEEKL VEEVKKALNI EKLEVKLERL KNDETQAVLL MAEHERRLQE
MSAMFGAEEM NKMFKGEETL ILNKSNNLVK ALGSLMDKEE KKEDFQMICS HIYDLALMGS
RGLDGDKLEA FLKRSGMILE RLANI
//
