ID A0A1M6I2F6_9CLOT Unreviewed; 626 AA.
AC A0A1M6I2F6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN05444401_2606 {ECO:0000313|EMBL:SHJ28615.1};
OS Clostridium amylolyticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121298 {ECO:0000313|EMBL:SHJ28615.1, ECO:0000313|Proteomes:UP000184080};
RN [1] {ECO:0000313|EMBL:SHJ28615.1, ECO:0000313|Proteomes:UP000184080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21864 {ECO:0000313|EMBL:SHJ28615.1,
RC ECO:0000313|Proteomes:UP000184080};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQZO01000004; SHJ28615.1; -; Genomic_DNA.
DR RefSeq; WP_073007290.1; NZ_FQZO01000004.1.
DR AlphaFoldDB; A0A1M6I2F6; -.
DR STRING; 1121298.SAMN05444401_2606; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000184080; 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:UP000184080};
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 553..626
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 73306 MW; 2487397D6BB17092 CRC64;
METKEFKAES KRLLDLMINS IYTHREIFLR ELISNASDAI DKIYYKALTD ENLTFDKDSY
YIKIVSDKEN KVLKVIDTGI GMTKEELENN LGVIAKSGSL AFKKENDAKD GYDIIGQFGV
GFYAAFMVAD RVTVISKALG SNEAYKWESK GAEGYTIEPW EKDSVGTEII LEIKENTQDE
KYEEYLEEYK LREIIKKYSD FIRYPIKMNI TNSKLKEGTE DEYESYIEEQ TINSMVPIWR
KNKSELTAED YEKFYSEKHY GYDKPVKHIH IIADGAVRYN SILFIPENIP FDYYTREYEK
GLELYSNGVL IMNKCSDLLP DYFSFVKGMV DSEDLSLNIS REMLQHDRQL KLIAKNIKNK
IKSELLNLLK NERDKYEGFY KSFGRQLKYG VYNDFGTDKE MLQDLLMFYS SKEKKLVTLD
EYISRMPEDQ KYIYYAVGES NERIEKLPQT ELVSEKGYEI LYFTEDIDEF TIKMLMNYKE
KEFRSVSSND LGIEDTKEND KEEAQEKDNK EIFEYMKKVL ADKVKDVRAS KRLKHHPVCF
SNDGEISIEM EKILNAMPNS QNIKADKILE ININHEVFNS LKNAYENDKE KLDLYTNLLY
SQALLIEGLP VSDPVEFTND ICKIMK
//
