ID E2Z9W9_9FIRM Unreviewed; 631 AA.
AC E2Z9W9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=HMPREF9429_00225 {ECO:0000313|EMBL:EFQ04944.1};
OS Megasphaera micronuciformis F0359.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=706434 {ECO:0000313|EMBL:EFQ04944.1, ECO:0000313|Proteomes:UP000003195};
RN [1] {ECO:0000313|EMBL:EFQ04944.1, ECO:0000313|Proteomes:UP000003195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0359 {ECO:0000313|EMBL:EFQ04944.1,
RC ECO:0000313|Proteomes:UP000003195};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFQ04944.1}.
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DR EMBL; AECS01000007; EFQ04944.1; -; Genomic_DNA.
DR AlphaFoldDB; E2Z9W9; -.
DR STRING; 706434.HMPREF9429_00225; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_9; -.
DR Proteomes; UP000003195; 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; IPR003594; HATPase_C.
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; 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.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000003195};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 8..168
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 556..631
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 497..524
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 631 AA; 71885 MW; 54A15620EEB0D48B CRC64;
MIHSIYTNRE IFLRELISNG SDAIDKLHYE ALTNRDLLEG DTEFSIRLAI DKDKKTLTVA
DNGIGMDKED IKANIGTIAR SGTKAFLERL KAEKEDSENV SDKELIGQFG VGFYSAFMVA
KAVTVLTRKA GTDTGYCWKS TGDGSYTLTE CDVKHHGTAV VLELKDEFTT GEDDFLDESR
LSELVKKYSD YIRYPIMMNV TVKEVPKNED GQPVEGADPI EKTELKTLNS MQPLWTRNKS
DIKDEEYADF FRHQFYEWEK PMEVFHTKAE GTVEYTALLF IPGSAPMNLY YSDYEPGIQL
YSRHVFIMDK CKDLLPEYLR FVKGLVDSPD LSLNISREML QQSRNLKVIG KNLEKTILKT
LARKAEKERP EYEKFWNEFG KSIKIGIYSG MMTGENNADK LKDLVLFYSA RQGRLVTLKE
YVEAMKDGQQ KIYYAVGKDK EGIDALPQTE LLKDRDLDVL YLFDPVDEFA IEALHEYDGK
SFHSVSRGDL DLDDDTFKEE KKKNEDLAKD NEGLLQDMKK ALESKVVDVR LSNRLKSGAV
CLVADAAGPS VAMEQAFAGA DNPFMKARRI LEINPHHELF NKLKTLHDGE TNEDAFKEYS
ELLYDQALLL EGIMPEDPVV FAQRLAKMMA K
//
