ID J5UFS4_9FIRM Unreviewed; 627 AA.
AC J5UFS4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
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 ECO:0000313|EMBL:EJU22179.1};
GN ORFNames=HMPREF1143_0761 {ECO:0000313|EMBL:EJU22179.1};
OS Peptoanaerobacter stomatis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoanaerobacter.
OX NCBI_TaxID=796937 {ECO:0000313|EMBL:EJU22179.1, ECO:0000313|Proteomes:UP000005244};
RN [1] {ECO:0000313|EMBL:EJU22179.1, ECO:0000313|Proteomes:UP000005244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OBRC8 {ECO:0000313|EMBL:EJU22179.1,
RC ECO:0000313|Proteomes:UP000005244};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) 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:EJU22179.1}.
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DR EMBL; ALNK01000023; EJU22179.1; -; Genomic_DNA.
DR RefSeq; WP_009531149.1; NZ_ALNK01000023.1.
DR AlphaFoldDB; J5UFS4; -.
DR PATRIC; fig|796941.3.peg.1301; -.
DR Proteomes; UP000005244; 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:UP000005244};
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..627
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 627 AA; 73347 MW; 7BB879CE4BEA1D8C CRC64;
MAKQEFKAES KRLLDLMINS IYTNRDIFLR ELISNASDAI DKVYYKTLAD ENKNFNKEDY
YIQISVDKAN RTITVEDTGI GMNKSDMEDN LGIIAKSGSL QFKKDNEIKD GFDIIGQFGV
GFYSAFMVAK KVKVLSKSID DDKAYLWESE GIDGYEISES EKSSNGTIIT IYLKDNTDEE
KYDEYLEEYK LRSLVKKYSD FIRYPIKMEV TKSRPKEDDK DNYEDYIEIE TLNSMVPIWR
KNKNELTEED YINFYNEKHY GFDKPLKYIH TSADGVIRYT SIMYIPSMLP FNYYSKEFKK
GLELYSNGVL IMDKCSELLP DYFGFVVGMV DSEDLSLNIS RETLQHDRQL KLIAKRLNEK
IKNELTNMLK NKREDYDKFY DTFSRSLKFG IYDNWGMNKD ELQDLIMFKS SLDKEKYTTL
EEYVSRMKDD QKEIYYATGE SVEKIEKMPQ TEFLLDKGYE ILYFTDEVDE FAIQVLRTYK
EKEFKSVSSS DINVDNTEKE KNEEKAKESK SMLDEMKEIL KSNISDVVIS NRLKSYPVCI
SAKGSVSVEM EKTLNAMPTD THVKAEKVLE INPENKSFDN LKKYYEQDKD KFTKLTEVLY
NQALLIEGLQ VQDPIKFANN ISDLLFG
//