ID A0A398BA91_9BACI Unreviewed; 626 AA.
AC A0A398BA91;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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:RID86772.1};
GN ORFNames=D1970_05815 {ECO:0000313|EMBL:RID86772.1};
OS Mesobacillus zeae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1917180 {ECO:0000313|EMBL:RID86772.1, ECO:0000313|Proteomes:UP000265816};
RN [1] {ECO:0000313|EMBL:RID86772.1, ECO:0000313|Proteomes:UP000265816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JJ-247 {ECO:0000313|EMBL:RID86772.1,
RC ECO:0000313|Proteomes:UP000265816};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus jemisoniae sp. nov., Bacillus chryseoplanitiae sp. nov., Bacillus
RT resnikiae sp. nov., and Bacillus frankliniae sp. nov., isolated from Viking
RT spacecraft and associated surfaces.";
RL Submitted (AUG-2018) 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:RID86772.1}.
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DR EMBL; QWVT01000011; RID86772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A398BA91; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000265816; 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:UP000265816};
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; 72023 MW; 76154F9E704A2980 CRC64;
MEKKQFQAES KRLMEMMVNS IYSHKEIFLR ELISNASDAI DKIYYKALAD DSLTFNKDSY
YIKVVPDKEN RTLTLIDTGI GMTKEELESN LGTIARSGSL AFKSENEVKN GHDIIGQFGV
GFYSAFMVAD QVTVISRALG SEEAYRWESE GTDGYTIAPC EKETVGTEII LKIKDNTEEE
QYGDYLEEYR LKSIIKKYSD FIRYPIKMEV TSSRLKDGSD SEFEEFSEEQ TVNSMVPIWR
KNKSELNEED YVNFYNEKRY GFDKPLKHVH ISVDGTIRYN AILFIPENMP FDYYSKEYEK
GLELYSNGVL IMEKCADLLP DHFSFVKGMV DSEDLSLNIS REILQHDRQL KLIAKNISKK
IKSELQSLLK DDREEYETFY NSFGRQLKYG VYSDFGVNKE ALQDLLLFHS SKEKKLVSLD
EYVSRMPEEQ KYIYYASGDS IDRIDKLPQT ELVAEKGFEI LYFTDEIDEF AIKMLMSYKD
KEFKSVASGD LGIEDGDGKE EAESAESEYK DLFASMKEIL ADKVKDVRAS KRLKSHPVCL
STDGEITIEM EKILKAMPNS QDVKAEKVLE INTNHEVFGS LKEAFGGDKE KLSLYTKLLY
SQALLIEGLP IQDPVEFTND MCKIMV
//
