ID A0A0U1KNH2_9BACI Unreviewed; 626 AA.
AC A0A0U1KNH2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:CQR47561.1};
GN ORFNames=BN1058_01886 {ECO:0000313|EMBL:CQR47561.1};
OS Paraliobacillus sp. PM-2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Paraliobacillus.
OX NCBI_TaxID=1462524 {ECO:0000313|EMBL:CQR47561.1, ECO:0000313|Proteomes:UP000199066};
RN [1] {ECO:0000313|EMBL:CQR47561.1, ECO:0000313|Proteomes:UP000199066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM-2 {ECO:0000313|EMBL:CQR47561.1,
RC ECO:0000313|Proteomes:UP000199066};
RA Murphy D.;
RL Submitted (MAR-2015) 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; CTEI01000002; CQR47561.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1KNH2; -.
DR STRING; 1462524.BN1058_01886; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000199066; 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 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:UP000199066};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 24..177
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..340
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 551..626
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 72082 MW; 74557DA2A65AC150 CRC64;
MPTKQFEAES KRLLEMMINS IYSQREVFLR ELISNASDAI DKLYYKALTD DSLTFNPEDY
YIKVSTDKNS RSLTITDTGI GMTEEELIDN IGVIARSGSL SFKKENEIKD GHDIIGQFGV
GFYAAFMVAD AVTVKTKALN SDQGYIWKSE GADGYSIEPY DKADTGTEIT LTIKESTDED
DYDQFLDVDQ LKSIIVKYSD FIRYPIKMDI VTKEPQGEGE EPVEVTEEKT VNSMVPIWKK
NKNELTEEDY NQFYTEKHYG FDQPLQHIHL SVDGTIRYDA ILYIPESMPY NYYSAEYEKG
LELYSNGVLI MNKCADLLPD YFSFVKGLVD SEDLSLNISR EMLQHDRQLK LIAKNINKKI
KTELQKLLKN DREKYETFYD SFGRQLKYGV YSDFGQNKET LQDLLLFYSS KEKKLVSLAE
YVERMPEDQP FIYYATGETN ERIESLPQTE MVLDKGYEIL YLTDDIDEFA IKMLATYQEK
TFKSVSSGDL GFEPEEEDST EEEIKENKAL LDHMKSVLAN EVKDVRISKR LKSHPVCLSN
DGEISIEMEK VLNMMPDNPQ LKADKILEIN THHDVFKTLQ TAYAKDDIQK TDLLTNILYH
QALLIEGLSI DDPVTFTNNI WKAIAN
//
