ID A0A345PLH9_9BACI Unreviewed; 625 AA.
AC A0A345PLH9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=CUC15_18850 {ECO:0000313|EMBL:AXI10859.1};
OS Oceanobacillus zhaokaii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=2052660 {ECO:0000313|EMBL:AXI10859.1, ECO:0000313|Proteomes:UP000253908};
RN [1] {ECO:0000313|Proteomes:UP000253908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=160 {ECO:0000313|Proteomes:UP000253908};
RA Zhu W.;
RL Submitted (NOV-2017) 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; CP024848; AXI10859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345PLH9; -.
DR KEGG; ocn:CUC15_18850; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000253908; Chromosome.
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:UP000253908};
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 552..625
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 625 AA; 72270 MW; BBCDF48544562CAE CRC64;
MAKKEFQAES KKLLDMMINS IYTQREVFLR ELISNASDAI DKIYYRALTD DNLSFNKENY
YIKVVPNKDE RTLKIIDTGI GMTKEDLESN LGVIAKSGSH TFKSENEVKD GHDIIGQFGV
GFYAAFMVSD VVTVVSKSID SDEAYKWEST GSDGYTIEPA EKSEVGTEIT LKIKESTEDD
NYDEFLEEYR LKQIIKKYSD FIRYPIKMDV TESKLKEGSE DEYEEVVEEQ TVNTMVPIWK
KNKSELTDED YENFYNEKHY GFDKPLKHIH LSVDGTVRYN AILFIPESAP YNYYSREYEK
GLELYSSGVL IMEKSPELLP DYFSFVKGMV DSEDLSLNIS REMLQHDRQL QIIAKNISKK
IKSQLLSLLR DDRESYEKFY QSFGQQLKFG LYSDYGQHKE VLQDLILFYS STEKKMVTLE
EYVSRMPEEQ KYIYYATGDS NERIDKLPQT EVVADKGYEI LYFTEEIDEF AIKMLMSYKE
KEFKSVSSGD LGIEDEDKDE KEEAATENKD LFAEMKTILA DKVKDVRASK RLKSHPVVIT
ADGEISIEME KVINAMPDDQ NIKADKVLEI NINHEVFGAL KDAFANDQDK LKLYTNLLYN
QALLIEGLPI NDPVEFTNDI CKVMV
//
