ID A0A0A1ML51_9BACI Unreviewed; 625 AA.
AC A0A0A1ML51;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:CEI80589.1};
GN ORFNames=BN997_00394 {ECO:0000313|EMBL:CEI80589.1};
OS Oceanobacillus oncorhynchi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI80589.1, ECO:0000313|Proteomes:UP000040453};
RN [1] {ECO:0000313|EMBL:CEI80589.1, ECO:0000313|Proteomes:UP000040453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI80589.1,
RC ECO:0000313|Proteomes:UP000040453};
RA Urmite Genomes Urmite Genomes;
RL Submitted (NOV-2014) 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; CDGG01000001; CEI80589.1; -; Genomic_DNA.
DR RefSeq; WP_042529156.1; NZ_CDGG01000001.1.
DR AlphaFoldDB; A0A0A1ML51; -.
DR STRING; 545501.BN997_00394; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000040453; 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:UP000040453};
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; 72301 MW; 4EBC52C23FE5E172 CRC64;
MAKHEFKAES QKLLDMVIHS IYSQREIFLR ELISNASDAI DKIYYKALTD DALTFDQSNY
YIKLIPNKEK RTLTVVDTGI GMTKEELEDN LGVIAKSGSH TFKSENEIKD GHDIIGQFGV
GFYAAFMVAD KVTVLTKSID SEEGYQWVSQ GSDGYTITPI DREEVGTEII LEIKENEEED
NYDTFLEEAT LKQIVKKYSD FIRYPIKMDV TESKLKEGTE DEYEDVIEEQ TLNTMVPIWK
KNKSELTDED YTNFYQEKRY GFDQPLRHIH INVDGAVRYN AILFIPEQTP FNYYSREYEK
GLELYSNGVL IMEKCADLLP DYFSFVKGMV DSEDLSLNIS REMLQHDRQL KIIAKNIHKK
IKQQLLSLLR DEREKYETFF KALGQQIKFG VYSDFGQHKE ELQDLLLFYS STEKKLVTLE
EYVSRMPEDQ KYIYYASGDS NERIEKLPQT EIVADKGYEI LYFTDEVDEF AIKMLMQYQD
KEFRSVSSGD LGIEADEKEE EKEETESHNE LFTAMKEVLG DKVKDVRASK RLKSHPVVLS
ADGDISLEME KIINAMPDNQ QIQADKVLEI NVDHSIFKAL EAAQGNDQDK LALYTNLLYN
QALLIEGLPI EDPVAFTNDM SKIMV
//
