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Database: UniProt
Entry: A0A089LTQ1_9BACL
LinkDB: A0A089LTQ1_9BACL
Original site: A0A089LTQ1_9BACL 
ID   A0A089LTQ1_9BACL        Unreviewed;       626 AA.
AC   A0A089LTQ1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=PSTEL_05375 {ECO:0000313|EMBL:AIQ62618.1};
OS   Paenibacillus stellifer.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ62618.1, ECO:0000313|Proteomes:UP000029507};
RN   [1] {ECO:0000313|EMBL:AIQ62618.1, ECO:0000313|Proteomes:UP000029507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ62618.1,
RC   ECO:0000313|Proteomes:UP000029507};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-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; CP009286; AIQ62618.1; -; Genomic_DNA.
DR   RefSeq; WP_038693930.1; NZ_CP009286.1.
DR   AlphaFoldDB; A0A089LTQ1; -.
DR   STRING; 169760.PSTEL_05375; -.
DR   KEGG; pste:PSTEL_05375; -.
DR   HOGENOM; CLU_006684_3_0_9; -.
DR   OrthoDB; 9802640at2; -.
DR   Proteomes; UP000029507; 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:UP000029507};
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;  71364 MW;  19CC240EF86C2FC8 CRC64;
     MAKKQFQAES KRLLEMMINS IYTQREIFLR ELISNSSDAI DKIYYKALTD DSLTFNKEDY
     FIRITADKEN RTLTLTDTGI GMTQEELENN LGVIAKSGSL AFKKENEAKD GHNIIGQFGV
     GFYSAFMVAD TVTVISRALG SDTAFKWESE GADGYSIEAA EKDAIGTDII LKIKANTEDD
     SYDEFLEEYR LRTIVKKYSD FIRYPIKMDV TRSKPKEGAE NEYEEVKEEQ TVNSMVPIWR
     KNKSELTDED YENFYQEKRY GFDKPLKHIH ISADGAVVYN AILFIPENTP FDYYTKEYEK
     GLELYSNGVL IMNKCGDLLP DYFSFVKGMV DSEDLSLNIS RELLQHDRQL SLIAKNIKNK
     IKGALQTLLK DEREKYETFY QAFGRGLKFG VYNNYGADKD TLQDLLLFHS SKEKKLVSLD
     EYVSGMPEDQ KYIYYASGES IERIEKLPQT ELVADKGYEI LYFTDDIDEF AIKMLMSYKD
     KEFRSVSGGD LGIDLDEETK EAENADNENK GLFESMKDIL GGKVKSVKAS KRLKSHPVCL
     SAEGDLSIEM EKTLRAMPNG GDVQADKVLE INVNHDVFHS LKNAAETDKE KLALYTNLLF
     NQALLIEGLP VGDPVEFTND ICKIMV
//
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