ID I0I222_CALAS Unreviewed; 629 AA.
AC I0I222;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:BAL99309.1};
GN OrderedLocusNames=CLDAP_12700 {ECO:0000313|EMBL:BAL99309.1};
OS Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS STL-6-O1).
OC Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC Caldilinea.
OX NCBI_TaxID=926550 {ECO:0000313|EMBL:BAL99309.1, ECO:0000313|Proteomes:UP000007880};
RN [1] {ECO:0000313|EMBL:BAL99309.1, ECO:0000313|Proteomes:UP000007880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC {ECO:0000313|Proteomes:UP000007880};
RA Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Hanada S., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT 102666).";
RL Submitted (FEB-2012) 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; AP012337; BAL99309.1; -; Genomic_DNA.
DR RefSeq; WP_014432550.1; NC_017079.1.
DR AlphaFoldDB; I0I222; -.
DR STRING; 926550.CLDAP_12700; -.
DR KEGG; cap:CLDAP_12700; -.
DR PATRIC; fig|926550.5.peg.1345; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_0; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000007880; 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; 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:UP000007880};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 32..188
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..333
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 548..629
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 629 AA; 72544 MW; AD20843A736595D5 CRC64;
MSEVVETQLE SLEYRTEVKQ LLDILAHSLY TDREIFLREL ISNASDALNR IQFEMLTNHD
VVDPEVELAI YIEADSDART ITIRDTGIGM NRDELIENLG TIAHSGARAF LQNASQNQSA
LEEIIGQFGV GFYSVFMVAE EVTVISRSYR PQDRAALWRS TGDSRFSLGE ADKQDRGTEI
RIRLKEDAAE FVQPWRLETI IKRHSDYVSF PIYLKSKDGE ARVVNRRIAL WRQSPSKVEP
KEYEEFYRQL TFDNRPPLLH IHILADSPVN VRGILFVPAQ RERSSLRLRP EYGLRLYSRK
ILIQEHNKEL LPEYLRFVEG VVDSEDLPLN VSRETVQSNP LVRQLRKALT NRLLKELRTL
ADENPEKYNT FWTEFGVFIK EGVASDYANR EALLELLRFH STRTGTEGWT TLKEYIQRMQ
PDQKAIYYIL GDNLKSAMRS PHLDYFRKHD IEVLFLTDFI DGYMVSNLRE VHDKPLQNVD
DPNLDLPETD EATADAAVSA QAFDKLIARI KQVLGERIRD VREGKTLVDS PARLVSPEDD
FARELQYVRR VLEENYVAPA KILEINRRHP MIVNLARLVD EESDNALIDP AIEQLFDNLQ
LLEGVYQGSV ADMVERIHRL MSAALASHS
//
