ID F7WZL6_9GAMM Unreviewed; 625 AA.
AC F7WZL6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 08-NOV-2023, entry version 68.
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:AEH39883.1};
GN ORFNames=BCTU_313 {ECO:0000313|EMBL:AEH39883.1};
OS Buchnera aphidicola (Cinara tujafilina).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=261317 {ECO:0000313|EMBL:AEH39883.1, ECO:0000313|Proteomes:UP000006811};
RN [1] {ECO:0000313|EMBL:AEH39883.1, ECO:0000313|Proteomes:UP000006811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cinara tujafilina {ECO:0000313|Proteomes:UP000006811};
RX PubMed=21571878; DOI=10.1128/AEM.00141-11;
RA Lamelas A., Gosalbes M.J., Moya A., Latorre A.;
RT "The genome of Buchnera aphidicola from the aphid Cinara tujafilina
RT provides new clues about the evolutionary history of metabolic losses in
RT bacterial endosymbionts.";
RL Appl. Environ. Microbiol. 77:4446-4454(2011).
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}.
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DR EMBL; CP001817; AEH39883.1; -; Genomic_DNA.
DR AlphaFoldDB; F7WZL6; -.
DR STRING; 261317.BCTU_313; -.
DR KEGG; baj:BCTU_313; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000006811; 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; 1.
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:UP000006811};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:AEH39883.1}.
FT REGION 1..337
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 338..553
FT /note="B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 554..625
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 625 AA; 73150 MW; D4A1F7C67EAB93D9 CRC64;
MNNENKTKHS FQSEVKQLLH LMIHSLYSNK EIFLRELISN ASDAIEKLRF SVISNPKKFI
NHNNTAKIQI SIDKTKKTLS IYDNGIGMTY DEVKNNLGTI AKSGTKSFLK NISNDKKEKN
DFIGQFGVGF YSSFIIAKKV CVFTKHAQNL SDTGTLWESE GQGEYTIEKI KQKEYGTKII
LYIKETEEEF LETWNIKNIV KKYSDHISIP VEIENYDEKT KLFLGRKLIK HKAYGLKIKK
EISAKSYQEF YKYITHDSEE PLLWSHNKVE GNQEYTSLLY IPQKATWDMW HRENKHGLKL
YVKHVYIMDD AIQFLPNYLR FVKGIIDSQD LPLNISREIL QDNKITQNLR KSLTKRVLTI
LNNLSETDDI KYQKFWNIFG LVLKEGLAED SINQKQISNL LRFTSISMQK KEQTLSLKQY
INNMLPEQEK IYFITADSYE SAINSPHLEI FREKNIDVLL LSDRVDEWMM NYLPEYENKK
FQSVSKSDIS LEKLIKNDKL NIDQKDQNID IFIEKNKNIL GNRVKDVRMT NRLINTPVMV
LTDTNDMSTQ MAKLFSAAGQ PIPDVKYLLE INPKHPLIKK IQNIKDIEKI SIWIEMLFEQ
AIFAEKGTLD NPHQFINRIN KLFIS
//
