ID F3KTJ9_9BURK Unreviewed; 647 AA.
AC F3KTJ9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=HGR_08899 {ECO:0000313|EMBL:EGI76878.1};
OS Hylemonella gracilis ATCC 19624.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hylemonella.
OX NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI76878.1, ECO:0000313|Proteomes:UP000016368};
RN [1] {ECO:0000313|EMBL:EGI76878.1, ECO:0000313|Proteomes:UP000016368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI76878.1,
RC ECO:0000313|Proteomes:UP000016368};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGI76878.1}.
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DR EMBL; AEGR01000056; EGI76878.1; -; Genomic_DNA.
DR RefSeq; WP_006297835.1; NZ_AEGR01000056.1.
DR AlphaFoldDB; F3KTJ9; -.
DR STRING; 887062.HGR_08899; -.
DR eggNOG; COG0326; Bacteria.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000016368; 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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
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.
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:UP000016368};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00505}.
FT DOMAIN 25..186
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..351
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 580..647
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 647 AA; 72055 MW; 49876D38F1ECB0C5 CRC64;
MSQKHSFQAE VAQLLHLVTH SLYSNKEIFV RELVSNASDA CDKLRYEALN NSALYEDAPE
LRVRIALDKK ARTLTITDNG IGMSAQEAID HLGTIAKSGT KDFMSKLGAD KQADAKEQGQ
LIGQFGVGFY SGFIVADKIT VESRRAGLKP EEGVRWTSGG TGDFEVETIT RPERGTSVIL
HLREDESNSA DEYLSAWKIK QIIGKYSDHI ALPIQMRKEE WKESEEEGKP GEMVTTDEWE
TVNKASALWT RAKKDITKEE YESFYQGISH DYEAPLAWSH NRVEGSTEYT QLLYVPAKAP
YDLWNRDKKG GLKLYVKRVF IMDEAEALLP SYLRFVKGVV DSADLPLNVS RELLQESRDV
RAIRDGNTKR VLTLLENLAK HDVPATDASE EDKAEAGKYS KFYAEFGTVL KEGLGEDFAN
RERLAKLLRY ASTTSDTATV SLADYKARMK EGQEAIYYIT ADTLAAAKNS PQLEVFKKKG
IEVLLMTERV DEWALSYLTE FDGTPLQSVA KGAVDLGKLQ DEAEKKAAEE AAEAFKPVLA
KLKEALKDKT EDVRVTTRLV DSPACLVVKD GEVSNQLARL LKQAGQKAPD SKPILEVNPE
HALVKKLDGS VHFHDLAHIL YDQALLAEGG LPEDPAAYVK RVNALLV
//
