ID F3KFX1_9GAMM Unreviewed; 643 AA.
AC F3KFX1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=imdm_1978 {ECO:0000313|EMBL:EGG98731.1};
OS gamma proteobacterium IMCC2047.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=434085 {ECO:0000313|EMBL:EGG98731.1, ECO:0000313|Proteomes:UP000004485};
RN [1] {ECO:0000313|EMBL:EGG98731.1, ECO:0000313|Proteomes:UP000004485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=imcc2047 {ECO:0000313|Proteomes:UP000004485};
RX PubMed=21602327; DOI=10.1128/JB.05226-11;
RA Kang I., Kang D., Oh H.M., Kim H., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT "Genome sequence of strain IMCC2047, a novel marine member of the
RT Gammaproteobacteria.";
RL J. Bacteriol. 193:3688-3689(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:EGG98731.1}.
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DR EMBL; AEGL01000504; EGG98731.1; -; Genomic_DNA.
DR AlphaFoldDB; F3KFX1; -.
DR PATRIC; fig|434085.3.peg.1685; -.
DR Proteomes; UP000004485; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000004485};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 30..187
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 215..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..643
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 514..545
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 643 AA; 73364 MW; 4E90B8DE0E0D6129 CRC64;
MSVEAQKETM GFQTEVKQLL HLMIHSLYSN KEIFLRELIS NASDAADKLR YEALENNALY
EDDPNLKIRI DFDKEANTIS ISDNGIGMSR DEVIANLGTI AKSGTGEFLK NLTGDQKKDS
QLIGQFGVGF YSAFIVADEV TVETRRAGAS ASEGVRWQSA AEGDFTIETI DKADRGTRLT
LHLKKDEAEF ADDFRLRNLV RKYSDHISLP VEMLEQETPA MPTEEGEEPK EEAPKERQYE
AVNEAKALWT CSRSELNDDE YKEFYKHVSH DFEDPLTWSH NKVEGKLEYT SLLYVPKRAP
FDMWNRDATH GLKLYIQRVF IMDDAEQFLP MYLRFIKGVV DSNDLSLNIS REILQKDPQI
DKMRGALTKR VLDMLAKMAK KEPEQYAEFW KEFGSVLKEG PAEDFANKET VAKLLRFSTT
HDDVEEQAIS LEDYVGRMQE GQDKIYYVVA DSFNTAKSSP HIEVFRKKGI EVLLLSDRID
DWLVSHLNEF DGKQFQDVAK GELDLGGVED EEEKKKQEET AEQFKDLVER VKSNLEERVE
EVRVTHRLTD SPACLVVGQY DMGAQMRRIM EAAGQPMPES KPTLELNPEH PLVEKLNAEA
NDERFADLAA IIFDQAHLAE GGQLDDPASY VQRLNKLLLE LSQ
//
