ID K6G778_9GAMM Unreviewed; 608 AA.
AC K6G778;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=B273_0369 {ECO:0000313|EMBL:EKO36984.1};
OS SAR86 cluster bacterium SAR86E.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX NCBI_TaxID=1208365 {ECO:0000313|EMBL:EKO36984.1, ECO:0000313|Proteomes:UP000010310};
RN [1] {ECO:0000313|EMBL:EKO36984.1, ECO:0000313|Proteomes:UP000010310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAR86E {ECO:0000313|EMBL:EKO36984.1};
RA Dupont C.L., Rusch D.B., Lombardo M.-J., Novotny M., Yee-Greenbaum J.,
RA Laskin R.;
RL Submitted (SEP-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}.
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:EKO36984.1}.
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DR EMBL; AMWX01000001; EKO36984.1; -; Genomic_DNA.
DR AlphaFoldDB; K6G778; -.
DR STRING; 1208365.B273_0369; -.
DR PATRIC; fig|1208365.4.peg.366; -.
DR Proteomes; UP000010310; 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 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:UP000010310};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 27..184
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..329
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 539..608
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 608 AA; 69412 MW; 2D7FBFDB32A24861 CRC64;
MARSKTKSFQ TETKQLLQLM IHSLYSNKEI FLRELVSNSS DALDKLRFNA IEDNKLLEGD
AELKININLN SQNNTVTISD NGIGMTEEEI IENIGTIAKS GTAQFLSEMT GDKKKDSNLI
GQFGVGFYSV FMVAEKVSVH SRSALAKAED AVMWESSGED TYQLSNIPKE DRGTKITIHL
NEDNKEFSEL MRVKFLLQKY SQYINFPLIL NPEEGESETI NDSEAIWLKS KRSVKDDEYK
EFYKFISYDS NDPLKWIHNK VEGKQEYSSL LFIPEKSPYD LWNRDTPRGI KLFIQRVFIM
DDAAHFLPLY LRFIKGVVDS SDLPLNVSRE ILQDHPLVDS IKKGLTKRVL DTLKKMQKDQ
PEDYQTFWKE FGLVIKEGPA EDYENAESIA ELFLFASTAN DGSNVETTLD QYIERMNADD
EKIYYSIADT YEAAANSPHI EHLKANDTEV LILTDRIDEW LMTTLMQYKG KSLINIAKEE
LDESAKKPRV TKEKQEVIDK MKKSLDSRVS DVIPSSRLVD SAACLVLSKD EPGAQLKRIL
EASGQTFEES KPVFEVNLKH KLIKKLSSMS GKEFTNFSQF LFDYAVIAEG GSPKDPAKYL
RQLDKYLG
//
