ID A9BG49_PETMO Unreviewed; 623 AA.
AC A9BG49;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 103.
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 OrderedLocusNames=Pmob_1086 {ECO:0000313|EMBL:ABX31805.1};
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC Petrotoga.
OX NCBI_TaxID=403833 {ECO:0000313|EMBL:ABX31805.1, ECO:0000313|Proteomes:UP000000789};
RN [1] {ECO:0000313|EMBL:ABX31805.1, ECO:0000313|Proteomes:UP000000789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95 {ECO:0000313|Proteomes:UP000000789};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-2007) 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; CP000879; ABX31805.1; -; Genomic_DNA.
DR RefSeq; WP_012208906.1; NC_010003.1.
DR AlphaFoldDB; A9BG49; -.
DR STRING; 403833.Pmob_1086; -.
DR KEGG; pmo:Pmob_1086; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_0; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000000789; 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 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};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:ABX31805.1}.
FT DOMAIN 25..182
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..339
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 548..623
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 489..517
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 623 AA; 72862 MW; 98C59C90DBD55172 CRC64;
MPEVKEFQAE TKQLLNLIIN SIYTHKDIFL RELISNASDA LDKIRFLSLK DPSILQNDTE
LQIRIDIDKD NNTLIVEDNG IGMSYEEVIE NLGTIAKSGT KNFLNQLKQA QSENTVISLI
GQFGVGFYSA FMVAKKVIVE TKKWDQDKGV RWESDGTGTY SVEECEKANR GTKITLILKD
DLDEDENYLD QYKIQELVKK HSNYIKYPIK MKWEEEVEAG KQKITVKILN SMVPLWNKNK
EEITQNEYNE FYKEHFYDWN DPFDVIHFKA EGTTVEFTAL LYIPSKLPFT FFSKDYKRGL
NLYSKNVFIM ENCEEVLPDY LGFVKGLVDS PDFSLNISRE ILQKNKQLKV IRKNIERKIL
DALKSKLENE REKYVEFWKE FGKVIKAGLY QNIQEKEKVQ DLLLFESSTS DKNMVTLKEY
ISKMKEDQGN YIYYAVGESK DIIENLPQME SFKEKGYEVL YLTDEIDEFL IKLMHDYEGK
EFKSISSSNV KIDEKFKEKE EENKDLLQKI KEYLKDKVKD VRLTDKLKES PACIVSANEA
ISLNMEKTLK NLEQLPFEAE KILELNPDHQ VFKILTDIYH KDPNSEEIKD YAELLYNQSL
LLEGLEIEDK ATFAKLITKL MIK
//
