ID M5DRG0_9GAMM Unreviewed; 634 AA.
AC M5DRG0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, 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=TOL_2091 {ECO:0000313|EMBL:CCU72500.1};
OS Thalassolituus oleivorans MIL-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Thalassolituus.
OX NCBI_TaxID=1298593 {ECO:0000313|EMBL:CCU72500.1, ECO:0000313|Proteomes:UP000011866};
RN [1] {ECO:0000313|EMBL:CCU72500.1, ECO:0000313|Proteomes:UP000011866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIL-1 {ECO:0000313|EMBL:CCU72500.1,
RC ECO:0000313|Proteomes:UP000011866};
RX PubMed=23599290; DOI=10.1128/genomeA.00141-13;
RA Golyshin P.N., Werner J., Chernikova T.N., Tran H., Ferrer M.,
RA Yakimov M.M., Teeling H., Golyshina O.V.;
RT "Genome Sequence of Thalassolituus oleivorans MIL-1 (DSM 14913T).";
RL Genome Announc. 1:1-3(2013).
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; HF680312; CCU72500.1; -; Genomic_DNA.
DR RefSeq; WP_015487220.1; NC_020888.1.
DR AlphaFoldDB; M5DRG0; -.
DR STRING; 187493.CN03_07775; -.
DR KEGG; tol:TOL_2091; -.
DR PATRIC; fig|1298593.3.peg.1995; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR Proteomes; UP000011866; 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 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:UP000011866};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:CCU72500.1}.
FT DOMAIN 29..186
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..342
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 560..634
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 634 AA; 71688 MW; 7E7EE65D1BD3063A CRC64;
MNAASKETLG FKTEVKQLLH LMIHSLYSNK EIFLRELVSN ASDACDKLRF EALQNDALLE
GGADLKIDIH FDKDARTVTI EDNGIGMTRD DVINHLGTIA KSGTAEFLGK LSGDQKKDSQ
LIGQFGVGFY SAFIVADNVV VETRRAGEDA ANAVRWESAG EGEFSLENIE KAERGTRIVL
HLKEGEEEFA DSFRLQSLIK KYSDHIAIPV FVQADAEEAA GEEGEEAKAP EAVNQAKAMW
TRSKSDLTDE DYTEFYKHIS HDWNAPLTWM HNRVEGKLDY TSLLYIPAKA PFDIWNRDAS
RGLKLYVQRV FIMDDAEQFL PLYLRFVKGV LDSNDLSLNV SREILQQDKQ VDSMRSALVK
RVLDTLEKTA KNEPEKYQSF WDQFGEVLKE GPAEDFANRE KIAGLFRFAT TLSEGETENV
GLADYVARMR EGQKKIYFIT GDNHAAVSTS PHLEYFKRKN IEVLLLTDRV DEWMVSHLAD
FDGKVFQDVT KGELDLDELA DDTEKDQQKA LEDSHKDLVE RIEKALEGEV KSVRVTSRLT
DSPACMVVGQ YDMGGHLRRM MEAAGQKMPE PEIALEVNPS HPLIERLDQE QDEERFVDLA
RLIHAQAQLA EGSQLKQPAL YVARLNKLLL DLMK
//
