ID A0A0C1Y8U5_9BURK Unreviewed; 637 AA.
AC A0A0C1Y8U5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=TSA66_24985 {ECO:0000313|EMBL:KIF83353.1};
OS Noviherbaspirillum autotrophicum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=709839 {ECO:0000313|EMBL:KIF83353.1, ECO:0000313|Proteomes:UP000031572};
RN [1] {ECO:0000313|EMBL:KIF83353.1, ECO:0000313|Proteomes:UP000031572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSA66 {ECO:0000313|EMBL:KIF83353.1,
RC ECO:0000313|Proteomes:UP000031572};
RA Ishii S., Ashida N., Ohno H., Otsuka S., Yokota A., Senoo K.;
RT "Denitrispirillum autotrophicum gen. nov., sp. nov., Denitrifying,
RT Facultatively Autotrophic Bacteria Isolated from Rice Paddy Soil.";
RL Submitted (DEC-2014) 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:KIF83353.1}.
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DR EMBL; JWJG01000028; KIF83353.1; -; Genomic_DNA.
DR RefSeq; WP_040041980.1; NZ_JWJG01000028.1.
DR AlphaFoldDB; A0A0C1Y8U5; -.
DR STRING; 709839.TSA66_24985; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000031572; 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:UP000031572};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00505}.
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 564..637
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 637 AA; 72425 MW; 7C6882ABC9F49249 CRC64;
MAASEKQTLG FQAEVKQLLH LMIHSLYSNK EIFLRELISN ASDAADKLRF EAINNAALFE
NDPELKIRVT FDKQARTITI SDNGIGMSRE EAIEHLGTIA KSGTKEFFSK LSGDQQKDAA
LIGQFGVGFY SAFIVADRIT VESRRAGLPA DQGVRWESAG EGDFSVEQIE KGTRGTDIIL
HLREGEDEFL SNWKLKSTIR KYSDHISLPI LMQKEEWDDE KKETVIKDEF ETINQASALW
TRNKSDITPE QYTEFYKHVS HDFEAPLAHT HNRVEGRSEY IQLLYIPARA PFDLWDRNKR
GGIKLYVKRV FIMDDAEQLM PVYLRFVKGV IDSSDLPLNV SREILQESRD IRVIREGSTK
RVLGLLEELA NGEEQEQKDK YATFWTEFGQ VLKEGIGEDQ ANKDRIAKLL RFASTINDSD
AQTVSFDDYI GRMKEGQDKI YYITADSYAA AKNSPHLEIF RKKGVEVLLM TDRVDEWMLS
FLQEVEGKEL VSVAKGDLDL GKLEDESEKK QHEETESQYK DLVEKMKKAL EPKAKEVRVT
FRLTDSPACL VADENELSGN LVRMLKAAGQ NAPESKPILE INPDHPLVQR LKYEEAKFDD
WANILFDQAM LAEGGALADP AGFVKRLNDM LLGMVSK
//
