ID A0A094IWV5_9GAMM Unreviewed; 630 AA.
AC A0A094IWV5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=IDSA_02580 {ECO:0000313|EMBL:KFZ31607.1};
OS Pseudidiomarina salinarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=435908 {ECO:0000313|EMBL:KFZ31607.1, ECO:0000313|Proteomes:UP000054363};
RN [1] {ECO:0000313|EMBL:KFZ31607.1, ECO:0000313|Proteomes:UP000054363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISL-52 {ECO:0000313|EMBL:KFZ31607.1,
RC ECO:0000313|Proteomes:UP000054363};
RA Du J., Shao Z.;
RT "The draft genome sequence of Idiomarina salinarum ISL-52.";
RL Submitted (JUN-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:KFZ31607.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPER01000001; KFZ31607.1; -; Genomic_DNA.
DR RefSeq; WP_034773957.1; NZ_PIQD01000001.1.
DR AlphaFoldDB; A0A094IWV5; -.
DR STRING; 435908.IDSA_02580; -.
DR eggNOG; COG0326; Bacteria.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000054363; 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:UP000054363};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:KFZ31607.1}.
FT DOMAIN 30..187
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..337
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 555..630
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 630 AA; 71537 MW; 57B752E6789E0D5D CRC64;
MAEARQSETH GFQTEVKQLL HLMIHSLYSN KEIFLRELVS NASDAADKLR FQALSDGSLL
ADDAELYVRV SADKEAGTIT ISDNGIGMTR DEVMSNLGTI AKSGTADFFS KLSGDQARDS
RLIGQFGVGF YSAFIVAESV TVRTRAAGAA ADEAIEWSSR GEGEFDLRQI DKAKRGTDVI
LQVRDDAEEY LDEWRLKSIV TKYSDHLNIP VQMPKRDDDG KADGWEAVNS GQALWTREKS
EISDEEYKEF YKTIAHDFED PLLWSHNKVE GTSEYTSLLY IPKRAPWDLW NREQQNGIKL
YVKRVFIMDD ATQLMPTYLR FVRGLMDSSD LPLNVSREIL QDNKITRSMR NGSTKKVLSM
LSKLAKDEPE TYQQFWNTFG TVLKEGPAED QANQEKIASL LRFASTHMDT SEASTSLDEY
LERMPEQQQS IYYIVADSYE AARDNPALEI FRKKGIEVLL LSERIDEWLM SHLSTYKEKA
FQSVTRGDLD LGELEDEDSK QQQEAAEKAF EDSAKRFEKA LGDKVKSVRV THRLTSSPAC
IVTDENDMST QMAKLMEAAG QKVPETKYIF EVNPEHTLVQ RVVALDDEQR FSEWAQLLLD
QATLAERGNL KDPAQFVTRL NRLMLELTDA
//
