ID A0A0A0EZE3_9GAMM Unreviewed; 634 AA.
AC A0A0A0EZE3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=N800_13875 {ECO:0000313|EMBL:KGM55413.1};
OS Lysobacter daejeonensis GH1-9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1385517 {ECO:0000313|EMBL:KGM55413.1, ECO:0000313|Proteomes:UP000029998};
RN [1] {ECO:0000313|EMBL:KGM55413.1, ECO:0000313|Proteomes:UP000029998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GH1-9 {ECO:0000313|EMBL:KGM55413.1,
RC ECO:0000313|Proteomes:UP000029998};
RA Zhang S., Wang G.;
RT "Genome sequencing of Lysobacter.";
RL Submitted (AUG-2013) 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:KGM55413.1}.
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DR EMBL; AVPU01000005; KGM55413.1; -; Genomic_DNA.
DR RefSeq; WP_036135261.1; NZ_AVPU01000005.1.
DR AlphaFoldDB; A0A0A0EZE3; -.
DR STRING; 1385517.N800_13875; -.
DR eggNOG; COG0326; Bacteria.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000029998; 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:UP000029998};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:KGM55413.1}.
FT DOMAIN 28..183
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..345
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 563..634
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 634 AA; 71331 MW; 3A99528AC4C18F0F CRC64;
MTTQTETHRF QAEVQQVLHL VTHSLYSNKD VFLRELVSNA ADACDKLRFE ALQDATLYGD
QPELAIDITW DKDARTLTLR DSGIGMSRDE LIGNLGTIAR SGTRKFIEAL SAQQKADAQL
IGQFGVGFYS AFVVADKVVV ESRRAGTDEA WRWTSSGEGE FALEPADTVA RGTTVTLHLK
DGEDEYLDGW RLRELVRRYS DHIGFPIRMP KEKWGNDEHA SDEAKAEDVS ELEAVNQASA
LWTRPKAELS DADYQAFYKH ISHDFNEALA WTHNRVEGNQ NFTSLVYLPS KAPFDFQYNR
DERRGLKLYV KRVFIMDAAE QMLPAYLRFV HGVLDSDDLP LNVSRELLQG NRQLDKLKSA
LVKRTLDLLD RVARDEADKY EGFWREFGNV LKEGLAEDHG NRERIAKLLR FASTRSEKAD
DLTSLDAYVE RMQAGQKAIY FLTADGWNAA RNSPQLEALR ARGIEVLLLH ERIDDWAIGH
LHEYASKPLR HVGKGDLDLG DLDSPQDKEK READAKAAAP LVEAVKGLLG DRVKDVRVST
RLTDSPACLV LEEYDVSLHL QQLLRAAGQP VPVSKPVLEI NPGHPLLKRL EGQQDGMGRE
DLALLLLEQA QLAEGNALDD PAAFIQRVNR LLVT
//
