ID T0FAE3_HELPX Unreviewed; 621 AA.
AC T0FAE3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=N206_00695 {ECO:0000313|EMBL:EPZ74859.1};
OS Helicobacter pylori UM111.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1352345 {ECO:0000313|EMBL:EPZ74859.1, ECO:0000313|Proteomes:UP000015461};
RN [1] {ECO:0000313|EMBL:EPZ74859.1, ECO:0000313|Proteomes:UP000015461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UM111 {ECO:0000313|EMBL:EPZ74859.1,
RC ECO:0000313|Proteomes:UP000015461};
RX PubMed=24051312;
RA Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA Loke M.F., Vadivelu J.;
RT "Multiple genome sequences of Helicobacter pylori strains of diverse
RT disease and antibiotic resistance backgrounds from malaysia.";
RL Genome Announc. 1:E00687-E00713(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}.
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:EPZ74859.1}.
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DR EMBL; AUSR01000001; EPZ74859.1; -; Genomic_DNA.
DR RefSeq; WP_021308384.1; NZ_AUSR01000001.1.
DR AlphaFoldDB; T0FAE3; -.
DR PATRIC; fig|1352345.3.peg.136; -.
DR Proteomes; UP000015461; 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};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:EPZ74859.1}.
FT DOMAIN 26..181
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..341
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 548..621
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 621 AA; 71167 MW; 3B2875DF34FF7F76 CRC64;
MSNQEYTFQT EINQLLDLMI HSLYSNKEIF LRELISNASD ALDKLNYLML TDEKLKGLNT
TPSIHLSFDS QKKTLTIKDN GIGMDKNDLI EHLGTIAKSG TKSFLSALSG DKKKDSALIG
QFGVGFYSAF MVASKIVVQT KKVTSNQAYA WVSDGKGKFE ISECVKEEQG TEITLFLKDE
DSHFASRWEI DGVVKKYSEH IPFPIFLTYT DTKYEGEGDN QKEIKEEKCD QINQASALWK
VNKSELKDKD YKEFYQSFAH DNSEPLSYIH NKVEGSLEYT TLFYIPSKAP FDMFRVDYKS
GVKLYVKRVF ITDDDKELLP SYLRFVKGVI DSEDLPLNVS REILQQNKIL ANIRSASVKK
ILSEIERLSK DEKNYHKFYE PFGKVLKEGL YGDFENKEKL LELLRFYSKD KEKLVSLKEY
KENLKENQKS IYYLLGENLD LLKASPLLEK YAQKGYDVLL LSDEIDAFVM PGVNEYDKTP
FRDASHSESL KELGLEEIND EIKERFKDLV KAFEENLKDE VKGVELSSHL TSAVALIGDE
QNAMMANWMR QMGQSVPESK KTLELNPNHA ILQKLLKCGD KEQLSAFIWL LYDGAKLLEK
GALKDAKSFN ERLNSVLLKA L
//
