ID B5Z9X9_HELPG Unreviewed; 621 AA.
AC B5Z9X9;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
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 OrderedLocusNames=HPG27_192 {ECO:0000313|EMBL:ACI26959.1};
OS Helicobacter pylori (strain G27).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041 {ECO:0000313|EMBL:ACI26959.1, ECO:0000313|Proteomes:UP000001735};
RN [1] {ECO:0000313|EMBL:ACI26959.1, ECO:0000313|Proteomes:UP000001735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27 {ECO:0000313|EMBL:ACI26959.1,
RC ECO:0000313|Proteomes:UP000001735};
RX PubMed=18952803; DOI=10.1128/JB.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(2009).
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; CP001173; ACI26959.1; -; Genomic_DNA.
DR RefSeq; WP_000070574.1; NC_011333.1.
DR AlphaFoldDB; B5Z9X9; -.
DR KEGG; hpg:HPG27_192; -.
DR HOGENOM; CLU_006684_3_0_7; -.
DR Proteomes; UP000001735; 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}; Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
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; 71366 MW; 955C09B4AAB313F6 CRC64;
MSNQEYTFQT EINQLLDLMI HSLYSNKEIF LRELISNASD ALDKLNYLML TDEKLKGLNT
TPSIHLSFDS QKKTLTIKDN GIGMDKSDLI EHLGTIAKSG TKSFLSALSG DKKKDSALIG
QFGVGFYSAF MVASKIVVQT KKVTSEQAYA WVSDGKGKFE ISECIKEEQG TEITLFLKEE
DSHFASRWEI DNVVKKYSEH IPFPIFLTYT DTKYEGEGDN QKEIKEEKCE QINQASALWK
MNKSELKDKD YKEFYQSFAH DNSEPLSYIH NKVEGSLEYT TLFYIPSKAP FDMFRVDYKS
GVKLYVKRVF ITDDDKELLP SYLRFVKGVI DSEDLPLNVS REILQQNKIL ANIRSASVKK
ILSEIERLSK DNKNYHKFYE PFGKVLKEGL YGDFENKEKL LELLRFYSKD KEKLISLKEY
KENLKENQKS IYYLLGENLD LLKASPILEK YAQKGYDVLL LSDEIDAFVM PGVNEYDKTP
FRDASHSESL KELGLEEIHD EVKDQFKDLM KAFEENLKDE IKGVELSNHL TSAVALIGDE
PNAMMANWMR QMGQSVPESK KTLELNPNHA ILQKLLKCED KEQLSAFIWL LYDGAKLLEK
GALKDAKSFN ERLNSVLLKA L
//
