ID R4QM32_HELPX Unreviewed; 621 AA.
AC R4QM32;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=K751_06400 {ECO:0000313|EMBL:AGL71835.1};
OS Helicobacter pylori UM066.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1321940 {ECO:0000313|EMBL:AGL71835.1, ECO:0000313|Proteomes:UP000013753};
RN [1] {ECO:0000313|EMBL:AGL71835.1, ECO:0000313|Proteomes:UP000013753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UM066 {ECO:0000313|EMBL:AGL71835.1,
RC ECO:0000313|Proteomes:UP000013753};
RA Khosravi Y., Rehvathy V., Amoyo A., Seow S., Ong J., Susana W., Primo B.,
RA Meredith A., Siddarth S., Pettersson S., Loke M., Goh K., Vadivelu J.;
RT "Draft Genome Sequences of Helicobacter pylori Strain UM037 and UM066 using
RT PacBio Sequencing Platform.";
RL Submitted (SEP-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}.
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DR EMBL; CP005493; AGL71835.1; -; Genomic_DNA.
DR RefSeq; WP_015643178.1; NZ_AUSJ01000001.1.
DR AlphaFoldDB; R4QM32; -.
DR KEGG; hpyu:K751_06400; -.
DR PATRIC; fig|1321940.5.peg.1302; -.
DR HOGENOM; CLU_006684_3_0_7; -.
DR Proteomes; UP000013753; 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; 71285 MW; 8E6AC77ED992123E CRC64;
MSNQEYTFQT EINQLLDLMI HSLYSNKEIF LRELISNASD ALDKLNYLML TDEKLKGLNI
TPSIHLSFDS QKKTLTIKDN GIGMDKNDLI EHLGTIAKSG TKSFLSALSG DKKKDSALIG
QFGVGFYSAF MVASKIVVQT KKVNSDQAYA WVSDGKGKFE ISECVKEEQG TEITLFLKDE
DSHFASRWEI DGIVKKYSEH IPFPIFLTYT DTKYEGEGDN QKEIKEEKCD QINQASALWK
TNKSELKDKD 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 EVKEQFKDLM KAFEENLKDE IKGVELSSHL TSAVALIGDE
QNAMMANWMR QMGQSVPESK KTLELNPNHA ILQKLLKCED KEQLSAFIWL LYDGAKLLEK
GALKDAKSFN ERLNSVLLKA L
//
