ID X2HTI8_HELPX Unreviewed; 621 AA.
AC X2HTI8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=HPOKI112_01355 {ECO:0000313|EMBL:AHN35745.1};
OS Helicobacter pylori oki112.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1382921 {ECO:0000313|EMBL:AHN35745.1, ECO:0000313|Proteomes:UP000019647};
RN [1] {ECO:0000313|EMBL:AHN35745.1, ECO:0000313|Proteomes:UP000019647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oki112 {ECO:0000313|EMBL:AHN35745.1};
RX PubMed=24744331;
RA Satou K., Shiroma A., Teruya K., Shimoji M., Nakano K., Juan A.,
RA Tamotsu H., Terabayashi Y., Aoyama M., Teruya M., Suzuki R., Matsuda M.,
RA Sekine A., Kinjo N., Kinjo F., Yamaoka Y., Hirano T.;
RT "Complete Genome Sequences of Eight Helicobacter pylori Strains with
RT Different Virulence Factor Genotypes and Methylation Profiles, Isolated
RT from Patients with Diverse Gastrointestinal Diseases on Okinawa Island,
RT Japan, Determined Using PacBio Single-Molecule Real-Time Technology.";
RL Genome Announc. 2:e00286-14(2014).
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; CP006821; AHN35745.1; -; Genomic_DNA.
DR RefSeq; WP_025275600.1; NZ_CP006821.1.
DR AlphaFoldDB; X2HTI8; -.
DR KEGG; hpyc:HPOKI112_01355; -.
DR HOGENOM; CLU_006684_3_0_7; -.
DR Proteomes; UP000019647; 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};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:AHN35745.1}.
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; 71337 MW; 78106A735148C0DD CRC64;
MSNQEYTFQT EINQLLDLMI HSLYSNKEIF LRELISNASD ALDKLNYLML TDEKLKGLNI
TPSIHLSFDS QKKTLTIKDN GIGMDKNDLI EHLGTIAKSG TKSFLSALSG DKKKDSALIG
QFGVGFYSAF MVASKIVVQT KKVTSEQAYA WVSDGKGKFE ISECVKEEQG TEITLFLKDE
DSHFASRWEI DGVVKKYSEH IPFPIFLTYT DTKFEGEGDN KKEIKEEKCE QINQASALWK
MNKSELKDKD YKEFYQSFAH DNSEPLSYIH NKVEGSLEYT TLFYIPSKAP FDLFRVDYKS
GVKLYVKRVF ITDDDKELLP SYLRFVKGVI DSEDLPLNVS REILQQNKIL ANIRSASVKK
ILSEIERLSK DNKNYHKFYE PFGKVLKEGL YGDFENKEKL LELLRFYSKD KEKLISLKEY
KENLKENQKS IYYLLGENLD LLKASPLLEK YAQKGYDVLL LSDEIDAFVM PGVNEYDKTP
FKDASHSESL KELGLEEIRD EVKDQFKDLM KAFEENLKDE IKGVELSNHL TSAVALIGDE
QNVMMANWMR QMGQSVPESK KTLELNPNHA ILQKLLKCED KEQLSAFIWL LYDGAKLLEK
GALKDAKSFN ERLNSVLLKA L
//
