ID E0TIR3_ZINIC Unreviewed; 607 AA.
AC E0TIR3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 ECO:0000313|EMBL:ADM89690.1};
GN OrderedLocusNames=ZICARI_068 {ECO:0000313|EMBL:ADM89690.1};
OS Zinderia insecticola (strain CARI).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Zinderia.
OX NCBI_TaxID=871271 {ECO:0000313|EMBL:ADM89690.1, ECO:0000313|Proteomes:UP000001303};
RN [1] {ECO:0000313|EMBL:ADM89690.1, ECO:0000313|Proteomes:UP000001303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CARI {ECO:0000313|EMBL:ADM89690.1,
RC ECO:0000313|Proteomes:UP000001303};
RX PubMed=20829280; DOI=10.1093/gbe/evq055;
RA McCutcheon J.P., Moran N.A.;
RT "Functional convergence in reduced genomes of bacterial symbionts spanning
RT 200 My of evolution.";
RL Genome Biol. Evol. 2:708-718(2010).
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; CP002161; ADM89690.1; -; Genomic_DNA.
DR AlphaFoldDB; E0TIR3; -.
DR STRING; 871271.ZICARI_068; -.
DR KEGG; zin:ZICARI_068; -.
DR HOGENOM; CLU_006684_3_0_4; -.
DR Proteomes; UP000001303; 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 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; IPR036890; HATPase_C_sf.
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 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.
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:UP000001303};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:ADM89690.1}.
FT REGION 1..315
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 530..607
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 607 AA; 72387 MW; C28D4047ED794AD7 CRC64;
MKKKIKFKAD IRKVLDIMIK NLYSYKEIFI REIISNSQDA IDKLKYIYNN INFNIKIKIN
KIKKKITIID NGIGMNKNEI INNLGTIAKS GTKNFLSKLT GNKKKDNKLI GKFGVGFYSV
FIVSKLVKVI SKKYNNKNIG YEWISEGKGN FYIKKKKKKN YGTTIKLYLK EKEKKFLSYK
KIIKIIKKYS NYISSPIKIK KKKKWITVNN PNVFWMKNKS SLLKKDYIKF YNNNIDNNEK
PLFYIHKKIE TNKNEYVLLL YVPLKDENII KNNSNIKLYS NKVLIINNIK EIIPNYLRFI
KGIVDCTNLN LNISREKLQD NNIIKIIKNT IINIFLKYLK YISKNKVKIY NLFWKNFGNI
FKEGIYEDFI NNKKILNLIR FKTTYNNNYI SLKEYYSRTK ENNNKIYYII SDNYNNAINS
PHLEYFLKKN IEVIIFTNKI DEWILNFLKK ISKKKFISVT KGILDINILN FNKKYKFKKN
IIKYNKLLNK IKNNLKKKIF EIKLTYRLIY SPSCLIVSNE KEISNNLIKI LKNSKQKILL
KNKNILEINP KHILIKYLLK KKKKIKFWSN FIYDLSLLKE GINIKNISNF SKVLNNIIIK
LIKINKF
//
