ID G0JSB3_9PROT Unreviewed; 629 AA.
AC G0JSB3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 70.
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=Acife_1572 {ECO:0000313|EMBL:AEM47710.1};
OS Acidithiobacillus ferrivorans SS3.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=743299 {ECO:0000313|EMBL:AEM47710.1, ECO:0000313|Proteomes:UP000009220};
RN [1] {ECO:0000313|EMBL:AEM47710.1, ECO:0000313|Proteomes:UP000009220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3 {ECO:0000313|EMBL:AEM47710.1,
RC ECO:0000313|Proteomes:UP000009220};
RX PubMed=21705598; DOI=10.1128/JB.05373-11;
RA Liljeqvist M., Valdes J., Holmes D.S., Dopson M.;
RT "Draft genome of the psychrotolerant acidophile Acidithiobacillus
RT ferrivorans SS3.";
RL J. Bacteriol. 193:4304-4305(2011).
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; CP002985; AEM47710.1; -; Genomic_DNA.
DR RefSeq; WP_014028966.1; NC_015942.1.
DR AlphaFoldDB; G0JSB3; -.
DR STRING; 743299.Acife_1572; -.
DR KEGG; afi:Acife_1572; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_6; -.
DR Proteomes; UP000009220; 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}; Reference proteome {ECO:0000313|Proteomes:UP000009220};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 28..185
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..337
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 555..629
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 629 AA; 71003 MW; 3605D89F579A9B42 CRC64;
MTASKETMQF QTEINQLLQL MIHSLYSNKE IFLRELISNA SDACDKLRFE ALADPALLTG
DSELKVEVDF DSEAGTITVR DNGIGMNRDE VIANIGTIAK SGTREFFDRL SGDQTKDAKL
IGQFGVGFYS AFIVADRVIL NTRRAGMEAE HGIRWESDGT GTYTLETLNL PAHGTEIVLH
LRAEERQDLL SAWRLRSIIN KYSDHIPLSI RMRKMGEDGK SGDEWETVNK ASALWQRSKS
EISDDEYKEF YRYVSHDYGD PLTWSHNHVE GRLEYTSLLF IPAKAPFDLW DHNHSHGIKL
YVQRVFIMDD AEQLLPRYLR FVRGVIDSSD LPLNVSREIL QGNRVIDQMR SGSVKRILSL
LEEMAEKEPE KYQTFWNEFG RALKEGPGED YSNREQIAKL LRFASSHTDT DTQNVSLADY
LARMAEGQDK IYYITADSFL AAKNSPQLEL LRKKGIEVLL LSDRVDEWLT SHLPEFAGKA
LASVAKGTLD LGTIETEEER KSQEETEKGA EGLVERIKNA LGERVEAVRV SHRLTSSPAC
IVLGERDMAL YMQQLLKQAG HEVSSTKPVL EINPTHPMLV RIEGEKDDTR FAEWSALLLD
QAILAEGGQL EDPAGFVARI NQLMLALAG
//
