ID A0A0R2HPI6_9FIRM Unreviewed; 633 AA.
AC A0A0R2HPI6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=IV49_GL000794 {ECO:0000313|EMBL:KRN51325.1};
OS Kandleria vitulina DSM 20405.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Kandleria.
OX NCBI_TaxID=1410657 {ECO:0000313|EMBL:KRN51325.1, ECO:0000313|Proteomes:UP000051841};
RN [1] {ECO:0000313|EMBL:KRN51325.1, ECO:0000313|Proteomes:UP000051841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20405 {ECO:0000313|EMBL:KRN51325.1,
RC ECO:0000313|Proteomes:UP000051841};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRN51325.1}.
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DR EMBL; JQBL01000002; KRN51325.1; -; Genomic_DNA.
DR RefSeq; WP_029070288.1; NZ_JQBL01000002.1.
DR AlphaFoldDB; A0A0R2HPI6; -.
DR PATRIC; fig|1410657.5.peg.828; -.
DR Proteomes; UP000051841; Unassembled WGS sequence.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000051841};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:KRN51325.1}.
FT DOMAIN 25..179
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..342
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 554..633
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 493..520
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 633 AA; 73677 MW; AD3A81009948DAB3 CRC64;
MSEKKQFKTE SKRLLDLMIN SIYTHKEIFL RELVSNASDA SDKLYYKALQ ENINGISRED
MDIFLSIDKE KRTITIEDHG IGMDHDELEE RLGTIANSGS NEFKNALEKG VDNVDIIGQF
GVGFYSAFMV ADKVEVFSKK YGEDKAYAWV SDTSDGYEIF ESGLDHHGTK IVLHLKDNTE
EENYDEYLSQ YEIERLIKKY SDYIHYPIKM EMTVSKKKED SDEYEDVTEV KVLNSQVPLW
KRNKKDITEE EYNDFYKSKF NDFTDPQRVM HNRVEGNITY DSLLFIPSQV PMNYFSSEYE
KGLQLYSRGV FIMDKAKDLV PEHFRFVRGL VDSQDLNLNI SREMLQHDRS MKLIADRIEK
RIQRELEDML KKDREEYVKF WKNFGMQIKF GIYHSYGMLK DKLQDLLLFY SANKKDYITL
NEYVEAMKED QKDIYFASGE TVEKIDMLPA CEAVKDKGFD ILYLTDNVDE FCLQMLRDYK
EKTFKNVTQG DLNLESEEEK KELEQKTTDH KDLLDAIKEA LGDKVVEVRL SSRLKSHPVC
LTSSEGVSFE MEKVLNAMPE AQGQNVKAGR ILEINPNHDL FNALVNVNEK NADKVKDYAS
LLFDEAMLIE GFTIEDPVGF SNKITSLMIE ASK
//
