ID A0A1M5VLY0_9FIRM Unreviewed; 637 AA.
AC A0A1M5VLY0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN02745823_00900 {ECO:0000313|EMBL:SHH76249.1};
OS Sporobacter termitidis DSM 10068.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Sporobacter.
OX NCBI_TaxID=1123282 {ECO:0000313|EMBL:SHH76249.1, ECO:0000313|Proteomes:UP000183995};
RN [1] {ECO:0000313|EMBL:SHH76249.1, ECO:0000313|Proteomes:UP000183995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10068 {ECO:0000313|EMBL:SHH76249.1,
RC ECO:0000313|Proteomes:UP000183995};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQXV01000002; SHH76249.1; -; Genomic_DNA.
DR RefSeq; WP_073076460.1; NZ_FQXV01000002.1.
DR AlphaFoldDB; A0A1M5VLY0; -.
DR STRING; 1123282.SAMN02745823_00900; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000183995; 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 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:UP000183995};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 24..178
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..350
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 562..637
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 637 AA; 72663 MW; C446B3CB70BE2047 CRC64;
MAKKQFKSES KRLLDLMVNS IYTHKEIFLR EIISNASDAI DKLCYISLTD DKVGLNRDDF
KITVTADKEN RTITVSDNGI GMTAEELEQN LGVIAKSGSL QFKKDIGDKK EDVDIIGQFG
VGFYSAFMVA SKVTVVTRAY GQEEANMWVS TGSDGYTITP CEKDSAGTEI IIALKEDEEG
ESYGEFLEEH ELHRIIKKYS DYIRWPIVMD VTKSRQVETD ETDKDGSKKK TWEDYTEKEV
VNSRVPIWQR SRSEVSDEEC MQFYKEKFFD MEDPVSVIRI SAEGAVTYKA MLFIPAKAPY
DYYTREYKSG LQLYTSGVMI METCADLLPE HFRFVRGIVD SQDLSLNISR EMLQHDRQLK
VIETNLEKKI KAELKRLLEN DYDKYAAFYK SFGLQLKYGI VNGYGANRDL LSDLIMFYSS
KAEKLITLAD YVKNMPEDQK YIYYACGESV QKLDKLPQAE NVREKGYEIL YLTDDVDEFV
VKTLIRFEEK EFRSVNDDDL GLETEEEKKE TEKLETENKD VLDFIKESLG GKIAAAKLSH
KLKSHPVCLT AQGGISLEME RYFAATQGDM AEHMKAERVL ELNAGHPVFQ ALKSTFPTDK
EKAAKYAELL YGQAQLIAGV SLDDPAHFAE LVSSLMI
//
