ID A0A1M7RLU4_9ACTN Unreviewed; 614 AA.
AC A0A1M7RLU4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN05443668_12042 {ECO:0000313|EMBL:SHN47086.1};
OS Cryptosporangium aurantiacum.
OC Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC Cryptosporangiaceae; Cryptosporangium.
OX NCBI_TaxID=134849 {ECO:0000313|EMBL:SHN47086.1, ECO:0000313|Proteomes:UP000184440};
RN [1] {ECO:0000313|EMBL:SHN47086.1, ECO:0000313|Proteomes:UP000184440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46144 {ECO:0000313|EMBL:SHN47086.1,
RC ECO:0000313|Proteomes:UP000184440};
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; FRCS01000020; SHN47086.1; -; Genomic_DNA.
DR RefSeq; WP_073264636.1; NZ_FRCS01000020.1.
DR AlphaFoldDB; A0A1M7RLU4; -.
DR STRING; 134849.SAMN05443668_12042; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000184440; 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:UP000184440};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 28..183
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..330
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 537..614
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 614 AA; 68527 MW; DBDF10D9FB9311B5 CRC64;
MTGRTETLEF QAETRQLLQL MIHSIYSNKD IFLRELISNG SDALDKLRIE SLVNSDLDVD
RSDLHLELVP DGDARTLTVR DNGIGMTHDE VVSLIGTIAK SGTAELVRKL RESSDDTAEL
IGQFGVGFYS SFMVADRVTL VTRKAGEATG TRWESSGEGT YTIEDVDDAP QGTAVTLHLK
PVDTDDQLHD YADPAVLRSI VKKYSDFIAW PIRLGDSDEP INSMKALWAR PRSEVTEDEY
HEFYRHVSHD WTDPLETIHV KAEGTFEYDA LLFLPARAPF DLYSRDAQRG VQLYVKRVFI
MADCEALLPQ YLRFVKGVVD AADLSLNVSR EILQQDRQIQ AVRRRLVKKV LGTVRDLQTE
HPEKYATFWG EFGRALKEGL IEDSANREQI LDLLSFSSTA DPSATTTLRE YVDRRPEGQT
EIYYLTGDSR ATIENSPHLE AFRAKGYEVL VLTDPVDEVW VDQVTEYDGI PLKSVAKGQV
DLADAPPEAE GFEAFLTWMT GALSETVKEV RLSTRLVSSP ACVVGDADDL TPTLEKMYRA
MGQPLPPVKR ILELNPSHPL VTGLRDAYGR AADDPALPET AELIYGMALL AEGGDLADPA
RFARLLAERL AKTL
//
