ID A0A1Q5M462_9ACTN Unreviewed; 632 AA.
AC A0A1Q5M462;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=AMK33_19035 {ECO:0000313|EMBL:OKK08979.1};
OS Streptomyces sp. CB02400.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703944 {ECO:0000313|EMBL:OKK08979.1, ECO:0000313|Proteomes:UP000185993};
RN [1] {ECO:0000313|EMBL:OKK08979.1, ECO:0000313|Proteomes:UP000185993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02400 {ECO:0000313|EMBL:OKK08979.1,
RC ECO:0000313|Proteomes:UP000185993};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKK08979.1}.
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DR EMBL; LIWB01000007; OKK08979.1; -; Genomic_DNA.
DR RefSeq; WP_073934103.1; NZ_LIWB01000007.1.
DR AlphaFoldDB; A0A1Q5M462; -.
DR Proteomes; UP000185993; 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:UP000185993};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 26..183
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..339
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 555..632
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 632 AA; 71615 MW; F90EC9E74B750E76 CRC64;
MPTETFEFQV EARQLLQLMI HSVYSNKDVF LRELVSNASD ALDKLRLAKL RDDSLDADLS
DLHIELEIDK DARTLTVRDN GVGMSYDEVG QLIGTIANSG TAQLLRELRE AQDGTGTEGL
IGQFGVGFYS GFMVADEVTL LTRRAGEGQG TRWTSRGEGT YTLERVDDAP QGTSVTLHLK
PADPDNQLHD YTSVWKIKEI VKRYSDFITW PIRLVGETGG DGEAAGPETL NSMKALWARS
REEVSEEEYH ELYKHIGHDW REPLQTIQLQ AEGTFEYQAL LFVPSHAPHD LFTQNFRHGL
QLYVKRVFIM DDCEALLPPY LRFVKGVVDA QDLSLNVSRE ILQQDRHIRM MQRRLTKKVL
ASVKSMMTGD AERYATFWRE FGAVLKEGLV TDPDNRDALL AVTSFATTRG DDGTATLKQY
VERMPDGQDD IWFITGESRE SIDNSPHMEA FRERGIEVLL LTDPVDEMWV DAVGEYEGKR
LRSIAKGEVD LGAREDDRSE DERQQQAEEY AGLLDWMRER LDEDVKEVRL STRLTVSPAC
LVADANDLTP ALENMYRAMG QEVPRTKRIL ELNPDHALVK GLNEAYGERE DRSDLTDTAE
LLHSLAVLAE GGRPKDPARF VRLMADRLER TL
//
