ID A0A231PQ21_9ACTN Unreviewed; 631 AA.
AC A0A231PQ21;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=CHR28_04165 {ECO:0000313|EMBL:OXS36821.1};
OS Streptomyces sp. XY006.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2021410 {ECO:0000313|EMBL:OXS36821.1, ECO:0000313|Proteomes:UP000215527};
RN [1] {ECO:0000313|EMBL:OXS36821.1, ECO:0000313|Proteomes:UP000215527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XY006 {ECO:0000313|EMBL:OXS36821.1,
RC ECO:0000313|Proteomes:UP000215527};
RA Shan W., Liu H., Zhou Y., Yu X.;
RT "Draft Genome Sequence of Streptomyces sp. XY006, an Endophyte Isolated
RT from Tea (Camellia sinensis).";
RL Submitted (JUL-2017) 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}.
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:OXS36821.1}.
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DR EMBL; NOKT01000002; OXS36821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A231PQ21; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000215527; 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}; 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 554..631
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 631 AA; 71552 MW; 578CF5E56BB27B65 CRC64;
MTTETFEFQV EARQLLQLMI HSVYSNKDVF LRELVSNASD ALDKLRLEKL RDDALDADVS
DLHIEIDVDR QARTLTVRDN GIGMSYEEVG QLIGTIAKSG TATLLKELRE AQDAAGAEGL
IGQFGVGFYS GFMVADEVTL VTRRAGEGQG TRWSSRGEAT YTLERVDDAP QGTSVTLHLK
PADPENQLHD YTSEWKIREI VKRYSDFITW PIRMVPETGD GEDAPEPQTL NSMKALWARS
REEVSDDEYH ELYKHISHDW REPLETIRLQ AEGTFEYQAL LFIPSHAPHD LFTRDFKRGV
QLYVKRVFIM DDCEALLPPY LRFVKGVVDA QDLSLNVSRE ILQQDRHIRM MQRRLTKKVL
STVKEIMTKD AERYATLWRE FGTVLKEGLV TDSDNRDALL AVASFATTHG EEPTTLAQYV
ERMKDGQEDI YYLTGESRQS IENSPHMEAF RAKGIEVLLL TDAVDEVWVD AVGEYEGKKL
RSVAKGEIDL DAEGTEKAGE EREKQTEEYS GLLGWMREQL DEEIKEVRLS TRLTVSPACV
VSDAHDLTPA LENMYRAMGQ EVPRTKRILE LNPGHPLVKG LNQAYQERAD RTELAESAEL
LHTLAVLAEG GQPKDPAKFV KLVADRLERT L
//
