ID A0A2S4YNA3_9ACTN Unreviewed; 631 AA.
AC A0A2S4YNA3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=C3489_22305 {ECO:0000313|EMBL:POX50385.1};
OS Streptomyces sp. Ru71.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2080746 {ECO:0000313|EMBL:POX50385.1, ECO:0000313|Proteomes:UP000237414};
RN [1] {ECO:0000313|EMBL:POX50385.1, ECO:0000313|Proteomes:UP000237414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru71 {ECO:0000313|EMBL:POX50385.1,
RC ECO:0000313|Proteomes:UP000237414};
RA Suneja G., Sharma R.;
RT "Genome sequencing of cellulose degrading bacteria.";
RL Submitted (FEB-2018) 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:POX50385.1}.
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DR EMBL; PQSS01000039; POX50385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4YNA3; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000237414; 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:UP000237414};
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..337
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 553..631
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 631 AA; 71191 MW; 62F6448257F3C853 CRC64;
MATETFEFQV EARQLLQLMI HSVYSNKDVF LRELVSNASD ALDKLRLAKL RDDTLDADVS
DPHIEIEVDR DARTLTVRDN GIGMSYDEVG RLIGTIANSG TAQFLKELKE AEDEAGAEGL
IGQFGVGFYS GFMVADEMTL LTRRAGESHG TRWSSRGEGT YTLERVDDAP QGTAVTLHLK
PADPDNQLHD YTSEWKIREI VKRYSDFITW PIKLVQPKGD DAPEPETLNS MKALWARSRD
EVSDDEYHEL YKHISHDWRD PLETIRLQAE GTFEYQALLF VPSHAPHDLF TQNHRRGLQL
YVKRVFIMDD CEELLPSYLR FVKGVVDAQD LSLNVSREIL QQDRHIRAMR SRLTKKVLST
VKEMRTKDAE RYATFWREFG AVVKEGLVTD AENRDAILAV ASFASTHGEE EQTTLAAYVE
RMKDGQEDIY YLTGESRQAV ENSPHMEAFR AKGIEVLLLT DPVDEVWVDA VGEFQGKRLR
SVAKGEIDLD GEDEQSTDAE KEKQAETYAG LLGWMKEQLA EDVKEVRLSS RLTVSPACVV
SDAGDLTPAL ENMYRAMGQE VPRAKRILEL NPGHALVQGL NRAYQEAGED RSALTETAEL
LHTLAVLAEG GQPKDPARFV KLVAERLERA L
//
