HTPG_STRCO
ID HTPG_STRCO Reviewed; 638 AA.
AC P58481;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=SCO7516;
GN ORFNames=SCBAC25F8.08;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000255|HAMAP-Rule:MF_00505}.
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DR EMBL; AL939131; CAC42143.1; -; Genomic_DNA.
DR RefSeq; NP_631561.1; NC_003888.3.
DR RefSeq; WP_003971629.1; NZ_VNID01000005.1.
DR AlphaFoldDB; P58481; -.
DR SMR; P58481; -.
DR STRING; 100226.SCO7516; -.
DR PRIDE; P58481; -.
DR GeneID; 1102954; -.
DR KEGG; sco:SCO7516; -.
DR PATRIC; fig|100226.15.peg.7629; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_11; -.
DR InParanoid; P58481; -.
DR OMA; MRRMKEM; -.
DR PhylomeDB; P58481; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 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_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..638
FT /note="Chaperone protein HtpG"
FT /id="PRO_0000063016"
FT REGION 1..345
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 346..560
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 561..638
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 638 AA; 71628 MW; F7394CAB2931EB30 CRC64;
MTTETFEFQV EARQLLQLMI HSVYSNKDVF LRELVSNASD ALDKLRLAAL RDDAPDADVS
DLHIELEVDK DARTLTVRDN GIGMSYDEVT RLIGTIANSG TAKFLEELRE AKDAAGADGL
IGQFGVGFYS GFMVADEVTL VTRHAGETEG TRWTSRGEGT YTLERIGEAP QGTAVTLHLK
PADVENQLHD YTSAWKIKEI VKRYSDFITW PVRLLPEPGG DGSDGEGAEA REAETLNSMK
ALWARPRDEV SDDEYHELYK HIAHDWRDPL ETIRLQAEGT FEYQALLFVP SHAPHDLFTQ
GYQRGVQLYV KRVFIMDDCE ELLPPHLRFV KGVVDAQDLS LNVSREILQQ DRHIRMIQRR
LTKKVLSTVK DLRTSAPDRY ATFWREFGAV LKEGLVTDSD NRDAILAACS FASTHDAEEP
TALKDYVERM KEGQDDIYYM TGESRQAIEN SPHMEAFRAK GVEVLLLTDA VDEVWVDAVG
EYEGKTLRSV AKGEIDLSGT EADKSDAEKE KQGEEYAGLL GWMTEHLGEE VKEVRLSSRL
TVSPACVVSD AGELTPALEN MYRAMGQEVP GAKRILELNP EHQLVKSLNR AWTDRQDRAE
LTETAELLHA LAVLAEGGRP KEPARFVQLM ADRLERTL
