ID   HTPG_SALTO              Reviewed;         636 AA.
AC   A4X7S0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=Strop_2474;
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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; CP000667; ABP54920.1; -; Genomic_DNA.
DR   RefSeq; WP_012013701.1; NC_009380.1.
DR   AlphaFoldDB; A4X7S0; -.
DR   SMR; A4X7S0; -.
DR   STRING; 369723.Strop_2474; -.
DR   PRIDE; A4X7S0; -.
DR   EnsemblBacteria; ABP54920; ABP54920; Strop_2474.
DR   KEGG; stp:Strop_2474; -.
DR   PATRIC; fig|369723.5.peg.2550; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_11; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000000235; Chromosome.
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:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
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..636
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_1000081525"
FT   REGION          1..342
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          343..558
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          559..636
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   636 AA;  71351 MW;  E0F8BD000730DA84 CRC64;
     MSSETLEFQA EARQLLQLMV HSIYSNKDVF LRELISNASD ALDKLRLASL RDKDLDVDTA
     DLHIAIEIDP DARTLTVRDN GIGMSRDEVV QVIGTIAKSG TAELLRTLRE SADAETSQEL
     IGQFGVGFYA AFMVADRVVL VTREAGATDG TRWESSGEGT YTIASATDAP QGTAVTLHLK
     PADSEDNLHD YATEWTVRQI VKRYSDFIAH PIRMAVEQPG TDGGESTTEV QTLNSMKALW
     ARSRDEVEPA EYHEFYKHVS HDWADPLEVV HMRGEGTFEY EALLFLPTHA PLDLFSPQGR
     RGVQLYVKRV FIMDDCEALM PGYLRFVKGV VDAHDLSLNI SRELLQQDRQ IQVVRRRLVK
     KILATVKELK ANQPEKYRTF WTEFGAVVKE GLIDDTENRD SLLEILSVAS THDPAEPTDL
     ADYVTRMKDG QTDIYYATGE NRSTIENSPH MEAFRAKGFE VLLLTDPVDE VWVERVGEYE
     GKTLRSVAKG QVDLDTEEER SAAEAERERQ RTEYADLLTW LSSTLADQVR EVRLSARLTT
     SPACVVGDAH DVTPTLEKMY RAMGHEVPQV KRILELNPTH PLVSGLRKAR EQGVTEESLK
     ETAELLYGMA LLAEGGELAD PSHFTRILAE RLARTL